Compounds > josamycin
Page last updated: 2024-12-10

josamycin

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Cross-References

ID SourceID
PubMed CID5282165
CHEMBL ID224436
CHEBI ID31739
SCHEMBL ID132829
MeSH IDM0023921

Synonyms (71)

Synonym
leucomycin a3
NSC122223 ,
en 141
[(2s,3s,4r,6s)-6-[(2r,3s,4r,5r,6s)-6-[[(4r,5s,6s,7r,9r,10r,11e,13e,16r)-4-acetoxy-10-hydroxy-5-methoxy-9,16-dimethyl-2-oxo-7-(2-oxoethyl)-1-oxacyclohexadeca-11,13-dien-6-yl]oxy]-4-(dimethylamino)-5-hydroxy-2-methyl-tetrahydropyran-3-yl]oxy-4-hydroxy-2,4-d
56689-45-3
6-{6-[3-acetyloxy-13-hydroxy-2-methoxy-7,14-dimethyl-6-oxa-5-oxo-16-(2-oxoethyl)cyclohexadeca-9,11-dienyloxy]-4-(dimethylamino)-5-hydroxy-2-methylperhydro-2h-pyran-3-yloxy}-4-hydroxy-2,4-dimethylperhydro-2h-pyran-3-yl 3-methylbutanoate
josacine
turimycin a5
kitasamycin a3
DB01321
leucomycin v 3-acetate 4b-(3-methylbutanoate)
leucomycin v 3-acetate 4beta-(3-methylbutanoate)
josamycin (jp17/usan/inn)
jm
josamycin (tn)
D01235
leucomycin v, 3-acetate 4(sup beta)-(3-methylbutanoate)
stereoisomer of 7-(formylmethyl)-4,10-dihydroxy-5-methoxy-9,16-dimethyl-2-oxooxacyclohexadeca-11,13-dien-6-yl 3,6-dideoxy-4-o-(2,6-dideoxy-3-c-methyl-alpha-l-ribo-hexopyranosyl)-3-(dimethylamino)-beta-d-glucopyranoside 4'-acetate 4''-isovalerate
antibiotic yl-704 a3
josamicina [inn-spanish]
einecs 240-871-6
yl-704 a3
josamycinum [inn-latin]
stereoisomer of 7-(formylmethyl)-4,10-dihydroxy-5-methoxy-9,16-dimethyl-2-oxooxacyclohexadeca-11,13-dien-6-yl 3,6-dideoxy-4-o-(2,6-dideoxy-3-c-methyl-alpha-l-ribo-hexopyranosyl)-3-(dimethylamino)-beta-d-glucopyranoside 4'-acetate 4'-isovalerate
stereoisomer of 4-(acetyloxy)-6-((3,6-dideoxy-4-o-(2,6-dideoxy-3-c-methyl-4-o-(3-methyl-1-oxobutyl)-alpha-l-ribo-hexopyranosyl)-3-(dimethylamino)-beta-d-glucopyranosyl)oxy)-10-hydroxy-5-methoxy-9,16-dimethyl-2-oxooxacyclohexadeca-11,13-diene-7-acetaldehyd
leucomycin v, 3-acetate 4(sup b)-(3-methylbutanoate)
josamycine [inn-french]
josamycin, >=98.0% (uv)
chebi:31739 ,
jomybel
CHEMBL224436
iosalide
en-141
josamina
[(2s,3s,4r,6s)-6-[(2r,3s,4r,5r,6s)-6-[[(4r,5s,6s,7r,9r,10r,11e,13e,16r)-4-acetyloxy-10-hydroxy-5-methoxy-9,16-dimethyl-2-oxo-7-(2-oxoethyl)-1-oxacyclohexadeca-11,13-dien-6-yl]oxy]-4-(dimethylamino)-5-hydroxy-2-methyloxan-3-yl]oxy-4-hydroxy-2,4-dimethyloxa
josamycin [usan:inn:ban:jan]
hv13hfs217 ,
ccris 8511
unii-hv13hfs217
ST075007
leucomycin v 3-acetate 4(beta)-(3-methylbutanoate)
josamycine
josamycinum
josamicina
S4421
leucomycin v 3-acetate 4(b)-(3-methylbutanoate)
SCHEMBL132829
josamycin [who-dd]
josamycin [inn]
josamycin [mart.]
josamycin [usan]
josamycin [mi]
josamycin [jan]
leucomycin v, 3-acetate 4(sup .beta.)-(3-methylbutanoate)
josamycin [ep monograph]
XJSFLOJWULLJQS-NGVXBBESSA-N
mfcd00210320
(2s,3s,4r,6s)-6-{[(2r,3s,4r,5r,6s)-6-{[(4r,5s,6s,7r,9r,10r,11e,13e,16r)-4-(acetyloxy)-10-hydroxy-5-methoxy-9,16-dimethyl-2-oxo-7-(2-oxoethyl)-1-oxacyclohexadeca-11,13-dien-6-yl]oxy}-4-(dimethylamino)-5-hydroxy-2-methyloxan-3-yl]oxy}-4-hydroxy-2,4-dimethyl
sr-01000883731
SR-01000883731-1
josamycin for peak identification, european pharmacopoeia (ep) reference standard
josamycin, european pharmacopoeia (ep) reference standard
josamycin; (4r,5s,6s,7r,9r,10r,11e,13e,16r)-4-(acetyloxy)-6-[[3,6-dideoxy-4-o-[2,6-dideoxy-3-c-methyl-4-o-(3-methylbutanoyl)-a-l-ribo-hexopyranosyl]-3-(dimethylamino)-ss-d-glucopyranosyl]oxy]-10-hydroxy-5-methoxy-9,16-dimethyl-7-(2-oxoethyl)oxacyclohexade
josamycin 10 microg/ml in acetonitrile
HY-B1920
CS-0013975
Q423369
[(2s,3s,4r,6s)-6-[(2r,3s,4r,5r,6s)-6-[[(4r,5s,6s,7r,9r,10r,11e,13e,16r)-4-acetyloxy-10-hydroxy-5-methoxy-9,16-dimethyl-2-oxo-7-(2-oxoethyl)-1-oxacyclohexadeca-11,13-dien-6-yl]oxy]-4-(dimethylamino)-5-
hydroxy-2-methyloxan-3-yl]oxy-4-hydroxy-2,4-dimethyloxan-3-yl] 3-methylbutanoate
josamycin 1000 microg/ml in acetonitrile
en-141;kitasamycin a3;leucomycin a3;turimycin a5
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Roles (2)

RoleDescription
antibacterial drugA drug used to treat or prevent bacterial infections.
metaboliteAny intermediate or product resulting from metabolism. The term 'metabolite' subsumes the classes commonly known as primary and secondary metabolites.
[role information is derived from Chemical Entities of Biological Interest (ChEBI), Hastings J, Owen G, Dekker A, Ennis M, Kale N, Muthukrishnan V, Turner S, Swainston N, Mendes P, Steinbeck C. (2016). ChEBI in 2016: Improved services and an expanding collection of metabolites. Nucleic Acids Res]

Drug Classes (7)

ClassDescription
macrolide antibioticA macrocyclic lactone with a ring of twelve or more members which exhibits antibiotic activity.
aldehydeA compound RC(=O)H, in which a carbonyl group is bonded to one hydrogen atom and to one R group.
tertiary amino compoundA compound formally derived from ammonia by replacing three hydrogen atoms by organyl groups.
tertiary alcoholA tertiary alcohol is a compound in which a hydroxy group, -OH, is attached to a saturated carbon atom which has three other carbon atoms attached to it.
acetate esterAny carboxylic ester where the carboxylic acid component is acetic acid.
disaccharide derivativeA carbohydrate derivative that is formally obtained from a disaccharide.
glycosideA glycosyl compound resulting from the attachment of a glycosyl group to a non-acyl group RO-, RS-, RSe-, etc. The bond between the glycosyl group and the non-acyl group is called a glycosidic bond. By extension, the terms N-glycosides and C-glycosides are used as class names for glycosylamines and for compounds having a glycosyl group attached to a hydrocarbyl group respectively. These terms are misnomers and should not be used. The preferred terms are glycosylamines and C-glycosyl compounds, respectively.
[compound class information is derived from Chemical Entities of Biological Interest (ChEBI), Hastings J, Owen G, Dekker A, Ennis M, Kale N, Muthukrishnan V, Turner S, Swainston N, Mendes P, Steinbeck C. (2016). ChEBI in 2016: Improved services and an expanding collection of metabolites. Nucleic Acids Res]

Protein Targets (55)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
30S ribosomal protein S6Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S7Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L15Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L10Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L11Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L7/L12Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L19Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L1Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L20Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L27Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L28Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L29Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L31Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L31 type BEscherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L32Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L33Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L34Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L35Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L36Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S10Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S11Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S12Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S13Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S16Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S18Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S19Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S20Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S2Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S3Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S4Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S5Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S8Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S9Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L13Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L14Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L16Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L23Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S15Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L17Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L21Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L30Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L6Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S14Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S17Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S1Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L18Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L2Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L3Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L24Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L4Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L22Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L5Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
30S ribosomal protein S21Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L25Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
50S ribosomal protein L36 2Escherichia coli K-12IC50 (µMol)1.20000.00891.20355.0000AID1137040
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (37)

