Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294 - Wikidata - wikimedia - TriplyDB

Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294

Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294

http://www.wikidata.org/entity/Q27653816

about

Inhibition of G9a Histone Methyltransferase Converts Bone Marrow Mesenchymal Stem Cells to Cardiac Competent Progenitors Structural and Functional Analyses of a Conserved Hydrophobic Pocket of Flavivirus Methyltransferase Hypoxia-induced methylation of a pontin chromatin remodeling factor Structural genomics of histone tail recognition A chemical probe selectively inhibits G9a and GLP methyltransferase activity in cells Functional Role of G9a Histone Methyltransferase in Cancer Synthesis of lysine methyltransferase inhibitors Epigenomics of leukemia: from mechanisms to therapeutic applications Chemical probes of histone lysine methyltransferases Discovery of a 2,4-Diamino-7-aminoalkoxyquinazoline as a Potent and Selective Inhibitor of Histone Lysine Methyltransferase G9a Structural Biology of Human H3K9 Methyltransferases Adding a Lysine Mimic in the Design of Potent Inhibitors of Histone Lysine Methyltransferases Structural and biochemical studies of human lysine methyltransferase Smyd3 reveal the important functional roles of its post-SET and TPR domains and the regulation of its activity by DNA binding An Analog of BIX-01294 Selectively Inhibits a Family of Histone H3 Lysine 9 Jumonji Demethylases Histone lysine methyltransferases as anti-cancer targets for drug discovery Properly substituted analogues of BIX-01294 lose inhibition of G9a histone methyltransferase and gain selective anti-DNA methyltransferase 3A activity.Gain- and Loss-of-Function Mutations in the Breast Cancer Gene GATA3 Result in Differential Drug Sensitivity Polymyxins and quinazolines are LSD1/KDM1A inhibitors with unusual structural features Inhibition of H3K9me2 Reduces Hair Cell Regeneration after Hair Cell Loss in the Zebrafish Lateral Line by Down-Regulating the Wnt and Fgf Signaling Pathways.Assay development for histone methyltransferases.Inhibition of H3K9 methyltransferases G9a/GLP prevents ototoxicity and ongoing hair cell death.The class I-specific HDAC inhibitor MS-275 modulates the differentiation potential of mouse embryonic stem cells.Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives A miniaturized screen for inhibitors of Jumonji histone demethylases.Histone lysine methyltransferase G9a is a novel epigenetic target for the treatment of hepatocellular carcinoma.Accessing protein methyltransferase and demethylase enzymology using microfluidic capillary electrophoresis Essential role of the histone methyltransferase G9a in cocaine-induced plasticity.Discovery of first-in-class reversible dual small molecule inhibitors against G9a and DNMTs in hematological malignancies.Epigenetic regulation of epithelial-mesenchymal transition Coordinated chromatin control: structural and functional linkage of DNA and histone methylation.A case study in cross-talk: the histone lysine methyltransferases G9a and GLP.A chemiluminescence-based method for identification of histone lysine methyltransferase inhibitors.Mixed lineage leukemia: a structure-function perspective of the MLL1 protein.Methods for Activity Analysis of the Proteins that Regulate Histone Methylation Protein lysine methyltransferase G9a inhibitors: design, synthesis, and structure activity relationships of 2,4-diamino-7-aminoalkoxy-quinazolines.Perspectives on the discovery of small-molecule modulators for epigenetic processes.Current limitations and future opportunities for epigenetic therapies.Development of diaminoquinazoline histone lysine methyltransferase inhibitors as potent blood-stage antimalarial compounds The hypoxia-inducible epigenetic regulators Jmjd1a and G9a provide a mechanistic link between angiogenesis and tumor growth.Microscale thermophoresis quantifies biomolecular interactions under previously challenging conditions

