Compounds > az 505
Page last updated: 2024-11-13

az 505

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Description

AZ 505: an SMYD2 inhibitor; structure in first source [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID SourceID
PubMed CID24961094
CHEMBL ID2169920
SCHEMBL ID3598040
MeSH IDM0569343

Synonyms (25)

Synonym
nh5 ,
n-cyclohexyl-n~3~-[2-(3,4-dichlorophenyl)ethyl]-n-(2-{[2-(5-hydroxy-3-oxo-3,4-dihydro-2h-1,4-benzoxazin-8-yl)ethyl]amino}ethyl)-beta-alaninamide
CHEMBL2169920 ,
bdbm50396022
az505 ,
gtpl7021
az-505
n-cyclohexyl-3-[2-(3,4-dichlorophenyl)ethylamino]-n-[2-[2-(5-hydroxy-3-oxo-4h-1,4-benzoxazin-8-yl)ethylamino]ethyl]propanamide
az 505
CS-1735
HY-15226
SCHEMBL3598040
1035227-43-0
n-cyclohexyl-3-((3,4-dichlorophenethyl)amino)-n-(2-((2-(5-hydroxy-3-oxo-3,4-dihydro-2h-benzo[b][1,4]oxazin-8-yl)ethyl)amino)ethyl)propanamide
EX-A2380
Q27074673
BCP20970
az505;az 505
az505 free base
C14051
MS-30384
nsc780404
nsc-780404
n-cyclohexyl-3-{[2-(3,4-dichlorophenyl)ethyl]amino}-n-(2-{[2-(5-hydroxy-3-oxo-3,4-dihydro-2h-1,4-benzoxazin-8-yl)ethyl]amino}ethyl)propanamide
AC-35774
[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Protein Targets (2)

Inhibition Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
N-lysine methyltransferase SMYD2Homo sapiens (human)IC50 (µMol)10.42380.01500.769210.0000AID1199193; AID1234041; AID1234083; AID1308097; AID1308098; AID1308099; AID1308102; AID1863574; AID1863576; AID1887903; AID700460
N-lysine methyltransferase SMYD2Homo sapiens (human)Ki0.30000.30000.30000.3000AID700452
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Activation Measurements

ProteinTaxonomyMeasurementAverageMin (ref.)Avg (ref.)Max (ref.)Bioassay(s)
N-lysine methyltransferase SMYD2Homo sapiens (human)Kd167.00000.50000.50000.5000AID1199194; AID1845921; AID1863573
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Biological Processes (15)

Processvia Protein(s)Taxonomy
nucleosome assemblyHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
myotube cell developmentHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
methylationHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
positive regulation of peptidyl-serine phosphorylationHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
establishment of protein localizationHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
positive regulation of transcription by RNA polymerase IIHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
cellular response to dexamethasone stimulusHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
negative regulation of transcription by RNA polymerase IIN-lysine methyltransferase SMYD2Homo sapiens (human)
chromatin remodelingN-lysine methyltransferase SMYD2Homo sapiens (human)
heart developmentN-lysine methyltransferase SMYD2Homo sapiens (human)
negative regulation of cell population proliferationN-lysine methyltransferase SMYD2Homo sapiens (human)
peptidyl-lysine monomethylationN-lysine methyltransferase SMYD2Homo sapiens (human)
peptidyl-lysine dimethylationN-lysine methyltransferase SMYD2Homo sapiens (human)
regulation of DNA damage response, signal transduction by p53 class mediatorN-lysine methyltransferase SMYD2Homo sapiens (human)
regulation of signal transduction by p53 class mediatorN-lysine methyltransferase SMYD2Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Molecular Functions (13)