Processvia Protein(s)Taxonomy
cytoplasmic translation30S ribosomal protein S6Escherichia coli K-12
translation30S ribosomal protein S6Escherichia coli K-12
ribosomal small subunit assembly30S ribosomal protein S7Escherichia coli K-12
negative regulation of translation30S ribosomal protein S7Escherichia coli K-12
ribosomal small subunit assembly30S ribosomal protein S7Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S7Escherichia coli K-12
translation30S ribosomal protein S7Escherichia coli K-12
negative regulation of translation30S ribosomal protein S7Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L15Escherichia coli K-12
translation50S ribosomal protein L15Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L10Escherichia coli K-12
translation50S ribosomal protein L10Escherichia coli K-12
regulation of translation50S ribosomal protein L10Escherichia coli K-12
negative regulation of translation50S ribosomal protein L10Escherichia coli K-12
translation50S ribosomal protein L11Escherichia coli K-12
translational termination50S ribosomal protein L11Escherichia coli K-12
stringent response50S ribosomal protein L11Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L11Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L11Escherichia coli K-12
translation50S ribosomal protein L11Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L7/L12Escherichia coli K-12
translation50S ribosomal protein L7/L12Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L19Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L19Escherichia coli K-12
translation50S ribosomal protein L19Escherichia coli K-12
negative regulation of translational initiation50S ribosomal protein L1Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L1Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L1Escherichia coli K-12
translation50S ribosomal protein L1Escherichia coli K-12
regulation of translation50S ribosomal protein L1Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L20Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L20Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L20Escherichia coli K-12
translation50S ribosomal protein L20Escherichia coli K-12
negative regulation of translation50S ribosomal protein L20Escherichia coli K-12
cytosolic ribosome assembly50S ribosomal protein L27Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L27Escherichia coli K-12
regulation of cell growth50S ribosomal protein L27Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L27Escherichia coli K-12
translation50S ribosomal protein L27Escherichia coli K-12
positive regulation of ribosome biogenesis50S ribosomal protein L27Escherichia coli K-12
assembly of large subunit precursor of preribosome50S ribosomal protein L27Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L28Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L28Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L28Escherichia coli K-12
translation50S ribosomal protein L28Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L29Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L29Escherichia coli K-12
translation50S ribosomal protein L29Escherichia coli K-12
translation50S ribosomal protein L31Escherichia coli K-12
translational initiation50S ribosomal protein L31Escherichia coli K-12
negative regulation of cytoplasmic translational initiation50S ribosomal protein L31Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L31Escherichia coli K-12
translation50S ribosomal protein L31Escherichia coli K-12
cellular response to zinc ion starvation50S ribosomal protein L31 type BEscherichia coli K-12
cytoplasmic translation50S ribosomal protein L31 type BEscherichia coli K-12
translation50S ribosomal protein L31 type BEscherichia coli K-12
response to reactive oxygen species50S ribosomal protein L32Escherichia coli K-12
response to radiation50S ribosomal protein L32Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L32Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L32Escherichia coli K-12
translation50S ribosomal protein L32Escherichia coli K-12
response to antibiotic50S ribosomal protein L33Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L33Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L33Escherichia coli K-12
translation50S ribosomal protein L33Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L34Escherichia coli K-12
translation50S ribosomal protein L34Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L35Escherichia coli K-12
translation50S ribosomal protein L35Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L36Escherichia coli K-12
translation50S ribosomal protein L36Escherichia coli K-12
transcription antitermination30S ribosomal protein S10Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S10Escherichia coli K-12
translation30S ribosomal protein S10Escherichia coli K-12
transcription antitermination30S ribosomal protein S10Escherichia coli K-12
regulation of DNA-templated transcription elongation30S ribosomal protein S10Escherichia coli K-12
ribosome biogenesis30S ribosomal protein S10Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S11Escherichia coli K-12
translation30S ribosomal protein S11Escherichia coli K-12
Group I intron splicing30S ribosomal protein S12Escherichia coli K-12
positive regulation of RNA splicing30S ribosomal protein S12Escherichia coli K-12
RNA folding30S ribosomal protein S12Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S12Escherichia coli K-12
translation30S ribosomal protein S12Escherichia coli K-12
response to antibiotic30S ribosomal protein S12Escherichia coli K-12
maintenance of translational fidelity30S ribosomal protein S12Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S13Escherichia coli K-12
translation30S ribosomal protein S13Escherichia coli K-12
ribosomal small subunit assembly30S ribosomal protein S16Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S16Escherichia coli K-12
DNA metabolic process30S ribosomal protein S16Escherichia coli K-12
translation30S ribosomal protein S16Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S18Escherichia coli K-12
translation30S ribosomal protein S18Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S19Escherichia coli K-12
translation30S ribosomal protein S19Escherichia coli K-12
ribosomal small subunit assembly30S ribosomal protein S19Escherichia coli K-12
ribosomal small subunit assembly30S ribosomal protein S20Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S20Escherichia coli K-12
translation30S ribosomal protein S20Escherichia coli K-12
ribosomal small subunit assembly30S ribosomal protein S2Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S2Escherichia coli K-12
translation30S ribosomal protein S2Escherichia coli K-12
ribosomal small subunit assembly30S ribosomal protein S3Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S3Escherichia coli K-12
translation30S ribosomal protein S3Escherichia coli K-12
transcription antitermination30S ribosomal protein S4Escherichia coli K-12
negative regulation of translational initiation30S ribosomal protein S4Escherichia coli K-12
maintenance of translational fidelity30S ribosomal protein S4Escherichia coli K-12
ribosomal small subunit assembly30S ribosomal protein S4Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S4Escherichia coli K-12
DNA-templated transcription termination30S ribosomal protein S4Escherichia coli K-12
translation30S ribosomal protein S4Escherichia coli K-12
regulation of translation30S ribosomal protein S4Escherichia coli K-12
transcription antitermination30S ribosomal protein S4Escherichia coli K-12
ribosome biogenesis30S ribosomal protein S4Escherichia coli K-12
response to antibiotic30S ribosomal protein S4Escherichia coli K-12
ribosomal small subunit biogenesis30S ribosomal protein S4Escherichia coli K-12
maintenance of translational fidelity30S ribosomal protein S5Escherichia coli K-12
ribosomal small subunit assembly30S ribosomal protein S5Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S5Escherichia coli K-12
translation30S ribosomal protein S5Escherichia coli K-12
response to antibiotic30S ribosomal protein S5Escherichia coli K-12
regulation of mRNA stability30S ribosomal protein S8Escherichia coli K-12
ribosomal small subunit assembly30S ribosomal protein S8Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S8Escherichia coli K-12
translation30S ribosomal protein S8Escherichia coli K-12
regulation of translation30S ribosomal protein S8Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S9Escherichia coli K-12
translation30S ribosomal protein S9Escherichia coli K-12
negative regulation of translation50S ribosomal protein L13Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L13Escherichia coli K-12
translation50S ribosomal protein L13Escherichia coli K-12
negative regulation of translation50S ribosomal protein L13Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L14Escherichia coli K-12
translation50S ribosomal protein L14Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L16Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L16Escherichia coli K-12
translation50S ribosomal protein L16Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L23Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L23Escherichia coli K-12
translation50S ribosomal protein L23Escherichia coli K-12
translation30S ribosomal protein S15Escherichia coli K-12
ribosomal small subunit assembly30S ribosomal protein S15Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S15Escherichia coli K-12
translation30S ribosomal protein S15Escherichia coli K-12
regulation of translation30S ribosomal protein S15Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L17Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L17Escherichia coli K-12
translation50S ribosomal protein L17Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L21Escherichia coli K-12
translation50S ribosomal protein L21Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L30Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L30Escherichia coli K-12
translation50S ribosomal protein L30Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L6Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L6Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L6Escherichia coli K-12
translation50S ribosomal protein L6Escherichia coli K-12
response to antibiotic50S ribosomal protein L6Escherichia coli K-12
ribosomal small subunit assembly30S ribosomal protein S14Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S14Escherichia coli K-12
translation30S ribosomal protein S14Escherichia coli K-12
response to antibiotic30S ribosomal protein S17Escherichia coli K-12
ribosomal small subunit assembly30S ribosomal protein S17Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S17Escherichia coli K-12
translation30S ribosomal protein S17Escherichia coli K-12
response to antibiotic30S ribosomal protein S17Escherichia coli K-12
translation30S ribosomal protein S1Escherichia coli K-12
RNA secondary structure unwinding30S ribosomal protein S1Escherichia coli K-12
negative regulation of cytoplasmic translation30S ribosomal protein S1Escherichia coli K-12
positive regulation of cytoplasmic translation30S ribosomal protein S1Escherichia coli K-12
ribosomal small subunit assembly30S ribosomal protein S1Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S1Escherichia coli K-12
translation30S ribosomal protein S1Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L18Escherichia coli K-12
translation50S ribosomal protein L18Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L2Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L2Escherichia coli K-12
translation50S ribosomal protein L2Escherichia coli K-12
negative regulation of DNA-templated DNA replication initiation50S ribosomal protein L2Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L3Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L3Escherichia coli K-12
translation50S ribosomal protein L3Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L24Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L24Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L24Escherichia coli K-12
translation50S ribosomal protein L24Escherichia coli K-12
transcriptional attenuation50S ribosomal protein L4Escherichia coli K-12
negative regulation of cytoplasmic translation50S ribosomal protein L4Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L4Escherichia coli K-12
DNA-templated transcription termination50S ribosomal protein L4Escherichia coli K-12
translation50S ribosomal protein L4Escherichia coli K-12
regulation of translation50S ribosomal protein L4Escherichia coli K-12
negative regulation of translation50S ribosomal protein L4Escherichia coli K-12
ribosome assembly50S ribosomal protein L4Escherichia coli K-12
negative regulation of DNA-templated transcription50S ribosomal protein L4Escherichia coli K-12
response to antibiotic50S ribosomal protein L4Escherichia coli K-12
translation50S ribosomal protein L22Escherichia coli K-12
cytosolic ribosome assembly50S ribosomal protein L22Escherichia coli K-12
assembly of large subunit precursor of preribosome50S ribosomal protein L22Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L22Escherichia coli K-12
translation50S ribosomal protein L22Escherichia coli K-12
ribosome assembly50S ribosomal protein L22Escherichia coli K-12
response to antibiotic50S ribosomal protein L22Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L5Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L5Escherichia coli K-12
translation50S ribosomal protein L5Escherichia coli K-12
ribosomal small subunit assembly30S ribosomal protein S21Escherichia coli K-12
cytoplasmic translation30S ribosomal protein S21Escherichia coli K-12
translation30S ribosomal protein S21Escherichia coli K-12
translation50S ribosomal protein L25Escherichia coli K-12
response to radiation50S ribosomal protein L25Escherichia coli K-12
negative regulation of translation50S ribosomal protein L25Escherichia coli K-12
ribosomal large subunit assembly50S ribosomal protein L25Escherichia coli K-12
cytoplasmic translation50S ribosomal protein L25Escherichia coli K-12
translation50S ribosomal protein L25Escherichia coli K-12
translation50S ribosomal protein L36 2Escherichia coli K-12
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (29)

