Divalent cations influence the dimerization mode of murine S100A9 protein by modulating its disulfide bond pattern-Reference-Cited by-同舟云学术

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Divalent cations influence the dimerization mode of murine S100A9 protein by modulating its disulfide bond pattern

Published:2021-03 Issue:1 Volume:213 Page:107689
ISSN:1047-8477
Container-title:Journal of Structural Biology
language:en
Short-container-title:Journal of Structural Biology

Author:

Signor Luca,Paris Theo,Mas Caroline,Picard Adrien,Lutfalla Georges,Boeri Erba Elisabetta,Yatime Laure

Funder

French Infrastructure for Integrated Structural Biology

Kræftens Bekæmpelse

Publisher

Elsevier BV

Subject

Structural Biology

Reference102 articles.

1. PHENIX : a comprehensive Python-based system for macromolecular structure solution;Adams;Acta Cryst. D Biol. Crystallogr.,2010

2. Ions Binding to S100 Proteins. 1. Calcium-Binding and Zinc-Binding Properties of Bovine Brain S100-Alpha-Alpha, S100a-(Alpha, Beta), and S100b-(Beta-Beta), Protein - Zn-2+ Regulates Ca-2+ Binding on S100b Protein;Baudier;J. Biol. Chem.,1986

3. Bjork, P., Bjork, A., Vogl, T., Stenstrom, M., Liberg, D., Olsson, A. et al., 2009. Identification of human S100A9 as a novel target for treatment of autoimmune disease via binding to quinoline-3-carboxamides. PLoS Biol 7, e97. https://doi.org/10.1371/journal.pbio.1000097.

4. The emerging role of native mass spectrometry in characterizing the structure and dynamics of macromolecular complexes: The Emerging Role of Native Mass Spectrometry;Boeri Erba;Protein Sci.,2015

5. Characterizing Intact Macromolecular Complexes Using Native Mass Spectrometry;Boeri Erba;Methods Mol Biol,2018

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