P2860

Q22306435-4C6C33EC-F210-4CF4-8ED3-EBD9EF5E840A Q24289239-E90C3650-908F-41CD-8593-D104AC257354 Q24614835-BC5079DA-B0B1-4052-B9BE-BF569168E3DC Q24634351-05FF56FB-CB7E-4C0D-A42E-61D3BE3B732B Q24635322-15693BD5-7475-4943-9099-3849C85FB7AF Q26781247-B802D776-9703-4FD7-8F4B-2E0908C85050 Q26799953-BE606264-018F-4DDB-9ED5-6B48324244CF Q26823403-299BE2C2-932E-40B9-8874-D64C0331089A Q26829218-44F664B7-8C45-4837-8ED5-7849B974D3ED Q27658070-23F349D2-B269-4B81-B488-6BC9DF1C5E52 Q27659033-E7F42BCB-1223-4EAF-A839-A4459541DD5D Q27661108-D3F63123-9CA6-488C-9F19-7AC16B9DEC84 Q27666725-4DF414F3-E1AA-4662-9676-18D3C49BA2CD Q27676635-4E0DFA1E-896E-49C8-9648-6405A20595A3 Q28076288-A72790AD-243B-4D8C-B910-FF6E5C6F455C Q28538629-6F5F8887-BCA7-4990-91A3-76918B15F432 Q28553888-D44C2765-BD49-4863-843A-20CFABED7A4F Q28595992-A5CC0FC5-DD6F-4EC6-86F2-CD595BF00CB1 Q30381443-AA311837-1ADA-4868-A4BD-97F7AA499317 Q30439019-E388E694-43B3-4AEA-9A45-01EA68784A40 Q30542318-2F8C930E-AF5F-41BC-8810-68A642C0CC87 Q30551120-3F2B4C12-324E-4C7D-9B70-317A8E2AA2DE Q30570945-1207E42C-887A-4437-8517-F5213807B83C Q33525920-142633CA-80E2-475F-8126-4EF423A74487 Q33591514-BB833A75-D430-4766-AF57-0AAEEA463FE5 Q33640900-AA9178C4-50CA-43E8-81DD-7D1B41808422 Q33646214-9B1F5C15-A4DB-45F4-8C62-3AA2970871C8 Q33762936-C66126D4-5065-4A22-8637-675EAFD8D201 Q33764436-5D1BAB7A-BC16-43DC-B4B1-8B0B8FC2DDED Q33802703-A28708BE-90BC-4EC6-98A9-788A89E32265 Q33922397-3E55DF52-25B0-429A-A521-96E3A85EC3FE Q33938622-B1BD4357-3D85-4A00-89A2-565843FCA533 Q33943731-3C430329-635F-4865-896E-968EBB658549 Q34037729-535CDB8E-8500-4297-8F2B-65B265F0988E Q34059822-1753E8C6-C16F-4E77-9396-897B62F1B5D8 Q34185471-FAEB8B1C-4049-4598-B7CC-52456E4C1D11 Q34195077-0936D2D0-13B2-4CAB-B80B-6D473C3100D0 Q34254755-104EAEF9-C432-42E2-A9F6-A878A68E6960 Q34298049-D038A2DF-5AAF-4C93-88AF-1C5C71EA897C Q34319793-881D831F-4422-4F78-BD7F-F53424438359

P2860

Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294

http://www.wikidata.org/entity/Q27653816

description

2009 nî lūn-bûn

@nan

2009 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի մարտին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294

