Histone acetyltransferases: Rising ancient counterparts to protein kinases.
about
Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Structure and mechanism of non-histone protein acetyltransferase enzymesSynchronous recruitment of epigenetic modifiers to endotoxin synergistically activated Tnf-α gene in acute kidney injuryStructural Basis for Bacterial Quorum Sensing-mediated OxalogenesisMitochondrial protein acetylation as a cell-intrinsic, evolutionary driver of fat storage: chemical and metabolic logic of acetyl-lysine modificationsBiochemical characterization of Hpa2 and Hpa3, two small closely related acetyltransferases from Saccharomyces cerevisiae.Epigenetics in acute kidney injuryThe molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatDHistones: Controlling Tumor Signaling CircuitryMechanistic and structural analysis of Drosophila melanogaster arylalkylamine N-acetyltransferases.Readers, writers, and erasers: chromatin as the whiteboard of heart diseaseCompetitive inhibition can linearize dose-response and generate a linear rectifier.Mechanistic and Structural Analysis of a Drosophila melanogaster Enzyme, Arylalkylamine N-Acetyltransferase Like 7, an Enzyme That Catalyzes the Formation of N-Acetylarylalkylamides and N-Acetylhistamine.The promise and failures of epigenetic therapies for cancer treatmentEpigenetic alterations in acute kidney injury.An evolving understanding of nuclear receptor coregulator proteins.An integrated perspective and functional impact of the mitochondrial acetylome.Epigenetic pathway targets for the treatment of disease: accelerating progress in the development of pharmacological tools: IUPHAR Review 11.Histone modifications: Targeting head and neck cancer stem cells.Inhibition of different histone acetyltransferases (HATs) uncovers transcription-dependent and -independent acetylation-mediated mechanisms in memory formation.Impact of Epigenetic Dietary Components on Cancer through Histone Modifications.Molecular Basis for Histone Acetyltransferase Regulation by Binding Partners, Associated Domains, and Autoacetylation.Chemical Biology for Investigating Epigenetic Functions of Lysine Acetyltransferases (KATs).Multitarget Drugs: an Epigenetic Epiphany.Epigenetic modifications, chromatin distribution and TP53 transcription in a model of breast cancer progression.Lysine acetylome profiling uncovers novel histone deacetylase substrate proteins in Arabidopsis.Structure of p300 in complex with acyl-CoA variants.Discovery of Spiro Oxazolidinediones as Selective, Orally Bioavailable Inhibitors of p300/CBP Histone Acetyltransferases.Nucleic acid-mimicking coordination polymer for label-free fluorescent activity assay of histone acetyltransferases.
P2860
Q26823798-70E45969-3E20-4656-9B5B-FE68896EFEFDQ26996044-68E6BEFF-98E4-4269-9964-F96D5D91A1D4Q27310345-DBC73B0E-07CD-4480-9065-BA08E204A6FBQ27682068-21FB58C1-03C1-4AE1-B0A9-B66A34BF4A02Q27694582-F9F226AE-E384-4BCE-8FCF-B498405ED250Q27934711-D795A382-6C4F-464D-9D08-3837CE3AF5F6Q28080924-D9C3A260-E665-4438-9745-E930BFB16341Q28596566-DE3F103C-A821-4403-8373-EA60218AD5A1Q34109472-7F5F6C56-7170-4544-9C99-5CAB3E030163Q34731719-8E79A981-D0F4-4285-950C-E26FFA924489Q35234488-249814BD-55DB-492D-AB4C-5F1DA7BE0146Q36174818-7881E9D9-560E-4989-B20B-AC6E910B1310Q36567484-64CBC765-732E-4DC8-A864-7270822B5A8AQ38119782-12CD6FC4-E5DA-4AE9-B2AF-69C08AAD843BQ38134935-903A636A-9E7F-44A9-B7C2-AF60C2FDE8A4Q38160822-91A5E8BA-F38B-4BD2-8916-BD11D8E66281Q38198756-418DBD8B-99B3-4E86-832E-490658E2B197Q38233723-622901CE-056D-4EDD-A584-0DFE2268FA2DQ38271597-199BBE87-B61B-49FF-9B96-865DB04D2DE5Q38363468-E5A56CD2-F718-4AF1-80E5-F2C0F675ADD3Q38428453-DE47D7F0-678E-4FE4-B56A-461289DAF90AQ38629689-736681AB-5A73-425F-A045-F4E477847416Q38645627-6F828006-FE4E-4E9D-A019-C36D3FD528C9Q38739347-7C04604C-ADC1-4A51-AE4F-97F6521B73D6Q38943772-DD844876-091D-417F-819B-C1F40B529D39Q43040141-0B6C8549-C84F-44F2-B6C5-DD9EE23A52BBQ48241438-1F7977FD-E103-49F8-81AF-4C837ADCDFA3Q49949196-70C22DC6-1899-431B-B8F1-EC71708252A5Q50439440-F75CA8CE-036C-451F-A105-BE6201109548
P2860
Histone acetyltransferases: Rising ancient counterparts to protein kinases.
description
2013 nî lūn-bûn
@nan
2013 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Histone acetyltransferases: Rising ancient counterparts to protein kinases.
@ast
Histone acetyltransferases: Rising ancient counterparts to protein kinases.
@en
Histone acetyltransferases: Rising ancient counterparts to protein kinases.
@nl
type
label
Histone acetyltransferases: Rising ancient counterparts to protein kinases.
@ast
Histone acetyltransferases: Rising ancient counterparts to protein kinases.
@en
Histone acetyltransferases: Rising ancient counterparts to protein kinases.
@nl
prefLabel
Histone acetyltransferases: Rising ancient counterparts to protein kinases.
@ast
Histone acetyltransferases: Rising ancient counterparts to protein kinases.
@en
Histone acetyltransferases: Rising ancient counterparts to protein kinases.
@nl
P2860
P356
P1433
P1476
Histone acetyltransferases: Rising ancient counterparts to protein kinases.
@en
P2093
Ronen Marmorstein
P2860
P304
P356
10.1002/BIP.22128
P577
2013-02-01T00:00:00Z