Processvia Protein(s)Taxonomy
RNA polymerase II cis-regulatory region sequence-specific DNA bindingHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
RNA polymerase II complex bindingHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
RNA polymerase II intronic transcription regulatory region sequence-specific DNA bindingHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
protein bindingHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
metal ion bindingHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
histone H4 methyltransferase activityHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
histone H3K36 dimethyltransferase activityHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
histone H3K4 trimethyltransferase activityHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
RNA polymerase II complex bindingN-lysine methyltransferase SMYD2Homo sapiens (human)
p53 bindingN-lysine methyltransferase SMYD2Homo sapiens (human)
protein bindingN-lysine methyltransferase SMYD2Homo sapiens (human)
lysine N-methyltransferase activityN-lysine methyltransferase SMYD2Homo sapiens (human)
protein-lysine N-methyltransferase activityN-lysine methyltransferase SMYD2Homo sapiens (human)
metal ion bindingN-lysine methyltransferase SMYD2Homo sapiens (human)
histone H3K36 methyltransferase activityN-lysine methyltransferase SMYD2Homo sapiens (human)
histone H3 methyltransferase activityN-lysine methyltransferase SMYD2Homo sapiens (human)
histone H3K4 trimethyltransferase activityN-lysine methyltransferase SMYD2Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Ceullar Components (4)

Processvia Protein(s)Taxonomy
nucleusHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
nucleoplasmHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
cytosolHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
nucleusHistone-lysine N-methyltransferase SMYD3Homo sapiens (human)
nucleusN-lysine methyltransferase SMYD2Homo sapiens (human)
nucleoplasmN-lysine methyltransferase SMYD2Homo sapiens (human)
cytoplasmN-lysine methyltransferase SMYD2Homo sapiens (human)
cytosolN-lysine methyltransferase SMYD2Homo sapiens (human)
nucleusN-lysine methyltransferase SMYD2Homo sapiens (human)
[Information is prepared from geneontology information from the June-17-2024 release]

Bioassays (41)

