Control of protein function by reversible Nɛ-lysine acetylation in bacteria
about
Metabolism leaves its mark on the powerhouse: recent progress in post-translational modifications of lysine in mitochondriaAcylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic StressCyclic AMP regulation of protein lysine acetylation in Mycobacterium tuberculosisStructural Insights into the Substrate Specificity of the Rhodopseudomonas palustris Protein Acetyltransferase RpPat: IDENTIFICATION OF A LOOP CRITICAL FOR RECOGNITION BY RpPatIn Salmonella enterica, the Gcn5-related acetyltransferase MddA (formerly YncA) acetylates methionine sulfoximine and methionine sulfone, blocking their toxic effectsGlobal analysis of lysine acetylation in strawberry leaves.Acetyl coenzyme A synthetase is acetylated on multiple lysine residues by a protein acetyltransferase with a single Gcn5-type N-acetyltransferase (GNAT) domain in Saccharopolyspora erythraeaInsights into the specificity of lysine acetyltransferasesThe E. coli sirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sitesDeterminants within the C-terminal domain of Streptomyces lividans acetyl-CoA synthetase that block acetylation of its active site lysine in vitro by the protein acetyltransferase (Pat) enzymeAcetate availability and utilization supports the growth of mutant sub-populations on aging bacterial coloniesDifferential lysine acetylation profiles of Erwinia amylovora strains revealed by proteomicsCheY's acetylation sites responsible for generating clockwise flagellar rotation in Escherichia coliChanges in the Acetylome and Succinylome of Bacillus subtilis in Response to Carbon Source.VimA-dependent modulation of acetyl coenzyme A levels and lipid A biosynthesis can alter virulence in Porphyromonas gingivalisSystem-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases.Cross Talk Inhibition Nullified by a Receiver Domain Missense SubstitutionComparative metagenome of a stream impacted by the urbanization phenomenon.Pro-Proliferative Function of Mitochondrial Sirtuin Deacetylase SIRT3 in Human MelanomaInactivation of the Pta-AckA pathway causes cell death in Staphylococcus aureusCentral metabolism controls transcription of a virulence gene regulator in Vibrio cholerae.Reactivity landscape of pyruvate under simulated hydrothermal vent conditions.Acetylation of the response regulator RcsB controls transcription from a small RNA promoter.Post-translational Serine/Threonine Phosphorylation and Lysine Acetylation: A Novel Regulatory Aspect of the Global Nitrogen Response Regulator GlnR in S. coelicolor M145.A tale of two machines: a review of the BLAST meeting, Tucson, AZ, 20-24 January 2013.Modulation of Central Carbon Metabolism by Acetylation of Isocitrate Lyase in Mycobacterium tuberculosis.Protein acetylation in prokaryotes.Metabolic regulation by SIRT3: implications for tumorigenesis.Post-translation modification in Archaea: lessons from Haloferax volcanii and other haloarchaea.Regulation of a Protein Acetyltransferase in Myxococcus xanthus by the Coenzyme NADP.Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoterProtein lysine acetylation in bacteria: Current state of the art.Bacterial protein acetylation: new discoveries unanswered questions.Regulation, Function, and Detection of Protein Acetylation in Bacteria.Mitochondrial Sirtuins in Cancer: Emerging Roles and Therapeutic Potential.The acetylation motif in AMP-forming Acyl coenzyme A synthetases contains residues critical for acetylation and recognition by the protein acetyltransferase pat of Rhodopseudomonas palustris.A multifaceted study of Pseudomonas aeruginosa shutdown by virulent podovirus LUZ19.A SIRT4-like auto ADP-ribosyltransferase is essential for the environmental growth of Mycobacterium smegmatis.Lysine acetylation regulates the activity of Escherichia coli S-adenosylmethionine synthase.Salmonella typhimurium and Escherichia coli dissimilarity: Closely related bacteria with distinct metabolic profiles.