Processvia Protein(s)Taxonomy
structural constituent of ribosome30S ribosomal protein S6Escherichia coli K-12
protein binding30S ribosomal protein S6Escherichia coli K-12
rRNA binding30S ribosomal protein S6Escherichia coli K-12
mRNA 5'-UTR binding30S ribosomal protein S6Escherichia coli K-12
small ribosomal subunit rRNA binding30S ribosomal protein S6Escherichia coli K-12
tRNA binding30S ribosomal protein S7Escherichia coli K-12
RNA binding30S ribosomal protein S7Escherichia coli K-12
mRNA binding30S ribosomal protein S7Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S7Escherichia coli K-12
protein binding30S ribosomal protein S7Escherichia coli K-12
rRNA binding30S ribosomal protein S7Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L15Escherichia coli K-12
protein binding50S ribosomal protein L15Escherichia coli K-12
rRNA binding50S ribosomal protein L15Escherichia coli K-12
GTPase activity50S ribosomal protein L10Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L10Escherichia coli K-12
protein binding50S ribosomal protein L10Escherichia coli K-12
rRNA binding50S ribosomal protein L10Escherichia coli K-12
ribosome binding50S ribosomal protein L10Escherichia coli K-12
large ribosomal subunit rRNA binding50S ribosomal protein L10Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L11Escherichia coli K-12
protein binding50S ribosomal protein L11Escherichia coli K-12
rRNA binding50S ribosomal protein L11Escherichia coli K-12
large ribosomal subunit rRNA binding50S ribosomal protein L11Escherichia coli K-12
GTPase activity50S ribosomal protein L7/L12Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L7/L12Escherichia coli K-12
protein binding50S ribosomal protein L7/L12Escherichia coli K-12
protein homodimerization activity50S ribosomal protein L7/L12Escherichia coli K-12
ribosome binding50S ribosomal protein L7/L12Escherichia coli K-12
mRNA binding50S ribosomal protein L7/L12Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L19Escherichia coli K-12
rRNA binding50S ribosomal protein L19Escherichia coli K-12
large ribosomal subunit rRNA binding50S ribosomal protein L19Escherichia coli K-12
tRNA binding50S ribosomal protein L1Escherichia coli K-12
RNA binding50S ribosomal protein L1Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L1Escherichia coli K-12
protein binding50S ribosomal protein L1Escherichia coli K-12
rRNA binding50S ribosomal protein L1Escherichia coli K-12
mRNA regulatory element binding translation repressor activity50S ribosomal protein L20Escherichia coli K-12
mRNA binding50S ribosomal protein L20Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L20Escherichia coli K-12
rRNA binding50S ribosomal protein L20Escherichia coli K-12
large ribosomal subunit rRNA binding50S ribosomal protein L20Escherichia coli K-12
tRNA binding50S ribosomal protein L27Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L27Escherichia coli K-12
protein binding50S ribosomal protein L27Escherichia coli K-12
rRNA binding50S ribosomal protein L27Escherichia coli K-12
ribosome binding50S ribosomal protein L27Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L28Escherichia coli K-12
protein binding50S ribosomal protein L28Escherichia coli K-12
rRNA binding50S ribosomal protein L28Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L29Escherichia coli K-12
rRNA binding50S ribosomal protein L29Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L31Escherichia coli K-12
zinc ion binding50S ribosomal protein L31Escherichia coli K-12
rRNA binding50S ribosomal protein L31Escherichia coli K-12
metal ion binding50S ribosomal protein L31Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L31 type BEscherichia coli K-12
structural constituent of ribosome50S ribosomal protein L32Escherichia coli K-12
protein binding50S ribosomal protein L32Escherichia coli K-12
tRNA binding50S ribosomal protein L33Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L33Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L34Escherichia coli K-12
protein binding50S ribosomal protein L34Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L35Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L36Escherichia coli K-12
tRNA binding30S ribosomal protein S10Escherichia coli K-12
transcription antitermination factor activity, RNA binding30S ribosomal protein S10Escherichia coli K-12
RNA binding30S ribosomal protein S10Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S10Escherichia coli K-12
protein binding30S ribosomal protein S10Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S11Escherichia coli K-12
protein binding30S ribosomal protein S11Escherichia coli K-12
rRNA binding30S ribosomal protein S11Escherichia coli K-12
small ribosomal subunit rRNA binding30S ribosomal protein S11Escherichia coli K-12
tRNA binding30S ribosomal protein S12Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S12Escherichia coli K-12
protein binding30S ribosomal protein S12Escherichia coli K-12
rRNA binding30S ribosomal protein S12Escherichia coli K-12
misfolded RNA binding30S ribosomal protein S12Escherichia coli K-12
tRNA binding30S ribosomal protein S13Escherichia coli K-12
RNA binding30S ribosomal protein S13Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S13Escherichia coli K-12
protein binding30S ribosomal protein S13Escherichia coli K-12
rRNA binding30S ribosomal protein S13Escherichia coli K-12
four-way junction DNA binding30S ribosomal protein S16Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S16Escherichia coli K-12
endonuclease activity30S ribosomal protein S16Escherichia coli K-12
DNA endonuclease activity30S ribosomal protein S16Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S18Escherichia coli K-12
protein binding30S ribosomal protein S18Escherichia coli K-12
rRNA binding30S ribosomal protein S18Escherichia coli K-12
mRNA 5'-UTR binding30S ribosomal protein S18Escherichia coli K-12
small ribosomal subunit rRNA binding30S ribosomal protein S18Escherichia coli K-12
tRNA binding30S ribosomal protein S19Escherichia coli K-12
RNA binding30S ribosomal protein S19Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S19Escherichia coli K-12
rRNA binding30S ribosomal protein S19Escherichia coli K-12
RNA binding30S ribosomal protein S20Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S20Escherichia coli K-12
ornithine decarboxylase inhibitor activity30S ribosomal protein S20Escherichia coli K-12
rRNA binding30S ribosomal protein S20Escherichia coli K-12
small ribosomal subunit rRNA binding30S ribosomal protein S20Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S2Escherichia coli K-12
protein binding30S ribosomal protein S2Escherichia coli K-12
zinc ion binding30S ribosomal protein S2Escherichia coli K-12
RNA binding30S ribosomal protein S3Escherichia coli K-12
mRNA binding30S ribosomal protein S3Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S3Escherichia coli K-12
rRNA binding30S ribosomal protein S3Escherichia coli K-12
mRNA regulatory element binding translation repressor activity30S ribosomal protein S4Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S4Escherichia coli K-12
protein binding30S ribosomal protein S4Escherichia coli K-12
rRNA binding30S ribosomal protein S4Escherichia coli K-12
mRNA 5'-UTR binding30S ribosomal protein S4Escherichia coli K-12
RNA binding30S ribosomal protein S5Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S5Escherichia coli K-12
protein binding30S ribosomal protein S5Escherichia coli K-12
rRNA binding30S ribosomal protein S5Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S8Escherichia coli K-12
rRNA binding30S ribosomal protein S8Escherichia coli K-12
tRNA binding30S ribosomal protein S9Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S9Escherichia coli K-12
RNA binding30S ribosomal protein S9Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L13Escherichia coli K-12
zinc ion binding50S ribosomal protein L13Escherichia coli K-12
mRNA 5'-UTR binding50S ribosomal protein L13Escherichia coli K-12
large ribosomal subunit rRNA binding50S ribosomal protein L13Escherichia coli K-12
mRNA binding50S ribosomal protein L13Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L14Escherichia coli K-12
protein binding50S ribosomal protein L14Escherichia coli K-12
rRNA binding50S ribosomal protein L14Escherichia coli K-12
large ribosomal subunit rRNA binding50S ribosomal protein L14Escherichia coli K-12
tRNA binding50S ribosomal protein L16Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L16Escherichia coli K-12
rRNA binding50S ribosomal protein L16Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L23Escherichia coli K-12
protein binding50S ribosomal protein L23Escherichia coli K-12
rRNA binding50S ribosomal protein L23Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S15Escherichia coli K-12
rRNA binding30S ribosomal protein S15Escherichia coli K-12
small ribosomal subunit rRNA binding30S ribosomal protein S15Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L17Escherichia coli K-12
protein binding50S ribosomal protein L17Escherichia coli K-12
RNA binding50S ribosomal protein L21Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L21Escherichia coli K-12
rRNA binding50S ribosomal protein L21Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L30Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L6Escherichia coli K-12
rRNA binding50S ribosomal protein L6Escherichia coli K-12
large ribosomal subunit rRNA binding50S ribosomal protein L6Escherichia coli K-12
tRNA binding30S ribosomal protein S14Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S14Escherichia coli K-12
rRNA binding30S ribosomal protein S14Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S17Escherichia coli K-12
zinc ion binding30S ribosomal protein S17Escherichia coli K-12
rRNA binding30S ribosomal protein S17Escherichia coli K-12
molecular adaptor activity30S ribosomal protein S17Escherichia coli K-12
small ribosomal subunit rRNA binding30S ribosomal protein S17Escherichia coli K-12
RNA binding30S ribosomal protein S1Escherichia coli K-12
single-stranded RNA binding30S ribosomal protein S1Escherichia coli K-12
mRNA binding30S ribosomal protein S1Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S1Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L18Escherichia coli K-12
5S rRNA binding50S ribosomal protein L18Escherichia coli K-12
rRNA binding50S ribosomal protein L18Escherichia coli K-12
RNA binding50S ribosomal protein L2Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L2Escherichia coli K-12
protein binding50S ribosomal protein L2Escherichia coli K-12
zinc ion binding50S ribosomal protein L2Escherichia coli K-12
transferase activity50S ribosomal protein L2Escherichia coli K-12
rRNA binding50S ribosomal protein L2Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L3Escherichia coli K-12
protein binding50S ribosomal protein L3Escherichia coli K-12
rRNA binding50S ribosomal protein L3Escherichia coli K-12
RNA binding50S ribosomal protein L24Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L24Escherichia coli K-12
protein binding50S ribosomal protein L24Escherichia coli K-12
rRNA binding50S ribosomal protein L24Escherichia coli K-12
large ribosomal subunit rRNA binding50S ribosomal protein L24Escherichia coli K-12
RNA-binding transcription regulator activity50S ribosomal protein L4Escherichia coli K-12
DNA binding50S ribosomal protein L4Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L4Escherichia coli K-12
protein binding50S ribosomal protein L4Escherichia coli K-12
rRNA binding50S ribosomal protein L4Escherichia coli K-12
translation repressor activity50S ribosomal protein L4Escherichia coli K-12
mRNA 5'-UTR binding50S ribosomal protein L4Escherichia coli K-12
endoribonuclease inhibitor activity50S ribosomal protein L4Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L22Escherichia coli K-12
protein binding50S ribosomal protein L22Escherichia coli K-12
rRNA binding50S ribosomal protein L22Escherichia coli K-12
large ribosomal subunit rRNA binding50S ribosomal protein L22Escherichia coli K-12
tRNA binding50S ribosomal protein L5Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L5Escherichia coli K-12
5S rRNA binding50S ribosomal protein L5Escherichia coli K-12
rRNA binding50S ribosomal protein L5Escherichia coli K-12
RNA binding50S ribosomal protein L5Escherichia coli K-12
structural constituent of ribosome30S ribosomal protein S21Escherichia coli K-12
rRNA binding30S ribosomal protein S21Escherichia coli K-12
RNA binding50S ribosomal protein L25Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L25Escherichia coli K-12
5S rRNA binding50S ribosomal protein L25Escherichia coli K-12
rRNA binding50S ribosomal protein L25Escherichia coli K-12
structural constituent of ribosome50S ribosomal protein L36 2Escherichia coli K-12
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (12)