Assay IDTitleYearJournalArticle
AID1346111Human SET and MYND domain containing 2 (2.1.1.43 Histone methyltransferases (HMTs))2011Structure (London, England : 1993), Sep-07, Volume: 19, Issue:9
Structural basis of substrate methylation and inhibition of SMYD2.
AID1863575Inhibition of SMYD3 (unknown origin) using p53 (361 to 380 residues) and [3H]-SAM as substrate incubated for 90 mins by SPA assay2022Journal of medicinal chemistry, 08-11, Volume: 65, Issue:15
Protein Lysine Methyltransferase SMYD2: A Promising Small Molecule Target for Cancer Therapy.
AID700457Selectivity ratio of IC50 for EZH2 to IC50 for human SMYD22012European journal of medicinal chemistry, Oct, Volume: 56Oncoepigenomics: making histone lysine methylation count.
AID1308102Inhibition of SMYD2 (unknown origin) expressed in human U2OS cells assessed as reduction in p53 methylation by Western blot analysis2016Journal of medicinal chemistry, 05-26, Volume: 59, Issue:10
Discovery and Characterization of a Highly Potent and Selective Aminopyrazoline-Based in Vivo Probe (BAY-598) for the Protein Lysine Methyltransferase SMYD2.
AID700456Selectivity ratio of IC50 for DOT1L to IC50 for human SMYD22012European journal of medicinal chemistry, Oct, Volume: 56Oncoepigenomics: making histone lysine methylation count.
AID1234082Inhibition of SMYD2 in human A549 cells assessed as reduction of p53K370me1 level at 10 uM after 18 hrs relative to control2015ACS medicinal chemistry letters, Jun-11, Volume: 6, Issue:6
Discovery of A-893, A New Cell-Active Benzoxazinone Inhibitor of Lysine Methyltransferase SMYD2.
AID1199199Selectivity ratio of IC50 for EZH2 (unknown origin) to IC50 for recombinant human full-length SMYD2 (1 to 433)2015Journal of medicinal chemistry, Feb-26, Volume: 58, Issue:4
Selective inhibitors of protein methyltransferases.
AID1234041Inhibition of SMYD2 (unknown origin) using biotinylated GSRAHSSHLKSKKGQSTSRH as substrate assessed as incorporation of tritium labeled methyl group from [3H]-SAM to biotinylated peptide substrate after 40 mins by scintillation proximity assay2015ACS medicinal chemistry letters, Jun-11, Volume: 6, Issue:6
Discovery of A-893, A New Cell-Active Benzoxazinone Inhibitor of Lysine Methyltransferase SMYD2.
AID1234042Competitive inhibition of SMYD2 (unknown origin) after 40 mins by scintillation proximity assay in presence of biotinylated GSRAHSSHLKSKKGQSTSRH substrate2015ACS medicinal chemistry letters, Jun-11, Volume: 6, Issue:6
Discovery of A-893, A New Cell-Active Benzoxazinone Inhibitor of Lysine Methyltransferase SMYD2.
AID1199196Selectivity ratio of IC50 for G9a (unknown origin) to IC50 for recombinant human full-length SMYD2 (1 to 433)2015Journal of medicinal chemistry, Feb-26, Volume: 58, Issue:4
Selective inhibitors of protein methyltransferases.
AID1234086Selectivity ratio of IC50 for EZH2 (unknown origin) to IC50 for recombinant full-length human SMYD2 (1 to 433)2015ACS medicinal chemistry letters, Jun-11, Volume: 6, Issue:6
Discovery of A-893, A New Cell-Active Benzoxazinone Inhibitor of Lysine Methyltransferase SMYD2.
AID1199198Selectivity ratio of IC50 for SETD7 (unknown origin) to IC50 for recombinant human full-length SMYD2 (1 to 433)2015Journal of medicinal chemistry, Feb-26, Volume: 58, Issue:4
Selective inhibitors of protein methyltransferases.
AID1308098Inhibition of SMYD2 (unknown origin) expressed in Escherichia coli BL21 (DE3) using Biotinaminohexanoyl-GSRAHSSHLKSKKGQSTSRH as substrate after 75 mins by scintillation proximity assay2016Journal of medicinal chemistry, 05-26, Volume: 59, Issue:10
Discovery and Characterization of a Highly Potent and Selective Aminopyrazoline-Based in Vivo Probe (BAY-598) for the Protein Lysine Methyltransferase SMYD2.
AID1887905Antiproliferative activity against human MDA-MB-231 cells assessed as inhibition of cell growth incubated for 72 hrs by CellTiter-Glo luminescent cell viability assay2022European journal of medicinal chemistry, Jan-05, Volume: 227Positioning of an unprecedented 1,5-oxaza spiroquinone scaffold into SMYD2 inhibitors in epigenetic space.
