Essential role of methionine residues in calmodulin binding to Bordetella pertussis adenylate cyclase, as probed by selective oxidation and repair by the peptide methionine sulfoxide reductases.
about
Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulinRegulation of protein function by reversible methionine oxidation and the role of selenoprotein MsrB1A tethered bilayer assembled on top of immobilized calmodulin to mimic cellular compartmentalization.Characterization of methionine oxidation and methionine sulfoxide reduction using methionine-rich cysteine-free proteins.N-terminal and C-terminal domains of calmodulin mediate FADD and TRADD interactionMethionine sulfoxide reductases: relevance to aging and protection against oxidative stress.Maintenance of proteins and aging: the role of oxidized protein repair.Increased catalytic efficiency following gene fusion of bifunctional methionine sulfoxide reductase enzymes from Shewanella oneidensisInteractions of Bordetella pertussis adenylyl cyclase toxin CyaA with calmodulin mutants and calmodulin antagonists: comparison with membranous adenylyl cyclase I.Modulating protein activity and cellular function by methionine residue oxidation.Molecular Modeling of the Catalytic Domain of CyaA Deepened the Knowledge of Its Functional Dynamics.Identification of a region that assists membrane insertion and translocation of the catalytic domain of Bordetella pertussis CyaA toxin.Use of top-down and bottom-up Fourier transform ion cyclotron resonance mass spectrometry for mapping calmodulin sites modified by platinum anticancer drugs.Overexpression of mitochondrial methionine sulfoxide reductase B2 protects leukemia cells from oxidative stress-induced cell death and protein damage.Allosteric activation of Bordetella pertussis adenylyl cyclase by calmodulin: molecular dynamics and mutagenesis studiesDifferent Roles of N-Terminal and C-Terminal Domains in Calmodulin for Activation of Bacillus anthracis Edema Factor.Role of calmodulin methionine residues in mediating productive association with cardiac ryanodine receptors.Conformational Ensembles of Calmodulin Revealed by Nonperturbing Site-Specific Vibrational Probe Groups.
P2860
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P2860
Essential role of methionine residues in calmodulin binding to Bordetella pertussis adenylate cyclase, as probed by selective oxidation and repair by the peptide methionine sulfoxide reductases.
description
2004 nî lūn-bûn
@nan
2004 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Essential role of methionine r ...... thionine sulfoxide reductases.
@ast
Essential role of methionine r ...... thionine sulfoxide reductases.
@en
type
label
Essential role of methionine r ...... thionine sulfoxide reductases.
@ast
Essential role of methionine r ...... thionine sulfoxide reductases.
@en
prefLabel
Essential role of methionine r ...... thionine sulfoxide reductases.
@ast
Essential role of methionine r ...... thionine sulfoxide reductases.
@en
P2093
P2860
P50
P356
P1476
Essential role of methionine r ...... ethionine sulfoxide reductases
@en
P2093
Nathalie Dautin
Stéphanie Vougier
P2860
P304
30210-30218
P356
10.1074/JBC.M400604200
P407
P577
2004-05-17T00:00:00Z