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-Reference-Cited by-同舟云学术

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

Published:2004-07 Issue:29 Volume:279 Page:30210-30218
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Vougier Stéphanie,Mary Jean,Dautin Nathalie,Vinh Joëlle,Friguet Bertrand,Ladant Daniel

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference36 articles.

1. Methionine residues may protect proteins from critical oxidative damage

2. The Sensitivity of Carboxyl-Terminal Methionines in Calmodulin Isoforms to Oxidation by H2O2 Modulates the Ability To Activate the Plasma Membrane Ca-ATPase

3. Calmodulin: a prototypical calcium sensor

4. Oxidation of Met144 and Met145 in Calmodulin Blocks Calmodulin Dependent Activation of the Plasma Membrane Ca-ATPase

5. Activation of Constitutive Nitric Oxide Synthases by Oxidized Calmodulin Mutants

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