Processvia Protein(s)Taxonomy
cytoplasm30S ribosomal protein S6Escherichia coli K-12
cytosol30S ribosomal protein S6Escherichia coli K-12
ribosome30S ribosomal protein S6Escherichia coli K-12
intracellular organelle30S ribosomal protein S6Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S6Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S6Escherichia coli K-12
cytosol30S ribosomal protein S7Escherichia coli K-12
ribosome30S ribosomal protein S7Escherichia coli K-12
membrane30S ribosomal protein S7Escherichia coli K-12
cytoplasm30S ribosomal protein S7Escherichia coli K-12
small ribosomal subunit30S ribosomal protein S7Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S7Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S7Escherichia coli K-12
ribosome30S ribosomal protein S7Escherichia coli K-12
ribosome50S ribosomal protein L15Escherichia coli K-12
cytoplasm50S ribosomal protein L15Escherichia coli K-12
large ribosomal subunit50S ribosomal protein L15Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L15Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L15Escherichia coli K-12
cytosol50S ribosomal protein L10Escherichia coli K-12
ribosome50S ribosomal protein L10Escherichia coli K-12
cytoplasm50S ribosomal protein L10Escherichia coli K-12
large ribosomal subunit50S ribosomal protein L10Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L10Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L10Escherichia coli K-12
cytosol50S ribosomal protein L11Escherichia coli K-12
ribosome50S ribosomal protein L11Escherichia coli K-12
cytoplasm50S ribosomal protein L11Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L11Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L11Escherichia coli K-12
cytoplasm50S ribosomal protein L7/L12Escherichia coli K-12
cytosol50S ribosomal protein L7/L12Escherichia coli K-12
ribosome50S ribosomal protein L7/L12Escherichia coli K-12
large ribosomal subunit50S ribosomal protein L7/L12Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L7/L12Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L7/L12Escherichia coli K-12
cytosol50S ribosomal protein L19Escherichia coli K-12
ribosome50S ribosomal protein L19Escherichia coli K-12
cytoplasm50S ribosomal protein L19Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L19Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L19Escherichia coli K-12
cytosol50S ribosomal protein L1Escherichia coli K-12
ribosome50S ribosomal protein L1Escherichia coli K-12
cytoplasm50S ribosomal protein L1Escherichia coli K-12
large ribosomal subunit50S ribosomal protein L1Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L1Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L1Escherichia coli K-12
cytosol50S ribosomal protein L20Escherichia coli K-12
ribosome50S ribosomal protein L20Escherichia coli K-12
cytoplasm50S ribosomal protein L20Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L20Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L20Escherichia coli K-12
ribosome50S ribosomal protein L27Escherichia coli K-12
cytoplasm50S ribosomal protein L27Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L27Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L27Escherichia coli K-12
cytosol50S ribosomal protein L28Escherichia coli K-12
ribosome50S ribosomal protein L28Escherichia coli K-12
cytoplasm50S ribosomal protein L28Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L28Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L28Escherichia coli K-12
ribosome50S ribosomal protein L29Escherichia coli K-12
cytoplasm50S ribosomal protein L29Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L29Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L29Escherichia coli K-12
cytosol50S ribosomal protein L31Escherichia coli K-12
ribosome50S ribosomal protein L31Escherichia coli K-12
cytoplasm50S ribosomal protein L31Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L31Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L31Escherichia coli K-12
ribosome50S ribosomal protein L31 type BEscherichia coli K-12
cytoplasm50S ribosomal protein L31 type BEscherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L31 type BEscherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L31 type BEscherichia coli K-12
cytosol50S ribosomal protein L32Escherichia coli K-12
ribosome50S ribosomal protein L32Escherichia coli K-12
cytoplasm50S ribosomal protein L32Escherichia coli K-12
large ribosomal subunit50S ribosomal protein L32Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L32Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L32Escherichia coli K-12
cytoplasm50S ribosomal protein L33Escherichia coli K-12
cytosol50S ribosomal protein L33Escherichia coli K-12
ribosome50S ribosomal protein L33Escherichia coli K-12
intracellular organelle50S ribosomal protein L33Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L33Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L33Escherichia coli K-12
ribosome50S ribosomal protein L34Escherichia coli K-12
cytoplasm50S ribosomal protein L34Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L34Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L34Escherichia coli K-12
ribosome50S ribosomal protein L35Escherichia coli K-12
cytoplasm50S ribosomal protein L35Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L35Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L35Escherichia coli K-12
cytoplasm50S ribosomal protein L36Escherichia coli K-12
ribosome50S ribosomal protein L36Escherichia coli K-12
intracellular organelle50S ribosomal protein L36Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L36Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L36Escherichia coli K-12
cytosol30S ribosomal protein S10Escherichia coli K-12
ribosome30S ribosomal protein S10Escherichia coli K-12
cytoplasm30S ribosomal protein S10Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S10Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S10Escherichia coli K-12
small ribosomal subunit30S ribosomal protein S10Escherichia coli K-12
cytosol30S ribosomal protein S11Escherichia coli K-12
ribosome30S ribosomal protein S11Escherichia coli K-12
cytoplasm30S ribosomal protein S11Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S11Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S11Escherichia coli K-12
cytosol30S ribosomal protein S12Escherichia coli K-12
ribosome30S ribosomal protein S12Escherichia coli K-12
cytoplasm30S ribosomal protein S12Escherichia coli K-12
small ribosomal subunit30S ribosomal protein S12Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S12Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S12Escherichia coli K-12
ribosome30S ribosomal protein S12Escherichia coli K-12
cytosol30S ribosomal protein S13Escherichia coli K-12
ribosome30S ribosomal protein S13Escherichia coli K-12
cytoplasm30S ribosomal protein S13Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S13Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S13Escherichia coli K-12
small ribosomal subunit30S ribosomal protein S13Escherichia coli K-12
cytosol30S ribosomal protein S13Escherichia coli K-12
cytoplasm30S ribosomal protein S16Escherichia coli K-12
ribosome30S ribosomal protein S16Escherichia coli K-12
intracellular organelle30S ribosomal protein S16Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S16Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S16Escherichia coli K-12
small ribosomal subunit30S ribosomal protein S16Escherichia coli K-12
cytosol30S ribosomal protein S18Escherichia coli K-12
ribosome30S ribosomal protein S18Escherichia coli K-12
cytoplasm30S ribosomal protein S18Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S18Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S18Escherichia coli K-12
cytoplasm30S ribosomal protein S19Escherichia coli K-12
cytosol30S ribosomal protein S19Escherichia coli K-12
ribosome30S ribosomal protein S19Escherichia coli K-12
intracellular organelle30S ribosomal protein S19Escherichia coli K-12
small ribosomal subunit30S ribosomal protein S19Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S19Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S19Escherichia coli K-12
cytosol30S ribosomal protein S20Escherichia coli K-12
ribosome30S ribosomal protein S20Escherichia coli K-12
cytoplasm30S ribosomal protein S20Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S20Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S20Escherichia coli K-12
small ribosomal subunit30S ribosomal protein S20Escherichia coli K-12
cytosol30S ribosomal protein S20Escherichia coli K-12
ribosome30S ribosomal protein S2Escherichia coli K-12
cytoplasm30S ribosomal protein S2Escherichia coli K-12
small ribosomal subunit30S ribosomal protein S2Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S2Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S2Escherichia coli K-12
cytosol30S ribosomal protein S3Escherichia coli K-12
ribosome30S ribosomal protein S3Escherichia coli K-12
cytoplasm30S ribosomal protein S3Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S3Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S3Escherichia coli K-12
cytosol30S ribosomal protein S4Escherichia coli K-12
ribosome30S ribosomal protein S4Escherichia coli K-12
cytoplasm30S ribosomal protein S4Escherichia coli K-12
small ribosomal subunit30S ribosomal protein S4Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S4Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S4Escherichia coli K-12
cytoplasm30S ribosomal protein S5Escherichia coli K-12
cytosol30S ribosomal protein S5Escherichia coli K-12
ribosome30S ribosomal protein S5Escherichia coli K-12
intracellular organelle30S ribosomal protein S5Escherichia coli K-12
small ribosomal subunit30S ribosomal protein S5Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S5Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S5Escherichia coli K-12
cytoplasm30S ribosomal protein S8Escherichia coli K-12
cytosol30S ribosomal protein S8Escherichia coli K-12
ribosome30S ribosomal protein S8Escherichia coli K-12
intracellular organelle30S ribosomal protein S8Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S8Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S8Escherichia coli K-12
cytosol30S ribosomal protein S9Escherichia coli K-12
ribosome30S ribosomal protein S9Escherichia coli K-12
intracellular organelle30S ribosomal protein S9Escherichia coli K-12
cytoplasm30S ribosomal protein S9Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S9Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S9Escherichia coli K-12
cytoplasm50S ribosomal protein L13Escherichia coli K-12
cytosol50S ribosomal protein L13Escherichia coli K-12
ribosome50S ribosomal protein L13Escherichia coli K-12
intracellular organelle50S ribosomal protein L13Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L13Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L13Escherichia coli K-12
ribosome50S ribosomal protein L13Escherichia coli K-12
cytosol50S ribosomal protein L14Escherichia coli K-12
ribosome50S ribosomal protein L14Escherichia coli K-12
cytoplasm50S ribosomal protein L14Escherichia coli K-12
large ribosomal subunit50S ribosomal protein L14Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L14Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L14Escherichia coli K-12
ribosome50S ribosomal protein L16Escherichia coli K-12
cytoplasm50S ribosomal protein L16Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L16Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L16Escherichia coli K-12
ribosome50S ribosomal protein L23Escherichia coli K-12
cytoplasm50S ribosomal protein L23Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L23Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L23Escherichia coli K-12
cytoplasm30S ribosomal protein S15Escherichia coli K-12
cytosol30S ribosomal protein S15Escherichia coli K-12
ribosome30S ribosomal protein S15Escherichia coli K-12
intracellular organelle30S ribosomal protein S15Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S15Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S15Escherichia coli K-12
cytosol50S ribosomal protein L17Escherichia coli K-12
ribosome50S ribosomal protein L17Escherichia coli K-12
cytoplasm50S ribosomal protein L17Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L17Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L17Escherichia coli K-12
cytoplasm50S ribosomal protein L21Escherichia coli K-12
cytosol50S ribosomal protein L21Escherichia coli K-12
ribosome50S ribosomal protein L21Escherichia coli K-12
intracellular organelle50S ribosomal protein L21Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L21Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L21Escherichia coli K-12
ribosome50S ribosomal protein L30Escherichia coli K-12
cytoplasm50S ribosomal protein L30Escherichia coli K-12
large ribosomal subunit50S ribosomal protein L30Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L30Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L30Escherichia coli K-12
cytosol50S ribosomal protein L6Escherichia coli K-12
ribosome50S ribosomal protein L6Escherichia coli K-12
cytoplasm50S ribosomal protein L6Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L6Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L6Escherichia coli K-12
cytoplasm30S ribosomal protein S14Escherichia coli K-12
ribosome30S ribosomal protein S14Escherichia coli K-12
intracellular organelle30S ribosomal protein S14Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S14Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S14Escherichia coli K-12
small ribosomal subunit30S ribosomal protein S14Escherichia coli K-12
ribosome30S ribosomal protein S17Escherichia coli K-12
cytoplasm30S ribosomal protein S17Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S17Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S17Escherichia coli K-12
cytoplasm30S ribosomal protein S1Escherichia coli K-12
ribosome30S ribosomal protein S1Escherichia coli K-12
membrane30S ribosomal protein S1Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S1Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S1Escherichia coli K-12
cytoplasm50S ribosomal protein L18Escherichia coli K-12
cytosol50S ribosomal protein L18Escherichia coli K-12
ribosome50S ribosomal protein L18Escherichia coli K-12
intracellular organelle50S ribosomal protein L18Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L18Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L18Escherichia coli K-12
cytosol50S ribosomal protein L2Escherichia coli K-12
ribosome50S ribosomal protein L2Escherichia coli K-12
cytoplasm50S ribosomal protein L2Escherichia coli K-12
large ribosomal subunit50S ribosomal protein L2Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L2Escherichia coli K-12
DnaA-L2 complex50S ribosomal protein L2Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L2Escherichia coli K-12
cytosol50S ribosomal protein L3Escherichia coli K-12
ribosome50S ribosomal protein L3Escherichia coli K-12
cytoplasm50S ribosomal protein L3Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L3Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L3Escherichia coli K-12
cytosol50S ribosomal protein L24Escherichia coli K-12
ribosome50S ribosomal protein L24Escherichia coli K-12
cytoplasm50S ribosomal protein L24Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L24Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L24Escherichia coli K-12
cytosol50S ribosomal protein L4Escherichia coli K-12
ribosome50S ribosomal protein L4Escherichia coli K-12
cytoplasm50S ribosomal protein L4Escherichia coli K-12
large ribosomal subunit50S ribosomal protein L4Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L4Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L4Escherichia coli K-12
cytosol50S ribosomal protein L22Escherichia coli K-12
ribosome50S ribosomal protein L22Escherichia coli K-12
cytoplasm50S ribosomal protein L22Escherichia coli K-12
large ribosomal subunit50S ribosomal protein L22Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L22Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L22Escherichia coli K-12
cytosol50S ribosomal protein L5Escherichia coli K-12
ribosome50S ribosomal protein L5Escherichia coli K-12
cytoplasm50S ribosomal protein L5Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L5Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L5Escherichia coli K-12
cytosol30S ribosomal protein S21Escherichia coli K-12
ribosome30S ribosomal protein S21Escherichia coli K-12
cytoplasm30S ribosomal protein S21Escherichia coli K-12
cytosolic small ribosomal subunit30S ribosomal protein S21Escherichia coli K-12
ribonucleoprotein complex30S ribosomal protein S21Escherichia coli K-12
cytosol50S ribosomal protein L25Escherichia coli K-12
ribosome50S ribosomal protein L25Escherichia coli K-12
cytoplasm50S ribosomal protein L25Escherichia coli K-12
cytosolic large ribosomal subunit50S ribosomal protein L25Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L25Escherichia coli K-12
ribosome50S ribosomal protein L36 2Escherichia coli K-12
cytosolic ribosome50S ribosomal protein L36 2Escherichia coli K-12
ribonucleoprotein complex50S ribosomal protein L36 2Escherichia coli K-12
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (85)