AID1234088Selectivity ratio of IC50 for G9a (unknown origin) to IC50 for recombinant full-length human SMYD2 (1 to 433)2015ACS medicinal chemistry letters, Jun-11, Volume: 6, Issue:6
Discovery of A-893, A New Cell-Active Benzoxazinone Inhibitor of Lysine Methyltransferase SMYD2.
AID700455Selectivity ratio of IC50 for GLP to IC50 for human SMYD22012European journal of medicinal chemistry, Oct, Volume: 56Oncoepigenomics: making histone lysine methylation count.
AID1234083Inhibition of recombinant full-length human SMYD2 (1 to 433) expressed in Escherichia coli BL21Star(DE3) cells using p53 peptide as substrate after 90 mins by scintillation proximity assay in presence of [3H]-SAM2015ACS medicinal chemistry letters, Jun-11, Volume: 6, Issue:6
Discovery of A-893, A New Cell-Active Benzoxazinone Inhibitor of Lysine Methyltransferase SMYD2.
AID1234089Selectivity ratio of IC50 for SET7/9 (unknown origin) to IC50 for recombinant full-length human SMYD2 (1 to 433)2015ACS medicinal chemistry letters, Jun-11, Volume: 6, Issue:6
Discovery of A-893, A New Cell-Active Benzoxazinone Inhibitor of Lysine Methyltransferase SMYD2.
AID1234087Selectivity ratio of IC50 for GLP (unknown origin) to IC50 for recombinant full-length human SMYD2 (1 to 433)2015ACS medicinal chemistry letters, Jun-11, Volume: 6, Issue:6
Discovery of A-893, A New Cell-Active Benzoxazinone Inhibitor of Lysine Methyltransferase SMYD2.
AID1308099Inhibition of N-terminal 2xc-myc-tagged human SMYD2 transfected in human MDA-MB-231 cells assessed as reduction in AHNAK methylation after 72 hrs by ICW assay2016Journal of medicinal chemistry, 05-26, Volume: 59, Issue:10
Discovery and Characterization of a Highly Potent and Selective Aminopyrazoline-Based in Vivo Probe (BAY-598) for the Protein Lysine Methyltransferase SMYD2.
AID1199195Selectivity ratio of IC50 for SMYD3 (unknown origin) to IC50 for recombinant human full-length SMYD2 (1 to 433)2015Journal of medicinal chemistry, Feb-26, Volume: 58, Issue:4
Selective inhibitors of protein methyltransferases.
AID1845921Competitive inhibition of SMYD2 (unknown origin) assessed as dissociation constant2021European journal of medicinal chemistry, Mar-05, Volume: 213HIV latency reversal agents: A potential path for functional cure?
AID1199200Selectivity ratio of IC50 for DOT1L (unknown origin) to IC50 for recombinant human full-length SMYD2 (1 to 433)2015Journal of medicinal chemistry, Feb-26, Volume: 58, Issue:4
Selective inhibitors of protein methyltransferases.
AID700454Selectivity ratio of IC50 for G9a to IC50 for human SMYD22012European journal of medicinal chemistry, Oct, Volume: 56Oncoepigenomics: making histone lysine methylation count.
AID1234079Inhibition of SMYD2 in human A549 cells assessed as reduction of p53K370me1 to overall p53 ratio at 10 uM after 18 hrs2015ACS medicinal chemistry letters, Jun-11, Volume: 6, Issue:6
Discovery of A-893, A New Cell-Active Benzoxazinone Inhibitor of Lysine Methyltransferase SMYD2.
AID1863573Binding affinity to full length human SMYD2 (1 to 433 residues) expressed in Escherichia coli strain BL21 (DE3) by ITC analysis2022Journal of medicinal chemistry, 08-11, Volume: 65, Issue:15
Protein Lysine Methyltransferase SMYD2: A Promising Small Molecule Target for Cancer Therapy.
AID1199193Inhibition of recombinant human full-length SMYD2 (1 to 433) using biotin-aminohexanoyl GSRAHSSHLKSKKGQSTSRH as substrate after 75 mins by AlphaScreen assay2015Journal of medicinal chemistry, Feb-26, Volume: 58, Issue:4
Selective inhibitors of protein methyltransferases.
AID1887903Inhibition of SMYD2 (unknown origin) using 3H-SAM as substrate incubated for 1 hr by filter binding method2022European journal of medicinal chemistry, Jan-05, Volume: 227Positioning of an unprecedented 1,5-oxaza spiroquinone scaffold into SMYD2 inhibitors in epigenetic space.
