Sinefungin derivatives as inhibitors and structure probes of protein lysine methyltransferase SETD2
about
Combating the epigenome: epigenetic drugs against non-Hodgkin's lymphomaStructure of the Catalytic Domain of EZH2 Reveals Conformational Plasticity in Cofactor and Substrate Binding Sites and Explains Oncogenic MutationsStructural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2Discovery of a selective, substrate-competitive inhibitor of the lysine methyltransferase SETD8Chemical Proteomic Profiling of Human MethyltransferasesMolecular basis for oncohistone H3 recognition by SETD2 methyltransferaseAnalogues of the Natural Product Sinefungin as Inhibitors of EHMT1 and EHMT2.An orally bioavailable chemical probe of the Lysine Methyltransferases EZH2 and EZH1Structure-activity relationship studies of SETD8 inhibitors.Recent progress in the discovery of small-molecule inhibitors of the HMT EZH2 for the treatment of cancer.S-adenosyl-homocysteine is a weakly bound inhibitor for a flaviviral methyltransferaseExploiting an allosteric binding site of PRMT3 yields potent and selective inhibitors.Selective inhibitors of protein methyltransferasesThe Human Mixed Lineage Leukemia 5 (MLL5), a Sequentially and Structurally Divergent SET Domain-Containing Protein with No Intrinsic Catalytic Activity.Development of Chemical Tools to Monitor and Control Isoaspartyl Peptide Methyltransferase Activity.Kinetic isotope effects reveal early transition state of protein lysine methyltransferase SET8.Two Loops Undergoing Concerted Dynamics Regulate the Activity of the ASH1L Histone Methyltransferase.A direct label-free MALDI-TOF mass spectrometry based assay for the characterization of inhibitors of protein lysine methyltransferases.Transition state for the NSD2-catalyzed methylation of histone H3 lysine 36Small Molecule Inhibitors of Protein Arginine Methyltransferases.Discovery of an in vivo chemical probe of the lysine methyltransferases G9a and GLP.Molecular basis for the role of oncogenic histone mutations in modulating H3K36 methylation.Small molecule epigenetic inhibitors targeted to histone lysine methyltransferases and demethylases.SAM/SAH Analogs as Versatile Tools for SAM-Dependent Methyltransferases.Inhibitors of protein methyltransferases as chemical tools.Inhibitors of Protein Methyltransferases and Demethylases.Nature's combinatorial biosynthesis and recently engineered production of nucleoside antibiotics in Streptomyces.Structure/Function Analysis of Recurrent Mutations in SETD2 Protein Reveals a Critical and Conserved Role for a SET Domain Residue in Maintaining Protein Stability and Histone H3 Lys-36 TrimethylationFactors affecting the persistence of drug-induced reprogramming of the cancer methylome.H3K36 methyltransferases as cancer drug targets: rationale and perspectives for inhibitor developmentInhibitors of enzymes catalyzing modifications to histone lysine residues: structure, function and activity.Resveratrol-salicylate derivatives as selective DNMT3 inhibitors and anticancer agents.Trimethylation of histone H3 lysine 36 by human methyltransferase PRDM9 proteinDynamic behavior of the post-SET loop region of NSD1: Implications for histone binding and drug development.Kinetic Isotope Effects and Transition State Structure for Human Phenylethanolamine N-Methyltransferase.Structural basis of arginine asymmetrical dimethylation by PRMT6.Mrg15 stimulates Ash1 H3K36 methyltransferase activity and facilitates Ash1 Trithorax group protein function in Drosophila.Investigation of the inhibitors of histone-lysine N-methyltransferase SETD2 for acute lymphoblastic leukaemia from traditional Chinese medicine.Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition.Roles of H3K36-specific histone methyltransferases in transcription: antagonizing silencing and safeguarding transcription fidelity