Assay IDTitleYearJournalArticle
AID1079940Granulomatous liver disease, proven histopathologically. Value is number of references indexed. [column 'GRAN' in source]
AID283577Reduction of NF-kappaB binding to DNA in cystic fibrosis IB3-1 cells at 8 ug after 24 hrs2007Antimicrobial agents and chemotherapy, Mar, Volume: 51, Issue:3
Azithromycin selectively reduces tumor necrosis factor alpha levels in cystic fibrosis airway epithelial cells.
AID283578Reduction of NF-kappaB binding to DNA in cystic fibrosis 16HBE14o-AS3 cells at 8 ug after 24 hrs2007Antimicrobial agents and chemotherapy, Mar, Volume: 51, Issue:3
Azithromycin selectively reduces tumor necrosis factor alpha levels in cystic fibrosis airway epithelial cells.
AID1064175Antimicrobial activity against methicillin-sensitive Staphylococcus epidermidis ATCC 12228 by broth microdilution method2014Bioorganic & medicinal chemistry letters, Jan-15, Volume: 24, Issue:2
Synthesis and antibacterial activity of a series of novel 9-O-acetyl- 4'-substituted 16-membered macrolides derived from josamycin.
AID556348Antimicrobial activity against macrolide-resistant Mycoplasma pneumoniae clinical isolates obtained from bronchial aspirations expressing 23S rRNA A2063G mutant gene and P1 RFLP type I gene by broth microdilution method2009Antimicrobial agents and chemotherapy, May, Volume: 53, Issue:5
Antimicrobial susceptibility of Mycoplasma pneumoniae isolates and molecular analysis of macrolide-resistant strains from Shanghai, China.
AID1137040Displacement of [14C]erythromycin from Escherichia coli ribosomes after 30 mins by scintillation spectrometer analysis1977Journal of medicinal chemistry, May, Volume: 20, Issue:5
Structure-activity relationships among the O-acyl derivatives of leucomycin. Correlation of minimal inhibitory concentrations with binding to Escherichia coli ribosomes.
AID423272Antibacterial activity against 0.01 MOI wild type Chlamydia trachomatis L2/LGV/434/Bu infected in mouse L2 cells treated 2 hrs after infection measured on day 7 by plaque assay2007Antimicrobial agents and chemotherapy, Dec, Volume: 51, Issue:12
Frequency of development and associated physiological cost of azithromycin resistance in Chlamydia psittaci 6BC and C. trachomatis L2.
AID1079937Severe hepatitis, defined as possibly life-threatening liver failure or through clinical observations. Value is number of references indexed. [column 'MASS' in source]
AID369233Antibacterial activity against macrolide-resistant Streptococcus pneumoniae isolates by double-disk diffusion method2007Antimicrobial agents and chemotherapy, Sep, Volume: 51, Issue:9
Serotypes, Clones, and Mechanisms of Resistance of Erythromycin-Resistant Streptococcus pneumoniae Isolates Collected in Spain.
AID1064178Antimicrobial activity against methicillin-sensitive Staphylococcus aureus 15 by broth microdilution method2014Bioorganic & medicinal chemistry letters, Jan-15, Volume: 24, Issue:2
Synthesis and antibacterial activity of a series of novel 9-O-acetyl- 4'-substituted 16-membered macrolides derived from josamycin.
AID422942Antimicrobial activity against macrolide-susceptible Mycoplasma pneumoniae isolated from pediatric patients with community-acquired pneumonia after 10 to 14 days by microdilution method2008Antimicrobial agents and chemotherapy, Jan, Volume: 52, Issue:1
Increased macrolide resistance of Mycoplasma pneumoniae in pediatric patients with community-acquired pneumonia.
AID1064177Antimicrobial activity against methicillin-sensitive Staphylococcus aureus 09-6 by broth microdilution method2014Bioorganic & medicinal chemistry letters, Jan-15, Volume: 24, Issue:2
Synthesis and antibacterial activity of a series of novel 9-O-acetyl- 4'-substituted 16-membered macrolides derived from josamycin.
AID556350Antimicrobial activity against Mycoplasma pneumoniae clinical isolate harboring point mutations in 23S rRNA at positions 2063 and 2064 isolated from human respiratory tract by microdilution method2009Antimicrobial agents and chemotherapy, May, Volume: 53, Issue:5
Molecular mechanisms of macrolide resistance in clinical isolates of Mycoplasma pneumoniae from China.
AID283582Reduction of Sp1 binding to DNA in cystic fibrosis 2CFSMEo cells at 8 ug after 24 hrs2007Antimicrobial agents and chemotherapy, Mar, Volume: 51, Issue:3
Azithromycin selectively reduces tumor necrosis factor alpha levels in cystic fibrosis airway epithelial cells.
AID1079936Choleostatic liver toxicity, either proven histopathologically or where the ratio of maximal ALT or AST activity above normal to that of Alkaline Phosphatase is < 2 (see ACUTE). Value is number of references indexed. [column 'CHOLE' in source]
AID1079942Steatosis, proven histopathologically. Value is number of references indexed. [column 'STEAT' in source]
AID1137039Antimicrobial activity against Klebsiella pneumoniae ATCC 10031 by agar dilution method1977Journal of medicinal chemistry, May, Volume: 20, Issue:5
Structure-activity relationships among the O-acyl derivatives of leucomycin. Correlation of minimal inhibitory concentrations with binding to Escherichia coli ribosomes.
AID369227Antibacterial activity against erythromycin-resistant Streptococcus pneumoniae by microdilution method2007Antimicrobial agents and chemotherapy, Sep, Volume: 51, Issue:9
Serotypes, Clones, and Mechanisms of Resistance of Erythromycin-Resistant Streptococcus pneumoniae Isolates Collected in Spain.
AID1064173Antimicrobial activity against methicillin-sensitive Staphylococcus epidermidis 09-9 by broth microdilution method2014Bioorganic & medicinal chemistry letters, Jan-15, Volume: 24, Issue:2
Synthesis and antibacterial activity of a series of novel 9-O-acetyl- 4'-substituted 16-membered macrolides derived from josamycin.
AID423273Antibacterial activity against azithromycin-tolerant 0.01 MOI Chlamydia trachomatis L2AZM#23 harboring mutation in bacterial ribosomal protein L4 infected in mouse L2 cells treated 2 hrs after infection measured on day 7 by plaque assay2007Antimicrobial agents and chemotherapy, Dec, Volume: 51, Issue:12
Frequency of development and associated physiological cost of azithromycin resistance in Chlamydia psittaci 6BC and C. trachomatis L2.
AID369228Antibacterial activity against erythromycin-resistant Streptococcus pneumoniae assessed as percent resistant isolates by microdilution method2007Antimicrobial agents and chemotherapy, Sep, Volume: 51, Issue:9
Serotypes, Clones, and Mechanisms of Resistance of Erythromycin-Resistant Streptococcus pneumoniae Isolates Collected in Spain.
AID1079946Presence of at least one case with successful reintroduction. [column 'REINT' in source]
AID529868Antimicrobial activity against Escherichia coli AG100A harboring pAT392 containing rdmC-like gene by broth microdilution method2008Antimicrobial agents and chemotherapy, Aug, Volume: 52, Issue:8
Emergence of macrolide resistance gene mph(B) in Streptococcus uberis and cooperative effects with rdmC-like gene.
AID283558Antibacterial activity against Escherichia coli AG102 with marR1 mutation after 24 hrs2007Antimicrobial agents and chemotherapy, Mar, Volume: 51, Issue:3
Substrate competition studies using whole-cell accumulation assays with the major tripartite multidrug efflux pumps of Escherichia coli.
AID1079939Cirrhosis, proven histopathologically. Value is number of references indexed. [column 'CIRRH' in source]
AID1079944Benign tumor, proven histopathologically. Value is number of references indexed. [column 'T.BEN' in source]
AID423274Antibacterial activity against azithromycin-tolerant 0.01 MOI Chlamydia trachomatis L2AZM#31 harboring mutation in bacterial ribosomal protein L4 infected in mouse L2 cells treated 2 hrs after infection measured on day 7 by plaque assay2007Antimicrobial agents and chemotherapy, Dec, Volume: 51, Issue:12
Frequency of development and associated physiological cost of azithromycin resistance in Chlamydia psittaci 6BC and C. trachomatis L2.
AID520741Antimicrobial activity against cfr-deficient Staphylococcus aureus RN4220 harboring erm(B) gene by broth microdilution method2008Antimicrobial agents and chemotherapy, May, Volume: 52, Issue:5
Transcriptional and translational control of the mlr operon, which confers resistance to seven classes of protein synthesis inhibitors.
AID518965Induction of erm(C) expression in Escherichia coli JM109 harboring Staphylococcus aureus erm(C)-containing pERMZalpha reporter plasmid at 10 mg/ml after 36 hrs at 37 degC by disc-based beta-galactosidase reporter gene assay2008Antimicrobial agents and chemotherapy, Mar, Volume: 52, Issue:3
Induction of erm(C) expression by noninducing antibiotics.
AID520740Antimicrobial activity against erm(B)-deficient Staphylococcus aureus RN4220 harboring cfr gene by broth microdilution method2008Antimicrobial agents and chemotherapy, May, Volume: 52, Issue:5
Transcriptional and translational control of the mlr operon, which confers resistance to seven classes of protein synthesis inhibitors.
AID1064174Antimicrobial activity against methicillin-resistant Staphylococcus epidermidis 09-3 by broth microdilution method2014Bioorganic & medicinal chemistry letters, Jan-15, Volume: 24, Issue:2
Synthesis and antibacterial activity of a series of novel 9-O-acetyl- 4'-substituted 16-membered macrolides derived from josamycin.
AID529875Antimicrobial activity against Enterococcus faecalis JH2-2 harboring pAT392 containing mph(B) gene by broth microdilution method2008Antimicrobial agents and chemotherapy, Aug, Volume: 52, Issue:8
Emergence of macrolide resistance gene mph(B) in Streptococcus uberis and cooperative effects with rdmC-like gene.
AID422943Antimicrobial activity against macrolide-resistant Mycoplasma pneumoniae harboring A2063G transition in domain V of 23S rRNA isolated from pediatric patients with community-acquired pneumonia after 10 to 14 days by microdilution method2008Antimicrobial agents and chemotherapy, Jan, Volume: 52, Issue:1
Increased macrolide resistance of Mycoplasma pneumoniae in pediatric patients with community-acquired pneumonia.
AID529866Antimicrobial activity against Streptococcus uberis UCN60 expressing mph(B) and rdmC-like genes by broth microdilution method2008Antimicrobial agents and chemotherapy, Aug, Volume: 52, Issue:8
Emergence of macrolide resistance gene mph(B) in Streptococcus uberis and cooperative effects with rdmC-like gene.
AID520736Antimicrobial activity against erm(B) and cfr-deficient Staphylococcus aureus RN4220 harboring plasmid LI50 by disk diffusion assay2008Antimicrobial agents and chemotherapy, May, Volume: 52, Issue:5
Transcriptional and translational control of the mlr operon, which confers resistance to seven classes of protein synthesis inhibitors.
AID422944Antimicrobial activity against macrolide-resistant Mycoplasma pneumoniae harboring A2064G transition in domain V of 23S rRNA isolated from pediatric patients with community-acquired pneumonia after 10 to 14 days by microdilution method2008Antimicrobial agents and chemotherapy, Jan, Volume: 52, Issue:1
Increased macrolide resistance of Mycoplasma pneumoniae in pediatric patients with community-acquired pneumonia.
AID529879Antimicrobial activity against Enterococcus faecalis JH2-2 harboring empty vector by broth microdilution method2008Antimicrobial agents and chemotherapy, Aug, Volume: 52, Issue:8
Emergence of macrolide resistance gene mph(B) in Streptococcus uberis and cooperative effects with rdmC-like gene.
AID1137038Antimicrobial activity against Bacillus subtilis ATCC 6633 by agar dilution method1977Journal of medicinal chemistry, May, Volume: 20, Issue:5
Structure-activity relationships among the O-acyl derivatives of leucomycin. Correlation of minimal inhibitory concentrations with binding to Escherichia coli ribosomes.
AID529877Antimicrobial activity against Escherichia coli AG100A harboring empty vector by broth microdilution method2008Antimicrobial agents and chemotherapy, Aug, Volume: 52, Issue:8
Emergence of macrolide resistance gene mph(B) in Streptococcus uberis and cooperative effects with rdmC-like gene.
AID520735Antimicrobial activity against Staphylococcus aureus RN4220 harboring erm(B) and cfr gene by disk diffusion assay2008Antimicrobial agents and chemotherapy, May, Volume: 52, Issue:5
Transcriptional and translational control of the mlr operon, which confers resistance to seven classes of protein synthesis inhibitors.
AID1079941Liver damage due to vascular disease: peliosis hepatitis, hepatic veno-occlusive disease, Budd-Chiari syndrome. Value is number of references indexed. [column 'VASC' in source]