AID1234084Selectivity ratio of IC50 for SMYD3 (unknown origin) to IC50 for recombinant full-length human SMYD2 (1 to 433)2015ACS medicinal chemistry letters, Jun-11, Volume: 6, Issue:6
Discovery of A-893, A New Cell-Active Benzoxazinone Inhibitor of Lysine Methyltransferase SMYD2.
AID1234081Upregulation of p53 protein level in human A549 cells at 10 uM after 18 hrs relative to control2015ACS medicinal chemistry letters, Jun-11, Volume: 6, Issue:6
Discovery of A-893, A New Cell-Active Benzoxazinone Inhibitor of Lysine Methyltransferase SMYD2.
AID1234085Selectivity ratio of IC50 for DOT1L (unknown origin) to IC50 for recombinant full-length human SMYD2 (1 to 433)2015ACS medicinal chemistry letters, Jun-11, Volume: 6, Issue:6
Discovery of A-893, A New Cell-Active Benzoxazinone Inhibitor of Lysine Methyltransferase SMYD2.
AID1887934Induction of apoptosis in HEK293 cells assessed as increase in cleaved PARP level at 0.0195 to 10 uM incubated for 24 hrs by immunoblot analysis2022European journal of medicinal chemistry, Jan-05, Volume: 227Positioning of an unprecedented 1,5-oxaza spiroquinone scaffold into SMYD2 inhibitors in epigenetic space.
AID1308097Inhibition of full length 6xHis-tagged SMYD2 (unknown origin) expressed in Escherichia coli using Btn-Ahx GSRAHSSHLKSKKGQSTSRH-amide as substrate after 30 mins in presence 3H-SAM of by scintillation proximity assay2016Journal of medicinal chemistry, 05-26, Volume: 59, Issue:10
Discovery and Characterization of a Highly Potent and Selective Aminopyrazoline-Based in Vivo Probe (BAY-598) for the Protein Lysine Methyltransferase SMYD2.
AID1863576Inhibition of FLAG-tagged SMYD2 (unknown origin) expressed in human U2OS cells mediated intracellular p53 methylation incubated for 24 hrs using p53 as substrate by immunofluorescence analysis2022Journal of medicinal chemistry, 08-11, Volume: 65, Issue:15
Protein Lysine Methyltransferase SMYD2: A Promising Small Molecule Target for Cancer Therapy.
AID700453Selectivity ratio of IC50 for SET7/9 to IC50 for human SMYD22012European journal of medicinal chemistry, Oct, Volume: 56Oncoepigenomics: making histone lysine methylation count.
AID700459Selectivity ratio of IC50 for SMYD3 to IC50 for human SMYD22012European journal of medicinal chemistry, Oct, Volume: 56Oncoepigenomics: making histone lysine methylation count.
AID1199197Selectivity ratio of IC50 for GLP (unknown origin) to IC50 for recombinant human full-length SMYD2 (1 to 433)2015Journal of medicinal chemistry, Feb-26, Volume: 58, Issue:4
Selective inhibitors of protein methyltransferases.
AID700452Competitive binding affinity to full length human SMYD2 amino acid 1 to 433 expressed in Escherichia coli BL21 (DE3) after 90 mins by radioactive filter-binding assay in presence of P53 peptide2012European journal of medicinal chemistry, Oct, Volume: 56Oncoepigenomics: making histone lysine methylation count.
AID700460Inhibition of full length human SMYD2 amino acid 1 to 433 expressed in Escherichia coli BL21 (DE3) using Biotinaminohexanoyl- GSRAHSSHLKSKKGQSTSRH as substrate after 75 mins by AlphaScreen assay2012European journal of medicinal chemistry, Oct, Volume: 56Oncoepigenomics: making histone lysine methylation count.
AID1199194Binding affinity to recombinant human full-length SMYD2 (1 to 433) by ITC analysis2015Journal of medicinal chemistry, Feb-26, Volume: 58, Issue:4
Selective inhibitors of protein methyltransferases.
AID1863574Inhibition of full length human SMYD2 (1 to 433 residues) expressed in Escherichia coli strain BL21 (DE3) using p53 (361 to 380 residues) and [3H]-SAM as substrate incubated for 90 mins by SPA assay2022Journal of medicinal chemistry, 08-11, Volume: 65, Issue:15
Protein Lysine Methyltransferase SMYD2: A Promising Small Molecule Target for Cancer Therapy.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (11)