P2860
Q21129226-700D364F-A8AA-4A8A-B73D-F1C226A1D623Q26801091-CC38AD83-F919-4546-8EE1-2DCB257E8E48Q27670673-646B4880-5EB1-4DF7-82AD-FB076B274080Q27674620-7F115C3D-6EFA-415E-B484-E1ADBF512345Q28490004-66092760-E73A-4DEA-8B63-95EF64D522EBQ30664521-F47C25C5-C6BC-49B1-BA54-E145BEDEB355Q34056727-E9148E92-E7D8-4813-B256-F8AC5AD834B8Q34774593-F1D2AC84-7D5F-4505-A4FF-699731DED60AQ35106207-2DDA0FDE-4AF2-4E93-BDEB-DD6A16D3EBFBQ35185420-379F5893-611D-46FF-89C7-9091A7FD6556Q35295130-F6B4F71F-09DA-447E-86CB-14C23DCC5F32Q35566272-2676E562-1DD3-4287-BD85-5AC755AF8B3DQ35591644-4A17FA82-2DAB-41BA-B86F-38091BF65D1FQ35670351-23ED9C7C-8724-4F0F-8174-94FE0A7E0BF6Q35689547-07576B1B-5735-49DA-8EF8-A56F050F1F1DQ35939782-77BF4AF5-33B8-40E9-B61C-251BD942B880Q36070050-C3231F80-DEDD-4504-A149-BEE8FA7F17FFQ36103712-11A6E14C-232F-4016-B2E0-8C091D6094DDQ36730675-52B32021-A5BA-474F-A456-F5C5821CA05AQ36970582-9FFF1F2D-C054-47A4-A256-C8E85CBC9E8AQ37007471-5D76F03F-090E-495C-86BA-57325EAE2166Q37103956-6C3ED787-0032-4C04-8D26-9FA4F6024345Q37125410-BACA6FA6-CB61-4FDA-8986-D62512898A7DQ37160425-51295DBE-13E3-4240-BDCF-E98ECD1A27E8Q37659614-477695A8-59AB-45AB-A73F-AAF9604D9804Q37713072-67A0AA3C-C738-4529-9C3B-6FA93C65C3D4Q37889858-25A88C07-20AE-495D-81C2-2F022405A1FCQ38022918-3F38652D-F711-445E-A026-36B6882A52F4Q38061206-BAFA8E1C-23FB-46D5-ACE4-5CFBFC3F524EQ38386655-1BCF538B-B556-4152-ADE7-B91B296A100DQ38570214-49204A2A-5295-457C-B1C2-B36EFFBFE0E1Q38590397-926C9FFA-2B00-4D45-A0A4-936EA59E3B30Q38667629-C09C3DF4-BFD6-49F9-96E3-DA72C6B17F24Q38691364-D2D68B13-FEFE-4677-B53B-99EA96DD1C2DQ38838565-709C3984-3113-4F91-B0A3-FF9AA8996FB3Q38850956-7695850B-9CEE-42F9-8103-7CAE96B865DFQ39448249-E964B8E3-31C1-4959-94CD-A959A75ED1FEQ40191162-2AEF1E64-0D92-4EE0-9481-349C28E89D12Q40649176-81C2CBA8-9358-4AC1-A1D2-3BE53BDF88E6Q41147322-1416EC12-8DFA-4EBF-A19B-5ED5FE941C86
P2860
Control of protein function by reversible Nɛ-lysine acetylation in bacteria
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Control of protein function by reversible Nɛ-lysine acetylation in bacteria
@ast
Control of protein function by reversible Nɛ-lysine acetylation in bacteria
@en
Control of protein function by reversible Nɛ-lysine acetylation in bacteria
@nl
type
label
Control of protein function by reversible Nɛ-lysine acetylation in bacteria
@ast
Control of protein function by reversible Nɛ-lysine acetylation in bacteria
@en
Control of protein function by reversible Nɛ-lysine acetylation in bacteria
@nl
prefLabel
Control of protein function by reversible Nɛ-lysine acetylation in bacteria
@ast
Control of protein function by reversible Nɛ-lysine acetylation in bacteria
@en
Control of protein function by reversible Nɛ-lysine acetylation in bacteria
@nl
P2860
P1476
Control of protein function by reversible Nɛ-lysine acetylation in bacteria
@en
P2093
Jorge C Escalante-Semerena
Sandy Thao
P2860
P304
P356
10.1016/J.MIB.2010.12.013
P577
2011-01-14T00:00:00Z