AID369232Antibacterial activity against inducible macrolide-lincosamide-streptogramin B-resistant Streptococcus pneumoniae isolates by double-disk diffusion method2007Antimicrobial agents and chemotherapy, Sep, Volume: 51, Issue:9
Serotypes, Clones, and Mechanisms of Resistance of Erythromycin-Resistant Streptococcus pneumoniae Isolates Collected in Spain.
AID1064176Antimicrobial activity against methicillin-resistant Staphylococcus aureus 09-13 by broth microdilution method2014Bioorganic & medicinal chemistry letters, Jan-15, Volume: 24, Issue:2
Synthesis and antibacterial activity of a series of novel 9-O-acetyl- 4'-substituted 16-membered macrolides derived from josamycin.
AID369230Antibacterial activity against erythromycin-resistant Streptococcus pneumoniae assessed as percent sensitive isolates by CLSI breakpoint method2007Antimicrobial agents and chemotherapy, Sep, Volume: 51, Issue:9
Serotypes, Clones, and Mechanisms of Resistance of Erythromycin-Resistant Streptococcus pneumoniae Isolates Collected in Spain.
AID423265Antibacterial activity against 0.01 MOI wild type Chlamydia psittaci 6BC BCRB infected in mouse L2 cells treated 2 hrs after infection measured on day 7 by plaque assay2007Antimicrobial agents and chemotherapy, Dec, Volume: 51, Issue:12
Frequency of development and associated physiological cost of azithromycin resistance in Chlamydia psittaci 6BC and C. trachomatis L2.
AID1424059Induction of ribosome stalling assessed as induction of stalling of ribosome at ermBL ORF at 50 uM by extension inhibition assay2017Journal of natural products, 04-28, Volume: 80, Issue:4
The Berkeleylactones, Antibiotic Macrolides from Fungal Coculture.
AID1079935Cytolytic liver toxicity, either proven histopathologically or where the ratio of maximal ALT or AST activity above normal to that of Alkaline Phosphatase is > 5 (see ACUTE). Value is number of references indexed. [column 'CYTOL' in source]
AID1079949Proposed mechanism(s) of liver damage. [column 'MEC' in source]
AID1079932Highest frequency of moderate liver toxicity observed during clinical trials, expressed as a percentage. [column '% BIOL' in source]
AID529876Antimicrobial activity against Enterococcus faecalis JH2-2 harboring pAT392 containing mph(B) and rdmC-like gene by broth microdilution method2008Antimicrobial agents and chemotherapy, Aug, Volume: 52, Issue:8
Emergence of macrolide resistance gene mph(B) in Streptococcus uberis and cooperative effects with rdmC-like gene.
AID423268Antibacterial activity against azithromycin-resistant 0.01 MOI Chlamydia psittaci 6BC BCRBAZ1 harboring A2059G mutation in bacterial 23S rRNA gene infected in mouse L2 cells treated 2 hrs after infection measured on day 7 by plaque assay2007Antimicrobial agents and chemotherapy, Dec, Volume: 51, Issue:12
Frequency of development and associated physiological cost of azithromycin resistance in Chlamydia psittaci 6BC and C. trachomatis L2.
AID1079938Chronic liver disease either proven histopathologically, or through a chonic elevation of serum amino-transferase activity after 6 months. Value is number of references indexed. [column 'CHRON' in source]
AID283560Antibacterial activity against Escherichia coli HNCE4 after 24 hrs2007Antimicrobial agents and chemotherapy, Mar, Volume: 51, Issue:3
Substrate competition studies using whole-cell accumulation assays with the major tripartite multidrug efflux pumps of Escherichia coli.
AID423266Antibacterial activity against azithromycin-resistant 0.01 MOI Chlamydia psittaci 6BC BCRBAZ2 harboring A2058C mutation in bacterial 23S rRNA gene infected in mouse L2 cells treated 2 hrs after infection measured on day 7 by plaque assay2007Antimicrobial agents and chemotherapy, Dec, Volume: 51, Issue:12
Frequency of development and associated physiological cost of azithromycin resistance in Chlamydia psittaci 6BC and C. trachomatis L2.
AID529867Antimicrobial activity against Streptococcus uberis UCN61 by broth microdilution method2008Antimicrobial agents and chemotherapy, Aug, Volume: 52, Issue:8
Emergence of macrolide resistance gene mph(B) in Streptococcus uberis and cooperative effects with rdmC-like gene.
AID529872Antimicrobial activity against Staphylococcus aureus RN4220 harboring pAT392 containing mph(B) gene by broth microdilution method2008Antimicrobial agents and chemotherapy, Aug, Volume: 52, Issue:8
Emergence of macrolide resistance gene mph(B) in Streptococcus uberis and cooperative effects with rdmC-like gene.
AID283559Antibacterial activity against Escherichia coli AG102MB after 24 hrs2007Antimicrobial agents and chemotherapy, Mar, Volume: 51, Issue:3
Substrate competition studies using whole-cell accumulation assays with the major tripartite multidrug efflux pumps of Escherichia coli.
AID1079945Animal toxicity known. [column 'TOXIC' in source]
AID1137037Antimicrobial activity against Staphylococcus aureus ATCC 6538P by agar dilution method1977Journal of medicinal chemistry, May, Volume: 20, Issue:5
Structure-activity relationships among the O-acyl derivatives of leucomycin. Correlation of minimal inhibitory concentrations with binding to Escherichia coli ribosomes.
AID556351Antimicrobial activity against Mycoplasma pneumoniae FH by microdilution method2009Antimicrobial agents and chemotherapy, May, Volume: 53, Issue:5
Molecular mechanisms of macrolide resistance in clinical isolates of Mycoplasma pneumoniae from China.
AID556349Antimicrobial activity against macrolide-resistant Mycoplasma pneumoniae ATCC 15531 by broth microdilution method2009Antimicrobial agents and chemotherapy, May, Volume: 53, Issue:5
Antimicrobial susceptibility of Mycoplasma pneumoniae isolates and molecular analysis of macrolide-resistant strains from Shanghai, China.
AID519669Inhibition of PAR2-mediated SLIGKV-NH2-induced interleukin-8 production in normal human epidermal keratinocytes preincubated for 24 hrs by ELISA2008Antimicrobial agents and chemotherapy, Apr, Volume: 52, Issue:4
Effect of 14-membered-ring macrolides on production of interleukin-8 mediated by protease-activated receptor 2 in human keratinocytes.
AID369229Antibacterial activity against erythromycin-resistant Streptococcus pneumoniae assessed as percent resistant isolates by CLSI breakpoint method2007Antimicrobial agents and chemotherapy, Sep, Volume: 51, Issue:9
Serotypes, Clones, and Mechanisms of Resistance of Erythromycin-Resistant Streptococcus pneumoniae Isolates Collected in Spain.
AID529869Antimicrobial activity against Escherichia coli AG100A harboring pAT392 containing mph(B) gene by broth microdilution method2008Antimicrobial agents and chemotherapy, Aug, Volume: 52, Issue:8
Emergence of macrolide resistance gene mph(B) in Streptococcus uberis and cooperative effects with rdmC-like gene.
AID1079947Comments (NB not yet translated). [column 'COMMENTAIRES' in source]
AID1079948Times to onset, minimal and maximal, observed in the indexed observations. [column 'DELAI' in source]
AID678738TP_TRANSPORTER: inhibition of Vinblastine efflux (Vinblastine: 0.002 uM, Josamycin: 100 uM) in P388/S and P388/ADR cells2000Clinical and experimental pharmacology & physiology, Aug, Volume: 27, Issue:8
Reversal of anticancer drug resistance by macrolide antibiotics in vitro and in vivo.
AID283581Reduction of Sp1 binding to DNA in cystic fibrosis 16HBE14o-AS3 cells at 8 ug after 24 hrs2007Antimicrobial agents and chemotherapy, Mar, Volume: 51, Issue:3
Azithromycin selectively reduces tumor necrosis factor alpha levels in cystic fibrosis airway epithelial cells.
AID1079934Highest frequency of acute liver toxicity observed during clinical trials, expressed as a percentage. [column '% AIGUE' in source]
AID678748TP_TRANSPORTER: inhibition of Cyclosporin A efflux (CsA: 0.005 uM, Josamycin: 100 uM) in P388/S and P388/ADR cells2000Clinical and experimental pharmacology & physiology, Aug, Volume: 27, Issue:8
Reversal of anticancer drug resistance by macrolide antibiotics in vitro and in vivo.
AID1064180Antimicrobial activity against methicillin-sensitive Staphylococcus aureus ATCC 29213 by broth microdilution method2014Bioorganic & medicinal chemistry letters, Jan-15, Volume: 24, Issue:2
Synthesis and antibacterial activity of a series of novel 9-O-acetyl- 4'-substituted 16-membered macrolides derived from josamycin.
AID1079931Moderate liver toxicity, defined via clinical-chemistry results: ALT or AST serum activity 6 times the normal upper limit (N) or alkaline phosphatase serum activity of 1.7 N. Value is number of references indexed. [column 'BIOL' in source]
AID529870Antimicrobial activity against Escherichia coli AG100A harboring pAT392 containing mph(B) and rdmC-like genes by broth microdilution method2008Antimicrobial agents and chemotherapy, Aug, Volume: 52, Issue:8
Emergence of macrolide resistance gene mph(B) in Streptococcus uberis and cooperative effects with rdmC-like gene.
AID283579Reduction of NF-kappaB binding to DNA in cystic fibrosis 2CFSMEo cells at 8 ug after 24 hrs2007Antimicrobial agents and chemotherapy, Mar, Volume: 51, Issue:3
Azithromycin selectively reduces tumor necrosis factor alpha levels in cystic fibrosis airway epithelial cells.
AID529874Antimicrobial activity against Enterococcus faecalis JH2-2 harboring pAT392 containing rdmC-like gene by broth microdilution method2008Antimicrobial agents and chemotherapy, Aug, Volume: 52, Issue:8
Emergence of macrolide resistance gene mph(B) in Streptococcus uberis and cooperative effects with rdmC-like gene.
AID1424070In-vitro inhibition of protein translation using pY71-sfGFP in PUREexpress in vitro protein synthesis system assessed as reduction in cell-free GFP protein translation at 50 uM measured every 20 mins for 2 hrs2017Journal of natural products, 04-28, Volume: 80, Issue:4
The Berkeleylactones, Antibiotic Macrolides from Fungal Coculture.
AID529871Antimicrobial activity against Staphylococcus aureus RN4220 harboring pAT392 containing rdmC-like gene by broth microdilution method2008Antimicrobial agents and chemotherapy, Aug, Volume: 52, Issue:8
Emergence of macrolide resistance gene mph(B) in Streptococcus uberis and cooperative effects with rdmC-like gene.
AID423267Antibacterial activity against azithromycin-resistant 0.01 MOI Chlamydia psittaci 6BC BCRBAZ5 harboring A2059C mutation in bacterial 23S rRNA gene infected in mouse L2 cells treated 2 hrs after infection measured on day 7 by plaque assay2007Antimicrobial agents and chemotherapy, Dec, Volume: 51, Issue:12
Frequency of development and associated physiological cost of azithromycin resistance in Chlamydia psittaci 6BC and C. trachomatis L2.
AID529873Antimicrobial activity against Staphylococcus aureus RN4220 harboring pAT392 containing mph(B) and rdmC-like genes by broth microdilution method2008Antimicrobial agents and chemotherapy, Aug, Volume: 52, Issue:8
Emergence of macrolide resistance gene mph(B) in Streptococcus uberis and cooperative effects with rdmC-like gene.
AID529878Antimicrobial activity against Staphylococcus aureus RN4220 harboring empty vector by broth microdilution method2008Antimicrobial agents and chemotherapy, Aug, Volume: 52, Issue:8
Emergence of macrolide resistance gene mph(B) in Streptococcus uberis and cooperative effects with rdmC-like gene.
AID1064179Antimicrobial activity against methicillin-resistant Staphylococcus aureus ATCC 33591 by broth microdilution method2014Bioorganic & medicinal chemistry letters, Jan-15, Volume: 24, Issue:2
Synthesis and antibacterial activity of a series of novel 9-O-acetyl- 4'-substituted 16-membered macrolides derived from josamycin.
AID1079933Acute liver toxicity defined via clinical observations and clear clinical-chemistry results: serum ALT or AST activity > 6 N or serum alkaline phosphatases activity > 1.7 N. This category includes cytolytic, choleostatic and mixed liver toxicity. Value is
AID1079943Malignant tumor, proven histopathologically. Value is number of references indexed. [column 'T.MAL' in source]
AID369231Antibacterial activity against constitutive macrolide-lincosamide-streptogramin B-resistant Streptococcus pneumoniae isolates by double-disk diffusion method2007Antimicrobial agents and chemotherapy, Sep, Volume: 51, Issue:9
Serotypes, Clones, and Mechanisms of Resistance of Erythromycin-Resistant Streptococcus pneumoniae Isolates Collected in Spain.
AID283580Reduction of Sp1 binding to DNA in cystic fibrosis IB3-1 cells at 8 ug after 24 hrs2007Antimicrobial agents and chemotherapy, Mar, Volume: 51, Issue:3
Azithromycin selectively reduces tumor necrosis factor alpha levels in cystic fibrosis airway epithelial cells.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (15)

