Insights into the catalytic mechanism of PPM Ser/Thr phosphatases from the atomic resolution structures of a mycobacterial enzyme
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A Third Metal Is Required for Catalytic Activity of the Signal-transducing Protein Phosphatase M tPphAStructure of the Phosphatase Domain of the Cell Fate Determinant SpoIIE from Bacillus subtilisStructural and Biochemical Characterization of Human Mitochondrial Branched-chain -Ketoacid Dehydrogenase PhosphataseStructural Basis for Rab1 De-AMPylation by the Legionella pneumophila Effector SidDStructure of the RsbX phosphatase involved in the general stress response of Bacillus subtilisDeterminants for substrate specificity of the bacterial PP2C protein phosphatase tPphA from Thermosynechococcus elongatusStructural and enzymatic characterization of the streptococcal ATP/diadenosine polyphosphate and phosphodiester hydrolase Spr1479/SapH."PP2C7s", Genes Most Highly Elaborated in Photosynthetic Organisms, Reveal the Bacterial Origin and Stepwise Evolution of PPM/PP2C Protein Phosphatases.Optimization of a cyclic peptide inhibitor of Ser/Thr phosphatase PPM1D (Wip1).CTL0511 from Chlamydia trachomatis Is a Type 2C Protein Phosphatase with Broad Substrate SpecificityBinding of a third metal ion by the human phosphatases PP2Cα and Wip1 is required for phosphatase activityBypass suppression analysis maps the signalling pathway within a multidomain protein: the RsbP energy stress phosphatase 2C from Bacillus subtilis.Eukaryote-like serine/threonine kinases and phosphatases in bacteria.The Role of Arg13 in Protein Phosphatase M tPphA from Thermosynechococcus elongatus.Crystallization and preliminary X-ray analysis of the stress-response PPM phosphatase RsbX from Bacillus subtilis.Ser/Thr Phosphorylation Regulates the Fatty Acyl-AMP Ligase Activity of FadD32, an Essential Enzyme in Mycolic Acid BiosynthesisThe unique serine/threonine phosphatase from the minimal bacterium Mycoplasma synoviae: biochemical characterization and metal dependence.Conformational Changes in Active and Inactive States of Human PP2Cα Characterized by Hydrogen/Deuterium Exchange-Mass Spectrometry.A trapped human PPM1A-phosphopeptide complex reveals structural features critical for regulation of PPM protein phosphatase activity.
P2860
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P2860
Insights into the catalytic mechanism of PPM Ser/Thr phosphatases from the atomic resolution structures of a mycobacterial enzyme
description
2007 nî lūn-bûn
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2007 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հուլիսին հրատարակված գիտական հոդված
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2007年の論文
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2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
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2007年论文
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name
Insights into the catalytic me ...... ures of a mycobacterial enzyme
@ast
Insights into the catalytic me ...... ures of a mycobacterial enzyme
@en
Insights into the catalytic me ...... ures of a mycobacterial enzyme
@nl
type
label
Insights into the catalytic me ...... ures of a mycobacterial enzyme
@ast
Insights into the catalytic me ...... ures of a mycobacterial enzyme
@en
Insights into the catalytic me ...... ures of a mycobacterial enzyme
@nl
prefLabel
Insights into the catalytic me ...... ures of a mycobacterial enzyme
@ast
Insights into the catalytic me ...... ures of a mycobacterial enzyme
@en
Insights into the catalytic me ...... ures of a mycobacterial enzyme
@nl
P1433
P1476
Insights into the catalytic me ...... ures of a mycobacterial enzyme
@en
P2093
Annemarie Wehenkel
William Shepard
P304
P356
10.1016/J.STR.2007.06.002
P577
2007-07-01T00:00:00Z