Metal binding and conformational studies of the calcium binding domain of NADPH oxidase 5 reveal its similarity and difference to calmodulin
Author:
Affiliation:
1. Department of Chemistry, Southern Illinois University Edwardsville, Edwardsville, Illinois, USA;
2. Department of Pathobiology, the Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio, USA
Funder
Southern Illinois University Edwardsville: Undergraduate Research and Creative Activities
National Science Foundation
Publisher
Informa UK Limited
Subject
Molecular Biology,General Medicine,Structural Biology
Link
https://www.tandfonline.com/doi/pdf/10.1080/07391102.2019.1633409
Reference60 articles.
1. Solvation energetics and conformational change in EF-hand proteins
2. Dual Oxidase-2 Has an Intrinsic Ca2+-dependent H2O2-generating Activity
3. NADPH Oxidase: An Update
4. Mechanism of Ca2+ Activation of the NADPH Oxidase 5 (NOX5)
5. The kinetics of calcium binding to calmodulin: Quin 2 and ANS stopped-flow fluorescence studies
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