TimeframeStudies, This Drug (%)All Drugs %
pre-19901 (6.67)18.7374
1990's0 (0.00)18.2507
2000's12 (80.00)29.6817
2010's2 (13.33)24.3611
2020's0 (0.00)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 51.34

According to the monthly volume, diversity, and competition of internet searches for this compound, as well the volume and growth of publications, there is estimated to be very strong demand-to-supply ratio for research on this compound.

MetricThis Compound (vs All)
Research Demand Index51.34 (24.57)
Research Supply Index2.83 (2.92)
Research Growth Index5.42 (4.65)
Search Engine Demand Index75.36 (26.88)
Search Engine Supply Index2.00 (0.95)

This Compound (51.34)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Reviews0 (0.00%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other16 (100.00%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Clinical Trials (1)

Trial Overview

TrialPhaseEnrollmentStudy TypeStart DateStatus
Reduction of Spontaneous Prematurity: Impact of Antibiotic Treatment (Josamycin) in Case of Positive PCR for Ureaplasma Spp and/or Mycoplasma Hominis in Amniotic Fluid [NCT00718705]Phase 33,200 participants (Actual)Interventional2008-07-31Completed
[information is prepared from clinicaltrials.gov, extracted Sep-2024]
SubstanceRelationship StrengthStudiesTrialsClassesRoles
verapamil
Verapamil: A calcium channel blocker that is a class IV anti-arrhythmia agent.. verapamil : A racemate comprising equimolar amounts of dexverapamil and (S)-verapamil. An L-type calcium channel blocker of the phenylalkylamine class, it is used (particularly as the hydrochloride salt) in the treatment of hypertension, angina pectoris and cardiac arrhythmia, and as a preventive medication for migraine.. 2-(3,4-dimethoxyphenyl)-5-{[2-(3,4-dimethoxyphenyl)ethyl](methyl)amino}-2-(propan-2-yl)pentanenitrile : A tertiary amino compound that is 3,4-dimethoxyphenylethylamine in which the hydrogens attached to the nitrogen are replaced by a methyl group and a 4-cyano-4-(3,4-dimethoxyphenyl)-5-methylhexyl group.		210aromatic ether;
nitrile;
polyether;
tertiary amino compound
carbonyl cyanide m-chlorophenyl hydrazone
Carbonyl Cyanide m-Chlorophenyl Hydrazone: A proton ionophore. It is commonly used as an uncoupling agent and inhibitor of photosynthesis because of its effects on mitochondrial and chloroplast membranes.. CCCP : A member of the class of monochlorobenzenes that is benzene substituted by 2-(1,3-dinitrilopropan-2-ylidene)hydrazinyl and chloro groups at positions 1 and 3, respectively. It is a mitochondrial depolarizing agent that induces reactive oxygen species mediated cell death.		2.0310hydrazone;
monochlorobenzenes;
nitrile		antibacterial agent;
geroprotector;
ionophore
ciprofloxacin
Ciprofloxacin: A broad-spectrum antimicrobial carboxyfluoroquinoline.. ciprofloxacin : A quinolone that is quinolin-4(1H)-one bearing cyclopropyl, carboxylic acid, fluoro and piperazin-1-yl substituents at positions 1, 3, 6 and 7, respectively.		2.4420aminoquinoline;
cyclopropanes;
fluoroquinolone antibiotic;
N-arylpiperazine;
quinolinemonocarboxylic acid;
quinolone antibiotic;
quinolone;
zwitterion		antibacterial drug;
antiinfective agent;
antimicrobial agent;
DNA synthesis inhibitor;
EC 5.99.1.3 [DNA topoisomerase (ATP-hydrolysing)] inhibitor;
environmental contaminant;
topoisomerase IV inhibitor;
xenobiotic
reserpine
Reserpine: An alkaloid found in the roots of Rauwolfia serpentina and R. vomitoria. Reserpine inhibits the uptake of norepinephrine into storage vesicles resulting in depletion of catecholamines and serotonin from central and peripheral axon terminals. It has been used as an antihypertensive and an antipsychotic as well as a research tool, but its adverse effects limit its clinical use.. reserpine : An alkaloid found in the roots of Rauwolfia serpentina and R. vomitoria.		2.0310alkaloid ester;
methyl ester;
yohimban alkaloid		adrenergic uptake inhibitor;
antihypertensive agent;
EC 3.4.21.26 (prolyl oligopeptidase) inhibitor;
environmental contaminant;
first generation antipsychotic;
plant metabolite;
xenobiotic
chloramphenicol
Amphenicol: Chloramphenicol and its derivatives.		3.1350C-nitro compound;
carboxamide;
diol;
organochlorine compound		antibacterial drug;
antimicrobial agent;
Escherichia coli metabolite;
geroprotector;
Mycoplasma genitalium metabolite;
protein synthesis inhibitor
kanamycin a
Kanamycin: Antibiotic complex produced by Streptomyces kanamyceticus from Japanese soil. Comprises 3 components: kanamycin A, the major component, and kanamycins B and C, the minor components.. kanamycin : Kanamycin is a naturally occurring antibiotic complex from Streptomyces kanamyceticus that consists of several components: kanamycin A, the major component (also usually designated as kanamycin), and kanamycins B, C, D and X the minor components.		2.0310kanamycinsbacterial metabolite
ampicillin
Ampicillin: Semi-synthetic derivative of penicillin that functions as an orally active broad-spectrum antibiotic.. ampicillin : A penicillin in which the substituent at position 6 of the penam ring is a 2-amino-2-phenylacetamido group.		2.0310beta-lactam antibiotic;
penicillin allergen;
penicillin		antibacterial drug
taurocholic acid
Taurocholic Acid: The product of conjugation of cholic acid with taurine. Its sodium salt is the chief ingredient of the bile of carnivorous animals. It acts as a detergent to solubilize fats for absorption and is itself absorbed. It is used as a cholagogue and cholerectic.. taurocholate : An organosulfonate oxoanion that is the conjugate base of taurocholic acid.. taurocholic acid : A bile acid taurine conjugate of cholic acid that usually occurs as the sodium salt of bile in mammals.		2.0310amino sulfonic acid;
bile acid taurine conjugate		human metabolite
gentian violet
Gentian Violet: A dye that is a mixture of violet rosanilinis with antibacterial, antifungal, and anthelmintic properties.. crystal violet : An organic chloride salt that is the monochloride salt of crystal violet cation. It has been used in creams for the topical treatment of bacterial and fungal infections, being effective against some Gram-positive bacteria (notably Staphylococcus species) and some pathogenic fungi (including Candida species) but use declined following reports of animal carcinogenicity. It has also been used for dying wood, silk, and paper, as well as a histological stain.		2.0310organic chloride saltanthelminthic drug;
antibacterial agent;
antifungal agent;
antiseptic drug;
histological dye
erythromycin
Erythromycin: A bacteriostatic antibiotic macrolide produced by Streptomyces erythreus. Erythromycin A is considered its major active component. In sensitive organisms, it inhibits protein synthesis by binding to 50S ribosomal subunits. This binding process inhibits peptidyl transferase activity and interferes with translocation of amino acids during translation and assembly of proteins.. erythromycin : Any of several wide-spectrum macrolide antibiotics obtained from actinomycete Saccharopolyspora erythraea (formerly known as Streptomyces erythraeus).. erythromycin A : An erythromycin that consists of erythronolide A having 2,6-dideoxy-3-C-methyl-3-O-methyl-alpha-L-ribo-hexopyranosyl and 3,4,6-trideoxy-3-(dimethylamino)-beta-D-xylo-hexopyranosyl residues attahced at positions 4 and 6 respectively.		3.97130cyclic ketone;
erythromycin
vinblastine
[no description available]		210
ethidium bromide
[no description available]		2.0310organic bromide saltgeroprotector;
intercalator;
trypanocidal drug
vancomycin
Vancomycin: Antibacterial obtained from Streptomyces orientalis. It is a glycopeptide related to RISTOCETIN that inhibits bacterial cell wall assembly and is toxic to kidneys and the inner ear.. vancomycin : A complex glycopeptide from Streptomyces orientalis. It inhibits a specific step in the synthesis of the peptidoglycan layer in the Gram-positive bacteria Staphylococcus aureus and Clostridium difficile.		2.4820glycopeptideantibacterial drug;
antimicrobial agent;
bacterial metabolite
cefazolin
Cefazolin: A semisynthetic cephalosporin analog with broad-spectrum antibiotic action due to inhibition of bacterial cell wall synthesis. It attains high serum levels and is excreted quickly via the urine.. cefazolin : A first-generation cephalosporin compound having [(5-methyl-1,3,4-thiadiazol-2-yl)sulfanyl]methyl and (1H-tetrazol-1-ylacetyl)amino side-groups at positions 3 and 7 respectively.		2.1510beta-lactam antibiotic allergen;
cephalosporin;
tetrazoles;
thiadiazoles		antibacterial drug
oleandomycin
[no description available]		2.4420oleandomycins
clarithromycin
Clarithromycin: A semisynthetic macrolide antibiotic derived from ERYTHROMYCIN that is active against a variety of microorganisms. It can inhibit PROTEIN SYNTHESIS in BACTERIA by reversibly binding to the 50S ribosomal subunits. This inhibits the translocation of aminoacyl transfer-RNA and prevents peptide chain elongation.. clarithromycin : The 6-O-methyl ether of erythromycin A, clarithromycin is a macrolide antibiotic used in the treatment of respiratory-tract, skin and soft-tissue infections. It is also used to eradicate Helicobacter pylori in the treatment of peptic ulcer disease. It prevents bacteria from growing by interfering with their protein synthesis.		3.1350macrolide antibioticantibacterial drug;