P2860
Q26851166-35513C1D-4093-48D1-A67C-4F6A8355C202Q27681082-540960F3-7E75-468E-A255-CE8FA3AA86C7Q27702306-AE8BCC5B-A3DF-4293-9EC9-2546A1B8A9D3Q28244062-41EA2715-5E5D-4582-AD43-67B4244122A5Q28821490-B2E490C4-F059-47FA-80EC-DC88D5154F84Q30794597-6E2713F5-F163-4D42-889D-ED190C180F04Q33636498-928082D1-2508-4313-AAE6-A169B5FE6E39Q34341058-A71D7B22-EE95-4B3E-9954-1869BB7A4143Q34782773-C8FFC231-EF71-4A41-B075-11B9D757847AQ34991896-03823897-4E1E-45C2-8ACF-F06EBCAF6E7CQ35018619-E6AA9698-472B-4775-84FE-0D8C3F47D1EDQ35057637-6D6D1B11-6C1B-462B-BCC7-E67CAE14F380Q35135783-0A825F06-9E47-4A71-8C34-D03A57A9231BQ36182103-92D5CE63-8C7E-43A3-BBC5-89E62F4C5AEFQ36217070-D7097259-19E6-44AA-BC9F-E8B10DFD6CC5Q36219705-EB1CFF1D-BF46-48BB-BC98-2F7594CB5014Q36332254-07218762-8C63-45FB-A3FF-3AE2021561B2Q36340686-F29427B7-7058-4879-894C-DC56D6779A22Q36563132-7961F255-E4EB-4434-955C-FA5DEC232F9EQ37056442-3C83EF11-D92B-4E07-A861-0194F4C00211Q37432733-D42A3454-7B0E-4C27-95C8-891B6894EF48Q37678797-CBEB64B1-9858-4716-9364-0ACB1A56C78BQ38132808-1E19EF94-4842-4A1D-AB45-E65132E3417BQ38625953-7FD0921F-F9A0-4FFC-B18A-71F23C6AAA60Q38662560-0B94822E-62CE-4D5C-B7D8-0C621814CDBBQ38740496-C21CEB00-1D90-43E0-B6E4-21C32C86569FQ38750640-A505B57B-0B39-40AB-AB77-C41E74280078Q38751593-0E17575C-523B-4109-B482-5C7E2BEB2475Q38777889-4CDFB70E-9FAD-47BA-A8EB-70DAEDB4728AQ38829055-A97F56F2-E2DE-4992-B19C-B491DBA2CCC9Q38833038-C77701B2-746B-4621-91CF-3484E2BEE90EQ38859365-DF8E7167-85CA-4B45-9EA0-1D99C144C75FQ39007308-8F7A298E-D562-4619-992E-CDE130BC9EDBQ40413518-88C3D1E4-1B47-45D5-AC9E-2FA1DC5D1DC9Q41358452-CEB22668-8D76-48DD-BDDA-97BB91467297Q41633725-6E86E725-5F5E-4806-8570-32E389E4E2CAQ45754918-15FFFEEB-37C0-48A0-9C44-E2A0357274D0Q47307503-4B067B1B-EAB2-461A-BA48-1B02A2F228A1Q55283269-CC6363ED-5028-4E0B-BA23-E89180EA2D28Q57498154-E9BFF1FC-8468-4884-B7C5-D837E6F50F4F
P2860
Sinefungin derivatives as inhibitors and structure probes of protein lysine methyltransferase SETD2
description
2012 nî lūn-bûn
@nan
2012 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Sinefungin derivatives as inhi ...... lysine methyltransferase SETD2
@ast
Sinefungin derivatives as inhi ...... lysine methyltransferase SETD2
@en
Sinefungin derivatives as inhi ...... lysine methyltransferase SETD2
@en-gb
Sinefungin derivatives as inhi ...... lysine methyltransferase SETD2
@nl
type
label
Sinefungin derivatives as inhi ...... lysine methyltransferase SETD2
@ast
Sinefungin derivatives as inhi ...... lysine methyltransferase SETD2
@en
Sinefungin derivatives as inhi ...... lysine methyltransferase SETD2
@en-gb
Sinefungin derivatives as inhi ...... lysine methyltransferase SETD2
@nl
altLabel
Sinefungin Derivatives as Inhi ...... Lysine Methyltransferase SETD2
@en
prefLabel
Sinefungin derivatives as inhi ...... lysine methyltransferase SETD2
@ast
Sinefungin derivatives as inhi ...... lysine methyltransferase SETD2
@en
Sinefungin derivatives as inhi ...... lysine methyltransferase SETD2
@en-gb
Sinefungin derivatives as inhi ...... lysine methyltransferase SETD2
@nl
P2093
P2860
P50
P921
P3181
P356
P1476
Sinefungin derivatives as inhi ...... lysine methyltransferase SETD2
@en
P2093
Aiping Dong
Fengling Li
Glorymar Ibáñez
Jinrong Min
Maria F Amaya
Minkui Luo
Taraneh Hajian
P2860
P304
P3181
P356
10.1021/JA307060P
P407
P577
2012-10-31T00:00:00Z