A general strategy to characterize calmodulin–calcium complexes involved in CaM–target recognition: DAPK and EGFR calmodulin binding domains interact with different calmodulin–calcium complexes-Reference-Cited by-同舟云学术

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A general strategy to characterize calmodulin–calcium complexes involved in CaM–target recognition: DAPK and EGFR calmodulin binding domains interact with different calmodulin–calcium complexes

Published:2011-05 Issue:5 Volume:1813 Page:1059-1067
ISSN:0167-4889
Container-title:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Author:

Dagher Rania,Peng Shan,Gioria Sophie,Fève Marie,Zeniou Maria,Zimmermann Michael,Pigault Claire,Haiech Jacques,Kilhoffer Marie-Claude

Funder

Agence Nationale de la Recherche (ANR CAPHE)

Ligue contre le Cancer

CNRS

University of Strasbourg

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference45 articles.

1. Signal transduction. The calcium entry pas de deux;Berridge;Science,2000

2. Calcium signalling: dynamics, homeostasis and remodelling;Berridge;Nat. Rev.,2003

3. EF-hand protein dynamics and evolution of calcium signal transduction: an NMR view;Capozzi;J. Biol. Inorg. Chem.,2006

4. Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: two ways to promote multifunctionality;Ikura;Proc. Natl Acad. Sci. USA,2006

5. Structures and metal-ion-binding properties of the Ca2+-binding helix–loop–helix EF-hand motifs;Gifford;Biochem. J.,2007

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