An Nalpha-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A.
about
Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotesNatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregationComposition and biological significance of the human Nα-terminal acetyltransferasesThe human N-alpha-acetyltransferase 40 (hNaa40p/hNatD) is conserved from yeast and N-terminally acetylates histones H2A and H4The chaperone-like protein HYPK acts together with NatA in cotranslational N-terminal acetylation and prevention of Huntingtin aggregationN-terminal modifications of cellular proteins: The enzymes involved, their substrate specificities and biological effectsMolecular basis for N-terminal acetylation by the heterodimeric NatA complexImplications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal orthologN-alpha-terminal acetylation of histone H4 regulates arginine methylation and ribosomal DNA silencingGlobal assessment of combinatorial post-translational modification of core histones in yeast using contemporary mass spectrometry. LYS4 trimethylation correlates with degree of acetylation on the same H3 tail.Protein N-terminal acetyltransferases act as N-terminal propionyltransferases in vitro and in vivo.Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p.Identification of lysine 37 of histone H2B as a novel site of methylationCrystal Structure of the Golgi-Associated Human Nα-Acetyltransferase 60 Reveals the Molecular Determinants for Substrate-Specific AcetylationThe molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatDQuantitative proteomic analysis of histone modificationsHuman Naa50 Protein Displays Broad Substrate Specificity for Amino-terminal Acetylation: DETAILED STRUCTURAL AND BIOCHEMICAL ANALYSIS USING TETRAPEPTIDE LIBRARY.Naa50/San-dependent N-terminal acetylation of Scc1 is potentially important for sister chromatid cohesion.Protein N-terminal acetylation: NAT 2007-2008 Symposia.A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature, subunits and substratesIdentification of the sequence determinants of protein N-terminal acetylation through a decision tree approach.N-terminal acetylation inhibits protein targeting to the endoplasmic reticulumUbiquitin ligases of the N-end rule pathway: assessment of mutations in UBR1 that cause the Johanson-Blizzard syndromeThe N-end rule pathway and regulation by proteolysisProtein N-terminal acetyltransferases in cancer.Physiological importance and identification of novel targets for the N-terminal acetyltransferase NatB.Importance of the Sir3 N terminus and its acetylation for yeast transcriptional silencing.Histone H4 acetylation differentially modulates arginine methylation by an in Cis mechanism.Histone deacetylase inhibitors globally enhance h3/h4 tail acetylation without affecting h3 lysine 56 acetylation.Knockdown of NAT12/NAA30 reduces tumorigenic features of glioblastoma-initiating cellsFungal KATs/KDACs: A New Highway to Better Antifungal Drugs?Absence of N-terminal acetyltransferase diversification during evolution of eukaryotic organisms.Combinatorial modification of human histone H4 quantitated by two-dimensional liquid chromatography coupled with top down mass spectrometry.Properties of Nat4, an N(alpha)-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4Loss of Nat4 and its associated histone H4 N-terminal acetylation mediates calorie restriction-induced longevity.Targeted large-scale analysis of protein acetylation.Protein alpha-N-acetylation studied by N-terminomics.Depletion of histone N-terminal-acetyltransferase Naa40 induces p53-independent apoptosis in colorectal cancer cells via the mitochondrial pathwayDevelopmental roles of protein N-terminal acetylation.Comprehensive Catalog of Currently Documented Histone Modifications.