TimeframeStudies, This Drug (%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's7 (63.64)24.3611
2020's4 (36.36)2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Market Indicators

Research Demand Index: 33.22

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 moderate demand-to-supply ratio for research on this compound.

MetricThis Compound (vs All)
Research Demand Index33.22 (24.57)
Research Supply Index2.48 (2.92)
Research Growth Index4.69 (4.65)
Search Engine Demand Index38.04 (26.88)
Search Engine Supply Index2.00 (0.95)

This Compound (33.22)

All Compounds (24.57)

Study Types

Publication TypeThis drug (%)All Drugs (%)
Trials0 (0.00%)5.53%
Reviews3 (27.27%)6.00%
Case Studies0 (0.00%)4.05%
Observational0 (0.00%)0.25%
Other8 (72.73%)84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]
SubstanceRelationship StrengthStudiesTrialsClassesRoles
beta-alanine
[no description available]		3.0640amino acid zwitterion;
beta-amino acid		agonist;
fundamental metabolite;
human metabolite;
inhibitor;
neurotransmitter
4-(dimethylamino)-n-(7-(hydroxyamino)-7-oxoheptyl)benzamide
4-(dimethylamino)-N-(7-(hydroxyamino)-7-oxoheptyl)benzamide: structure in first source. 4-(dimethylamino)-N-[7-(hydroxyamino)-7-oxoheptyl]benzamide : A benzamide resulting from the formal condensation of the carboxy group of 4-(dimethylamino)benzoic acid with the amino group of 7-amino-N-hydroxyheptanamide. It is a potent inhibitor of histone deacetylases and induces cell cycle arrest and apoptosis in several human cancer cell lines.		3.4110benzamides;
hydroxamic acid;
secondary carboxamide;
tertiary amino compound		antineoplastic agent;
apoptosis inducer;
EC 3.5.1.98 (histone deacetylase) inhibitor
vorinostat
Vorinostat: A hydroxamic acid and anilide derivative that acts as a HISTONE DEACETYLASE inhibitor. It is used in the treatment of CUTANEOUS T-CELL LYMPHOMA and SEZARY SYNDROME.. vorinostat : A dicarboxylic acid diamide comprising suberic (octanedioic) acid coupled to aniline and hydroxylamine. A histone deacetylase inhibitor, it is marketed under the name Zolinza for the treatment of cutaneous T cell lymphoma (CTCL).		3.4110dicarboxylic acid diamide;
hydroxamic acid		antineoplastic agent;
apoptosis inducer;
EC 3.5.1.98 (histone deacetylase) inhibitor
lysine
Lysine: An essential amino acid. It is often added to animal feed.. lysine : A diamino acid that is caproic (hexanoic) acid bearing two amino substituents at positions 2 and 6.. L-lysine : An L-alpha-amino acid; the L-isomer of lysine.		2.3110aspartate family amino acid;
L-alpha-amino acid zwitterion;
L-alpha-amino acid;
lysine;
organic molecular entity;
proteinogenic amino acid		algal metabolite;
anticonvulsant;
Escherichia coli metabolite;
human metabolite;
micronutrient;
mouse metabolite;
nutraceutical;
plant metabolite;
Saccharomyces cerevisiae metabolite
gliotoxin
Gliotoxin: A fungal toxin produced by various species of Trichoderma, Gladiocladium fimbriatum, Aspergillus fumigatus, and Penicillium. It is used as an immunosuppressive agent.. gliotoxin : A pyrazinoindole with a disulfide bridge spanning a dioxo-substituted pyrazine ring; mycotoxin produced by several species of fungi.		3.1710dipeptide;
organic disulfide;
organic heterotetracyclic compound;
pyrazinoindole		antifungal agent;
EC 2.5.1.58 (protein farnesyltransferase) inhibitor;
immunosuppressive agent;
mycotoxin;
proteasome inhibitor
azacitidine
Azacitidine: A pyrimidine analogue that inhibits DNA methyltransferase, impairing DNA methylation. It is also an antimetabolite of cytidine, incorporated primarily into RNA. Azacytidine has been used as an antineoplastic agent.. 5-azacytidine : An N-glycosyl-1,3,5-triazine that is 4-amino-1,3,5-triazin-2(1H)-one substituted by a beta-D-ribofuranosyl residue via an N-glycosidic linkage. An antineoplastic agent, it is used in the treatment of myeloid leukaemia.		3.4110N-glycosyl-1,3,5-triazine;
nucleoside analogue		antineoplastic agent
staurosporine
[no description available]		2.4110indolocarbazole alkaloid;
organic heterooctacyclic compound		apoptosis inducer;