@ast

Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294

@en

Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294

@nl

type

label

Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294

@ast

Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294

@en

Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294

@nl

prefLabel

Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294

@ast

Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294

@en

Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294

@nl

P1433

Q27653816-DCFEDB19-ADDF-4538-B92B-E9FDCBCA88A3

P1476

Q27653816-7EFE7238-E523-476D-B0B3-98B60763F733

P2093

Q27653816-0317B7CF-D4BF-4C42-981B-24EE359CCE91

Q27653816-28F4C5CB-77FF-48D7-8AE5-0C233227F549

Q27653816-42837BFF-0C62-4D43-9E49-876223F9B885

Q27653816-576C59ED-4C9E-4F14-AD3E-F14291DBB871

Q27653816-B5310856-A92A-4AFF-B681-03CB74C22A90

Q27653816-C81DB2E5-313B-4432-9D05-6279B83B3EC9

Q27653816-C9E11A1E-2A72-4802-8AC7-35D6E658395C

P2860

Q27653816-363B6C4D-4486-4BBA-9627-427B40EE0727

Q27653816-3C509866-FF54-4DE4-AA5C-CDEC09D400E6

Q27653816-47610741-0E35-4942-90DF-0B96805317CF

Q27653816-4B202C9C-A153-4E1E-9544-D0ED05311B48

Q27653816-4E1BC08D-815D-4418-9759-67BD50C9FF93

Q27653816-4F5AE611-E9CE-4969-98E3-8B17F72D8DD2

Q27653816-50FC3805-8447-45BF-8002-1BE06B2B118B

Q27653816-5E76F449-FB3F-4914-A8D6-8241AF7514F2

Q27653816-679412D0-C791-4752-A594-F84C00C6B38B

Q27653816-6837B98C-3C2E-4839-B763-6EB46FD78FC6

P2888

Q27653816-A81CEED8-1EC9-4175-8788-0CDC825F5AAC

P304

Q27653816-9E3A604C-B3A9-49F0-825E-ED5F61E504DF

P31

Q27653816-9A5DF3EA-8AC0-45E8-9A5A-769CB593F840

P3181

Q27653816-F894AEE0-B66C-4E61-B43C-12EEC89AD6A9

P356

Q27653816-344AE96A-679F-4C77-8D27-7C124ACD1215

P433

Q27653816-54166A0B-B5D4-43A3-A7B0-066D95F637F0

P478

Q27653816-1BA50575-AB52-46D6-9A6C-189E563E8E34

P50

Q27653816-74F60406-7D7D-46D7-97C3-257B11E401A7

Q27653816-FB4373FA-09FC-487C-82E4-87989E10DA19

P577

Q27653816-904F8D43-820E-4B5E-9413-8F9F568AC5EE

P5875

Q27653816-DAD15D7B-967C-421F-857C-F3BC6D87FD71

P6179

Q27653816-8242C83F-2DD1-4331-A6CC-62ED94810365

P698

Q27653816-9CA9B979-2A4C-45CC-BBCC-E1FC30664F1B

P921

Q27653816-C103325B-88A6-480A-91F7-59AC94B253A7

P932

Q27653816-B73B2BA7-ABA0-4358-8A5E-450B57364A52

P3181

P356

P1433

Nature Structural & Molecular Biology

P1476

Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294

@en

P2093

Anup K Upadhyay

http://www.w3.org/2001/XMLSchema#string

Astrid Spannhoff

http://www.w3.org/2001/XMLSchema#string

James P Snyder

http://www.w3.org/2001/XMLSchema#string

Jin Liu

http://www.w3.org/2001/XMLSchema#string

Mark T Bedford

http://www.w3.org/2001/XMLSchema#string

Xiaodong Cheng

http://www.w3.org/2001/XMLSchema#string

Xing Zhang

http://www.w3.org/2001/XMLSchema#string

P2860

Regulation of p53 activity through lysine methylation

In vitro and in vivo analyses of a Phe/Tyr switch controlling product specificity of histone lysine methyltransferases

Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase

Structural basis for the product specificity of histone lysine methyltransferases

G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase

PRODRG: a tool for high-throughput crystallography of protein-ligand complexes

Likelihood-enhanced fast rotation functions

P2888

P304

312-317

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

1266956

http://www.w3.org/2001/XMLSchema#string

P356

10.1038/NSMB.1560

http://www.w3.org/2001/XMLSchema#string

P433

3

http://www.w3.org/2001/XMLSchema#string

P478

16

http://www.w3.org/2001/XMLSchema#string

P50

P577

2009-02-15T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

24012208

http://www.w3.org/2001/XMLSchema#string

P6179

1030525601

http://www.w3.org/2001/XMLSchema#string

P698

19219047

http://www.w3.org/2001/XMLSchema#string

P921

structural biology

P932

2676930

http://www.w3.org/2001/XMLSchema#string