Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine. - Wikidata - wikimedia - TriplyDB

Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine.

Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine.

http://www.wikidata.org/entity/Q30876890

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Metabolism leaves its mark on the powerhouse: recent progress in post-translational modifications of lysine in mitochondria Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2 SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways Metabolism, cytoskeleton and cellular signalling in the grip of protein Nepsilon - and O-acetylation Acetylation of conserved lysines in the catalytic core of cyclin-dependent kinase 9 inhibits kinase activity and regulates transcription Crystal structures of human SIRT3 displaying substrate-induced conformational changes Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human genome Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases Gatekeepers of chromatin: Small metabolites elicit big changes in gene expression SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1 Lysine acetylation: codified crosstalk with other posttranslational modifications Structure-Function, Stability, and Chemical Modification of the Cyanobacterial Cytochrome b6f Complex from Nostoc sp. PCC 7120 Catalysis and substrate selection by histone/protein lysine acetyltransferases Control of acetyl-coenzyme A synthetase (AcsA) activity by acetylation/deacetylation without NAD(+) involvement in Bacillus subtilis Bacterial GCN5-Related N-Acetyltransferases: From Resistance to Regulation Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress Evolution and functional cross-talk of protein post-translational modifications Structural basis for sirtuin activity and inhibition Structure and mechanism of non-histone protein acetyltransferase enzymes Protein lysine acylation and cysteine succination by intermediates of energy metabolism Succinylome analysis reveals the involvement of lysine succinylation in metabolism in pathogenic Mycobacterium tuberculosis Flavonoid derivative 7,8-DHF attenuates TBI pathology via TrkB activation.Structural Basis for Nicotinamide Inhibition and Base Exchange in Sir2 Enzymes Biochemical and Crystallographic Analysis of Substrate Binding and Conformational Changes in Acetyl-CoA Synthetase † , ‡Crystal Structures of a Populus tomentosa 4-Coumarate:CoA Ligase Shed Light on Its Enzymatic Mechanisms Structure of Sir2Tm bound to a propionylated peptide Structural Insights into the Substrate Specificity of the Rhodopseudomonas palustris Protein Acetyltransferase RpPat: IDENTIFICATION OF A LOOP CRITICAL FOR RECOGNITION BY RpPat Structural, kinetic and proteomic characterization of acetyl phosphate-dependent bacterial protein acetylation Eukaryotic NAD+ synthetase Qns1 contains an essential, obligate intramolecular thiol glutamine amidotransferase domain related to nitrilase.Budding yeast silencing complexes and regulation of Sir2 activity by protein-protein interactions.Short-chain fatty acid activation by acyl-coenzyme A synthetases requires SIR2 protein function in Salmonella enterica and Saccharomyces cerevisiae.Acetyl-coenzyme A synthetase 2 is a nuclear protein required for replicative longevity in Saccharomyces cerevisiae Discovery of amide (peptide) bond synthetic activity in Acyl-CoA synthetase.Evidence that feedback inhibition of NAD kinase controls responses to oxidative stress Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase DNA pooling: a comprehensive, multi-stage association analysis of ACSL6 and SIRT5 polymorphisms in schizophrenia Nε-lysine acetylation of a bacterial transcription factor inhibits Its DNA-binding activity Identification of inhibitor binding site in human sirtuin 2 using molecular docking and dynamics simulations cAMP-regulated protein lysine acetylases in mycobacteria Reversible acetylation and inactivation of Mycobacterium tuberculosis acetyl-CoA synthetase is dependent on cAMP

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P2860

Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine.

http://www.wikidata.org/entity/Q30876890

description

2002 nî lūn-bûn

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2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2002年の論文

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年學術文章

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name

Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine.

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Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine.

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type

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Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine.

@ast

Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine.

@en

prefLabel

Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine.

@ast

Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine.

@en

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SCIENCE.1077650

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Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine.

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Boeke JD

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Celic I

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Cole RN

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Escalante-Semerena JC

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Starai VJ

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