bacterial metabolite;
EC 2.7.11.13 (protein kinase C) inhibitor;
geroprotector
indolactam v
indolactam V: only the (-)-isomer of indolactam V showed carcinogenic activity; structure given in first source		3.4110indoles
nsc 663284
NSC 663284: structure in first source		2.1110quinolone
trichostatin a
trichostatin A: chelates zinc ion in the active site of histone deacetylases, resulting in preventing histone unpacking so DNA is less available for transcription; do not confuse with TRICHOSANTHIN which is a protein; found in STREPTOMYCES		3.4110antibiotic antifungal agent;
hydroxamic acid;
trichostatin		bacterial metabolite;
EC 3.5.1.98 (histone deacetylase) inhibitor;
geroprotector
12-deoxyphorbol 13-acetate
[no description available]		3.4110phorbol estermetabolite
5-carboxy-8-hydroxyquinoline
5-carboxy-8-hydroxyquinoline: a JmjC histone demethylase inhibitor; structure in first source		3.1710quinolines
verticillins
verticillins: 3 antibiotics isolated from imperfect fungus Verticillium: verticillin A, verticillin B (mono-3-hydroxymethyl analog of verticillin A), & verticillin C (differs from verticillin B in that 1 of dioxopiperazine rings has a trisulfide rather than a disulfide bridge; active against gram-positive bacteria & mycobacteria but not against gram-negative bacteria & fungi; RN given refers to cpd with unknown MF; structure (verticillins A & B))		3.1710
ellagic acid
[no description available]		2.1110catechols;
cyclic ketone;
lactone;
organic heterotetracyclic compound;
polyphenol		antioxidant;
EC 1.14.18.1 (tyrosinase) inhibitor;
EC 2.3.1.5 (arylamine N-acetyltransferase) inhibitor;
EC 2.4.1.1 (glycogen phosphorylase) inhibitor;
EC 2.5.1.18 (glutathione transferase) inhibitor;
EC 2.7.1.127 (inositol-trisphosphate 3-kinase) inhibitor;
EC 2.7.1.151 (inositol-polyphosphate multikinase) inhibitor;
EC 2.7.4.6 (nucleoside-diphosphate kinase) inhibitor;
EC 2.7.7.7 (DNA-directed DNA polymerase) inhibitor;
EC 5.99.1.2 (DNA topoisomerase) inhibitor;
EC 5.99.1.3 [DNA topoisomerase (ATP-hydrolysing)] inhibitor;
food additive;
fungal metabolite;
geroprotector;
plant metabolite;
skin lightening agent
bvt.948
[no description available]		2.1110
belinostat
[no description available]		3.4110hydroxamic acid;
olefinic compound;
sulfonamide		antineoplastic agent;
EC 3.5.1.98 (histone deacetylase) inhibitor
panobinostat
Panobinostat: An indole and hydroxamic acid derivative that acts as a HISTONE DEACETYLASE inhibitor. It is used as an antineoplastic agent in combination with BORTEZOMIB and DEXAMETHASONE for the treatment of MULTIPLE MYELOMA.. panobinostat : A hydroxamic acid obtained by formal condensation of the carboxy group of (2E)-3-[4-({[2-(2-methylindol-3-yl)ethyl]amino}methyl)phenyl]prop-2-enoic acid with the amino group of hydroxylamine. A histone deacetylase inhibitor used (as its lactate salt) in combination with bortezomib and dexamethasone for the treatment of multiple myeloma.		3.4110cinnamamides;
hydroxamic acid;
methylindole;
secondary amino compound		angiogenesis modulating agent;
antineoplastic agent;
EC 3.5.1.98 (histone deacetylase) inhibitor
n-(2-amino-5-fluorobenzyl)-4-(n-(pyridine-3-acrylyl)aminomethyl)benzamide
[no description available]		3.4110
cl 075
[no description available]		3.4110
chetomin
[no description available]		3.1710
bi 2536
[no description available]		3.4110
bix 01294
[no description available]		4.4330piperidines
unc 0638
UNC 0638: inhibits lysine methyltransferases G9a and GLP; structure in first source		4.1520quinazolines
jq1 compound
[no description available]		3.4110carboxylic ester;
organochlorine compound;
tert-butyl ester;
thienotriazolodiazepine		angiogenesis inhibitor;
anti-inflammatory agent;
antineoplastic agent;
apoptosis inducer;
bromodomain-containing protein 4 inhibitor;
cardioprotective agent;
ferroptosis inducer
epz004777
[no description available]		3.5920N-glycosyl compound
epz-5676
[no description available]		2.11105'-deoxyribonucleoside
epz005687
EPZ005687: inhibits EZH2 protein; structure in first source		2.1110indazoles
