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1-((3,5-dichloro)-2,6-dihydroxy-4-methoxyphenyl)-1-hexanone and puromycin

1-((3,5-dichloro)-2,6-dihydroxy-4-methoxyphenyl)-1-hexanone has been researched along with puromycin in 5 studies

Compound Research Comparison

Studies
(1-((3,5-dichloro)-2,6-dihydroxy-4-methoxyphenyl)-1-hexanone)
Trials
(1-((3,5-dichloro)-2,6-dihydroxy-4-methoxyphenyl)-1-hexanone)
Recent Studies (post-2010)
(1-((3,5-dichloro)-2,6-dihydroxy-4-methoxyphenyl)-1-hexanone)
Studies
(puromycin)
Trials
(puromycin)
Recent Studies (post-2010) (puromycin)
7,66601,6585,8281311

Protein Interaction Comparison

ProteinTaxonomy1-((3,5-dichloro)-2,6-dihydroxy-4-methoxyphenyl)-1-hexanone (IC50)puromycin (IC50)
30S ribosomal protein S6Escherichia coli K-120.9
30S ribosomal protein S7Escherichia coli K-120.9
50S ribosomal protein L15Escherichia coli K-120.9
50S ribosomal protein L10Escherichia coli K-120.9
50S ribosomal protein L11Escherichia coli K-120.9
50S ribosomal protein L7/L12Escherichia coli K-120.9
50S ribosomal protein L19Escherichia coli K-120.9
50S ribosomal protein L1Escherichia coli K-120.9
50S ribosomal protein L20Escherichia coli K-120.9
50S ribosomal protein L27Escherichia coli K-120.9
50S ribosomal protein L28Escherichia coli K-120.9
50S ribosomal protein L29Escherichia coli K-120.9
50S ribosomal protein L31Escherichia coli K-120.9
50S ribosomal protein L31 type BEscherichia coli K-120.9
50S ribosomal protein L32Escherichia coli K-120.9
50S ribosomal protein L33Escherichia coli K-120.9
50S ribosomal protein L34Escherichia coli K-120.9
50S ribosomal protein L35Escherichia coli K-120.9
50S ribosomal protein L36Escherichia coli K-120.9
30S ribosomal protein S10Escherichia coli K-120.9
30S ribosomal protein S11Escherichia coli K-120.9
30S ribosomal protein S12Escherichia coli K-120.9
30S ribosomal protein S13Escherichia coli K-120.9
30S ribosomal protein S16Escherichia coli K-120.9
30S ribosomal protein S18Escherichia coli K-120.9
30S ribosomal protein S19Escherichia coli K-120.9
30S ribosomal protein S20Escherichia coli K-120.9
30S ribosomal protein S2Escherichia coli K-120.9
30S ribosomal protein S3Escherichia coli K-120.9
30S ribosomal protein S4Escherichia coli K-120.9
30S ribosomal protein S5Escherichia coli K-120.9
30S ribosomal protein S8Escherichia coli K-120.9
30S ribosomal protein S9Escherichia coli K-120.9
50S ribosomal protein L13Escherichia coli K-120.9
50S ribosomal protein L14Escherichia coli K-120.9
50S ribosomal protein L16Escherichia coli K-120.9
50S ribosomal protein L23Escherichia coli K-120.9
30S ribosomal protein S15Escherichia coli K-120.9
50S ribosomal protein L17Escherichia coli K-120.9
50S ribosomal protein L21Escherichia coli K-120.9
50S ribosomal protein L30Escherichia coli K-120.9
50S ribosomal protein L6Escherichia coli K-120.9
30S ribosomal protein S14Escherichia coli K-120.9
30S ribosomal protein S17Escherichia coli K-120.9
30S ribosomal protein S1Escherichia coli K-120.9
50S ribosomal protein L18Escherichia coli K-120.9
Puromycin-sensitive aminopeptidaseHomo sapiens (human)6.075
50S ribosomal protein L2Escherichia coli K-120.9
50S ribosomal protein L3Escherichia coli K-120.9
50S ribosomal protein L24Escherichia coli K-120.9
50S ribosomal protein L4Escherichia coli K-120.9
50S ribosomal protein L22Escherichia coli K-120.9
50S ribosomal protein L5Escherichia coli K-120.9
30S ribosomal protein S21Escherichia coli K-120.9
50S ribosomal protein L25Escherichia coli K-120.9
50S ribosomal protein L36 2Escherichia coli K-120.9