P2860
Q21090782-2447D9DD-2450-4070-A359-D9BF04975678Q21144944-2004A7F5-241E-4EBC-9CB5-228EA9097974Q21202069-1994A434-AEC4-46F9-B155-15CAAB013302Q21560927-C366472C-D750-4A98-AFAE-F6510D6531A1Q24605078-CA116497-68F0-4878-8BE4-1BA38C6BDF7CQ27011436-BDB1AFA4-0E72-4873-B94C-936754BE81C0Q27679359-9276C235-79D0-4582-B044-16AF820EFDA0Q27679722-E8D8DBE6-784F-46DC-BC03-83734A15304EQ27930575-CA291A6C-573B-4C13-A774-4E3CE6783097Q27935735-9067BE19-7386-48A0-B51F-FCCF248A7933Q27939409-3F60792B-3F58-4D83-96A1-80A46D3BC0E0Q27939495-F3228F55-0F3F-4847-AC2F-205D4F1DE752Q28476731-018B9E27-FCDD-4B68-994E-50BDF8B4B77EQ28596558-C19E541D-C59F-4D9B-B3A6-A6A14AA15A27Q28596566-F374E325-5981-48DF-8CC8-F7B904766140Q30375585-CB56F8B3-DB8B-4071-8C8B-60F37B0EA4ABQ30391361-5D77E8DC-07CE-49F2-8B38-4DC2FDD444DBQ30832532-72757057-A626-4274-8E04-2D9ACCD2CEA7Q33491259-83EC6EAA-1B4D-470E-9B0E-D17B26DB6B1CQ33491261-1A87596C-F055-4E98-BBCC-EBDF619E1D44Q33759511-ED636F4E-ABDE-40CB-91A4-30CD2DB024CFQ33927332-4468D64A-A2C1-46D5-A5BD-2B24AC408934Q34024105-1B88CA16-23F2-4896-8209-0A6B6B7B698AQ34189152-206872B5-0662-40DE-AC1E-0477256D40C3Q34258775-C0A35B04-AA41-4E3C-B7A1-E6033817C991Q34492928-CA2B15D1-1FE4-48A6-B829-FA4815C9EC29Q34567211-AD2397A7-4313-4B0B-9033-B69707F6EFA3Q35063526-A07EAAFC-D051-4D2A-B6DA-1E486570812AQ35667942-8264003C-B590-4BD6-AAFD-4A4CBC789BDFQ35986799-CB3DE42B-4F86-4F30-9824-97740A3FA3F5Q36188969-DBA42A32-45C1-4052-93D0-BD22C4DBC0A4Q36565138-11A0D580-1F3A-4511-BE1F-156384084EA8Q36678491-A495C879-8FE7-462F-B7FF-626925912078Q37192022-F8C79403-FAAD-48BC-B3C3-32D5309BDDE5Q37515461-B2B04FDB-8B8C-427A-98BC-032F6CCA7D39Q37829997-0BD6FA38-BC1A-4825-879E-790B3CD634E3Q37898754-FFD6AC99-9E89-49B9-9139-A182D35841B7Q38292041-D47B39A5-D15B-40CC-B9C0-B0A50B52D9A4Q38446887-067FC6B8-3924-415E-8E32-845A50E74728Q38578748-30983CD6-590F-4D34-9397-6E2876D08698
P2860
An Nalpha-acetyltransferase responsible for acetylation of the N-terminal residues of histones H4 and H2A.
description
2003 nî lūn-bûn
@nan
2003 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
An Nalpha-acetyltransferase re ...... sidues of histones H4 and H2A.
@ast
An Nalpha-acetyltransferase re ...... sidues of histones H4 and H2A.
@en
An Nalpha-acetyltransferase re ...... sidues of histones H4 and H2A.
@nl
type
label
An Nalpha-acetyltransferase re ...... sidues of histones H4 and H2A.
@ast
An Nalpha-acetyltransferase re ...... sidues of histones H4 and H2A.
@en
An Nalpha-acetyltransferase re ...... sidues of histones H4 and H2A.
@nl
prefLabel
An Nalpha-acetyltransferase re ...... sidues of histones H4 and H2A.
@ast
An Nalpha-acetyltransferase re ...... sidues of histones H4 and H2A.
@en
An Nalpha-acetyltransferase re ...... sidues of histones H4 and H2A.
@nl
P2860
P3181
P356
P1476
An Nalpha-acetyltransferase re ...... esidues of histones H4 and H2A
@en
P2093
Ok-kyu Song
Rolf Sternglanz
P2860
P304
38109-38112
P3181
P356
10.1074/JBC.C300355200
P407
P577
2003-08-12T00:00:00Z