epz-6438
tazemetostat: a histone methyltransferase EZH2 inhibitor with antineoplastic activity		3.6820
gsk-2816126
GSK-2816126: inhibits EZH2 methyltransferase; structure in first source		2.1110piperazines;
pyridines
gsk343
GSK343: an EZH2 methyltransferase inhibitor. GSK343 : A member of the class of indazoles that is 1-isopropyl-1H-indazole-4-carboxamide in which the nitrogen of the carboxamide group is substituted by a (6-methyl-2-oxo-4-propyl-1,2-dihydropyridin-3-yl)methyl group and in which the indazole ring is substituted at position 6 by a 2-(4-methylpiperazin-1-yl)pyridin-4-yl group. A highly potent and selective EZH2 inhibitor (IC50 = 4 nM).		3.4110aminopyridine;
indazoles;
N-alkylpiperazine;
N-arylpiperazine;
pyridone;
secondary carboxamide		antineoplastic agent;
apoptosis inducer;
EC 2.1.1.43 (enhancer of zeste homolog 2) inhibitor
2-methoxy-n-(3-methyl-2-oxo-1,2,3,4-tetrahydroquinazolin-6-yl)benzenesulfonamide
2-methoxy-N-(3-methyl-2-oxo-1,2,3,4-tetrahydroquinazolin-6-yl)benzenesulfonamide: a probe for bromo and extra C-terminal domain proteins; structure in first source		3.4110quinazolines
(r)-pfi-2
(R)-PFI-2: a potent and selective inhibitor of SETD7 methyltransferase; structure in first source		2.1110
lly-507
LLY-507: inhibits methyltransferase SMYD2; structure in first source. LLY-507 : A secondary carboxamide resulting from the formal condensation of the carboxy group of 5-cyano-2'-{4-[2-(3-methyl-1H-indol-1-yl)ethyl]piperazin-1-yl}[biphenyl]-3-carboxylic acid with the amino group of 3-(pyrrolidin-1-yl)propan-1-amine. It is a potent and selective inhibitor of SMYD2 and inhibits the ability of SMYD2 to methylate p53. It serves as a valuable chemical probe to aid in the dissection of SMYD2 function in cancer and other biological processes.		4.3750
rvx 208
apabetalone: a bromodomain and extra-terminal domain protein (BET) inhibitor; prevents interactions between BET proteins and acetyl-lysine residues on histone tails to modify epigenetic regulation		3.4110
ConditionIndicatedRelationship StrengthStudiesTrials
Cancer of Esophagus
[description not available]		02.0610
Esophageal Neoplasms
Tumors or cancer of the ESOPHAGUS.		02.0610
Benign Neoplasms
[description not available]		03.9420
Neoplasms
New abnormal growth of tissue. Malignant neoplasms show a greater degree of anaplasia and have the properties of invasion and metastasis, compared to benign neoplasms.		03.9420
HIV Coinfection
[description not available]		03.2310
HIV Infections
Includes the spectrum of human immunodeficiency virus infections that range from asymptomatic seropositivity, thru AIDS-related complex (ARC), to acquired immunodeficiency syndrome (AIDS).		03.2310
Experimental Mammary Neoplasms
[description not available]		02.4110
Cirrhosis
[description not available]		02.3110
Ureteral Obstruction
Blockage in any part of the URETER causing obstruction of urine flow from the kidney to the URINARY BLADDER. The obstruction may be congenital, acquired, unilateral, bilateral, complete, partial, acute, or chronic. Depending on the degree and duration of the obstruction, clinical features vary greatly such as HYDRONEPHROSIS and obstructive nephropathy.		02.3110
Fibrosis
Any pathological condition where fibrous connective tissue invades any organ, usually as a consequence of inflammation or other injury.		02.3110
Kidney Diseases
Pathological processes of the KIDNEY or its component tissues.		02.3110
Cyst
[description not available]		02.1510
ADPKD
[description not available]		02.1510
Polycystic Kidney, Autosomal Dominant
Kidney disorders with autosomal dominant inheritance and characterized by multiple CYSTS in both KIDNEYS with progressive deterioration of renal function.		02.1510
Disease Exacerbation
[description not available]		02.1710
ER-Negative PR-Negative HER2-Negative Breast Cancer
[description not available]		02.1710
Triple Negative Breast Neoplasms
Breast neoplasms that do not express ESTROGEN RECEPTORS; PROGESTERONE RECEPTORS; and do not overexpress the NEU RECEPTOR/HER-2 PROTO-ONCOGENE PROTEIN.		02.1710