environmental contaminant;
protein synthesis inhibitor;
xenobiotic
florfenicol
florfenicol: structure given in first source. florfenicol : A carboxamide that is the N-dichloroacetyl derivative of (1R,2S)-2-amino-3-fluoro-1-[4-(methanesulfonyl)phenyl]propan-1-ol. A synthetic veterinary antibiotic that is used for treatment of bovine respiratory disease and foot rot; also used in aquaculture.		2.0410organochlorine compound;
organofluorine compound;
secondary alcohol;
secondary carboxamide;
sulfone		antimicrobial agent
levofloxacin
Levofloxacin: The L-isomer of Ofloxacin.. levofloxacin : An optically active form of ofloxacin having (S)-configuration; an inhibitor of bacterial topoisomerase IV and DNA gyrase.		2.97409-fluoro-3-methyl-10-(4-methylpiperazin-1-yl)-7-oxo-2,3-dihydro-7H-[1,4]oxazino[2,3,4-ij]quinoline-6-carboxylic acid;
fluoroquinolone antibiotic;
quinolone antibiotic		antibacterial drug;
DNA synthesis inhibitor;
EC 5.99.1.3 [DNA topoisomerase (ATP-hydrolysing)] inhibitor;
topoisomerase IV inhibitor
moxifloxacin
Moxifloxacin: A fluoroquinolone that acts as an inhibitor of DNA TOPOISOMERASE II and is used as a broad-spectrum antibacterial agent.. moxifloxacin : A quinolone that consists of 4-oxo-1,4-dihydroquinoline-3-carboxylic acid bearing a cyclopropyl substituent at position 1, a fluoro substitiuent at position 6, a (4aS,7aS)-octahydro-6H-pyrrolo[3,4-b]pyridin-6-yl group at position 7 and a methoxy substituent at position 8. A member of the fluoroquinolone class of antibacterial agents.		2.4420aromatic ether;
cyclopropanes;
fluoroquinolone antibiotic;
pyrrolidinopiperidine;
quinolinemonocarboxylic acid;
quinolone antibiotic;
quinolone		antibacterial drug
a 195773
[no description available]		2.0410macrolide antibiotic;
monosaccharide derivative;
quinolines		antibacterial drug;
protein synthesis inhibitor
cholic acid
Cholic Acid: A major primary bile acid produced in the liver and usually conjugated with glycine or taurine. It facilitates fat absorption and cholesterol excretion.. cholic acid : A bile acid that is 5beta-cholan-24-oic acid bearing three alpha-hydroxy substituents at position 3, 7 and 12.		2.031012alpha-hydroxy steroid;
3alpha-hydroxy steroid;
7alpha-hydroxy steroid;
bile acid;
C24-steroid;
trihydroxy-5beta-cholanic acid		human metabolite;
mouse metabolite
linezolid
[no description available]		2.4820acetamides;
morpholines;
organofluorine compound;
oxazolidinone		antibacterial drug;
protein synthesis inhibitor
tacrolimus
Tacrolimus: A macrolide isolated from the culture broth of a strain of Streptomyces tsukubaensis that has strong immunosuppressive activity in vivo and prevents the activation of T-lymphocytes in response to antigenic or mitogenic stimulation in vitro.. tacrolimus (anhydrous) : A macrolide lactam containing a 23-membered lactone ring, originally isolated from the fermentation broth of a Japanese soil sample that contained the bacteria Streptomyces tsukubaensis.		210macrolide lactambacterial metabolite;
immunosuppressive agent
clindamycin
Clindamycin: An antibacterial agent that is a semisynthetic analog of LINCOMYCIN.. clindamycin : A carbohydrate-containing antibiotic that is the semisynthetic derivative of lincomycin, a natural antibiotic.		3.1550
zithromax
Azithromycin: A semi-synthetic macrolide antibiotic structurally related to ERYTHROMYCIN. It has been used in the treatment of Mycobacterium avium intracellulare infections, toxoplasmosis, and cryptosporidiosis.. azithromycin : A macrolide antibiotic useful for the treatment of bacterial infections.		3.5480macrolide antibioticantibacterial drug;
environmental contaminant;
xenobiotic
tiamulin
tiamulin: 81723 HFU and tiamutin are for fumarate salt; prevents senescence in ascomycete; pleuromutilin derivative; RN given refers to ((3aS-(3aalpha,4beta,5alpha,6alpha,8beta,9alpha,9abeta,10S*))-isomer. tiamulin : A carbotricyclic compound that is pleuromutilin in which the hydroxyacetate group is replaced by a 2-{[2-(diethylamino)ethyl]sulfanyl}acetate group. An antibacterial drug, tiamulin is used in veterinary medicine (generally as its hydrogen fumarate salt) for the treatment of swine dysentery caused by Serpulina hyodysenteriae.		2.0410carbotricyclic compound;
carboxylic ester;
cyclic ketone;
organic sulfide;
secondary alcohol;
semisynthetic derivative;
tertiary amino compound;
tetracyclic diterpenoid		antibacterial drug
fusidic acid
Fusidic Acid: An antibiotic isolated from the fermentation broth of Fusidium coccineum. (From Merck Index, 11th ed). It acts by inhibiting translocation during protein synthesis.. fusidic acid : A steroid antibiotic that is isolated from the fermentation broth of Fusidium coccineum.		2.031011alpha-hydroxy steroid;
3alpha-hydroxy steroid;
alpha,beta-unsaturated monocarboxylic acid;
steroid acid;
steroid antibiotic;
sterol ester		EC 2.7.1.33 (pantothenate kinase) inhibitor;
Escherichia coli metabolite;
protein synthesis inhibitor
hmr 3647
[no description available]		2.7330
sodium dodecyl sulfate
Sodium Dodecyl Sulfate: An anionic surfactant, usually a mixture of sodium alkyl sulfates, mainly the lauryl; lowers surface tension of aqueous solutions; used as fat emulsifier, wetting agent, detergent in cosmetics, pharmaceuticals and toothpastes; also as research tool in protein biochemistry.. sodium dodecyl sulfate : An organic sodium salt that is the sodium salt of dodecyl hydrogen sulfate.		2.0310organic sodium saltdetergent;
protein denaturant
tylosin
[no description available]		3.1550aldehyde;
disaccharide derivative;
enone;
leucomycin;
macrolide antibiotic;
monosaccharide derivative		allergen;
bacterial metabolite;
environmental contaminant;
xenobiotic
rokitamycin
rokitamycin: structure in first source		2.0410organic molecular entity
cyclosporine
ramihyphin A: one of the metabolites produced by Fusarium sp. S-435; RN given refers to cpd with unknown MF		210homodetic cyclic peptideanti-asthmatic drug;
anticoronaviral agent;
antifungal agent;
antirheumatic drug;
carcinogenic agent;
dermatologic drug;
EC 3.1.3.16 (phosphoprotein phosphatase) inhibitor;
geroprotector;
immunosuppressive agent;
metabolite
demycarosylturimycin h
[no description available]		3.1450
cefotaxime
Cefotaxime: Semisynthetic broad-spectrum cephalosporin.. cefotaxime : A cephalosporin compound having acetoxymethyl and [2-(2-amino-1,3-thiazol-4-yl)-2-(methoxyimino)acetyl]amino side groups.		2.03101,3-thiazoles;
cephalosporin;
oxime O-ether		antibacterial drug;
drug allergen
dirithromycin
[no description available]		2.0310macrolide antibioticprodrug
roxithromycin
(E)-roxithromycin : A major geometrical isomer of roxithromycin.		2.7330roxithromycinenvironmental contaminant;
xenobiotic
a26771b
A26771B: produced by Penicillium turbatum; structure		2.1510
novobiocin
Novobiocin: An antibiotic compound derived from Streptomyces niveus. It has a chemical structure similar to coumarin. Novobiocin binds to DNA gyrase, and blocks adenosine triphosphatase (ATPase) activity. (From Reynolds, Martindale The Extra Pharmacopoeia, 30th ed, p189). novobiocin : A coumarin-derived antibiotic obtained from Streptomyces niveus.		2.0310carbamate ester;
ether;
hexoside;
hydroxycoumarin;
monocarboxylic acid amide;
monosaccharide derivative;
phenols		antibacterial agent;
antimicrobial agent;
EC 5.99.1.3 [DNA topoisomerase (ATP-hydrolysing)] inhibitor;
Escherichia coli metabolite;
hepatoprotective agent
tetracycline
Tetracycline: A naphthacene antibiotic that inhibits AMINO ACYL TRNA binding during protein synthesis.. tetracycline : A broad-spectrum polyketide antibiotic produced by the Streptomyces genus of actinobacteria.		2.7330
minocycline
Minocycline: A TETRACYCLINE analog, having a 7-dimethylamino and lacking the 5 methyl and hydroxyl groups, which is effective against tetracycline-resistant STAPHYLOCOCCUS infections.. minocycline : A tetracycline analogue having a dimethylamino group at position 7 and lacking the methyl and hydroxy groups at position 5.		2.4520
ConditionIndicatedRelationship StrengthStudiesTrials
Leukemia P388
An experimental lymphocytic leukemia originally induced in DBA/2 mice by painting with methylcholanthrene.		0210
Cystic Fibrosis of Pancreas
[description not available]		02.0310
Cystic Fibrosis
An autosomal recessive genetic disease of the EXOCRINE GLANDS. It is caused by mutations in the gene encoding the CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR expressed in several organs including the LUNG, the PANCREAS, the BILIARY SYSTEM, and the SWEAT GLANDS. Cystic fibrosis is characterized by epithelial secretory dysfunction associated with ductal obstruction resulting in AIRWAY OBSTRUCTION; chronic RESPIRATORY INFECTIONS; PANCREATIC INSUFFICIENCY; maldigestion; salt depletion; and HEAT PROSTRATION.		02.0310
Infections, Pneumococcal
[description not available]		02.0310
Pneumococcal Infections
Infections with bacteria of the species STREPTOCOCCUS PNEUMONIAE.		02.0310
Community Acquired Infection
[description not available]		02.0410
Mycoplasma dispar Infection
[description not available]		02.7430
Infections, Respiratory
[description not available]		02.4520
Respiratory Tract Infections
Invasion of the host RESPIRATORY SYSTEM by microorganisms, usually leading to pathological processes or diseases.		02.4520