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19901 (20.00)18.7374
1990's0 (0.00)18.2507
2000's2 (40.00)29.6817
2010's2 (40.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Amara, JF; Lodish, HF1
Drainas, D; Stathopoulos, C; Tekos, A; Tsagla, A1
Drainas, D; Kalavrizioti, D; Stathopoulos, C; Tekos, A; Tsagla, A; Vourekas, A1
Catalano, A; O'Day, DH; Poloz, Y1
Catalano, A; Huber, RJ; O'Day, DH1

Other Studies

5 other study(ies) available for 1-((3,5-dichloro)-2,6-dihydroxy-4-methoxyphenyl)-1-hexanone and puromycin

ArticleYear
Specific mRNA destabilization in Dictyostelium discoideum requires RNA synthesis.
    Molecular and cellular biology, 1987, Volume: 7, Issue:12

    Topics: Actins; Cycloheximide; Dactinomycin; Daunorubicin; Dictyostelium; Drug Synergism; Fungal Proteins; Puromycin; RNA, Fungal; RNA, Messenger; RNA, Ribosomal

1987
Effect of peptidyltransferase inhibitors on ribonuclease P activity from Dictyostelium discoideum. Effect of antibiotics on RNase P.
    Molecular biology reports, 2000, Volume: 27, Issue:2

    Topics: Animals; Anti-Bacterial Agents; Cell-Free System; Dictyostelium; Endoribonucleases; Enzyme Inhibitors; Inhibitory Concentration 50; Nucleosides; Peptidyl Transferases; Puromycin; Pyrimidine Nucleosides; Ribonuclease P; RNA, Catalytic

2000
Kinetics of inhibition of ribonuclease P activity by peptidyltransferase inhibitors. Effect of antibiotics on RNase P.
    Molecular biology reports, 2003, Volume: 30, Issue:1

    Topics: Animals; Dictyostelium; Dose-Response Relationship, Drug; Endoribonucleases; Kinetics; Nucleosides; Peptidyl Transferases; Protein Synthesis Inhibitors; Puromycin; Pyrimidine Nucleosides; Ribonuclease P; RNA, Catalytic

2003
Dictyostelium puromycin-sensitive aminopeptidase A is a nucleoplasmic nucleomorphin-binding protein that relocates to the cytoplasm during mitosis.
    Histochemistry and cell biology, 2011, Volume: 136, Issue:6

    Topics: Amino Acid Sequence; Animals; Calmodulin-Binding Proteins; Cell Nucleus; Cytoplasm; Dictyostelium; Drosophila; Glutamyl Aminopeptidase; Humans; Mice; Mitosis; Molecular Sequence Data; Protein Structure, Tertiary; Puromycin; Signal Transduction; Trypanocidal Agents

2011
Cyclin-dependent kinase 5 is a calmodulin-binding protein that associates with puromycin-sensitive aminopeptidase in the nucleus of Dictyostelium.
    Biochimica et biophysica acta, 2013, Volume: 1833, Issue:1

    Topics: Aminopeptidases; Antigens, Protozoan; Calmodulin; Calmodulin-Binding Proteins; Cell Nucleus; Cyclin-Dependent Kinase 5; Dictyostelium; Drug Resistance, Microbial; Immunoprecipitation; Membrane Glycoproteins; Models, Biological; Protein Binding; Protein Interaction Domains and Motifs; Protozoan Proteins; Puromycin; Sequence Deletion; Trypanocidal Agents

2013