Intrinsic flexibility of NLRP pyrin domains is a key factor in their conformational dynamics, fold stability, and dimerization-Reference-Cited by-同舟云学术

Intrinsic flexibility of NLRP pyrin domains is a key factor in their conformational dynamics, fold stability, and dimerization

Published:2014-12-26 Issue:2 Volume:24 Page:174-181
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Huber Roland G.¹²,Eibl Clarissa³⁴,Fuchs Julian E.¹⁵

Affiliation:

1. Institute for General, Inorganic and Theoretical Chemistry; Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck; Innrain 80/82 Innsbruck Austria

2. Bioinformatics Institute, Agency for Science; Technology and Research (A*STAR); 30 Biopolis Street #07-01 Matrix Singapore 138671

3. Department of Molecular Biology; University of Salzburg; Billrothstrasse 11 5020 Salzburg Austria

4. Molecular Neuroscience and Biophysics, Leibniz-Institute for Molecular Pharmacology; Robert-Roessle Strasse 10; 13125 Berlin Germany

5. Centre for Molecular Informatics, Department of Chemistry; University of Cambridge; Cambridge CB2 1EW United Kingdom

Funder

Austrian Science Fund

Medical Research Council

Austrian Academy of Sciences (DOC Fellowship at University of Innsbruck)

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2601/fullpdf

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3. NOD-like receptors and the innate immune system: coping with danger, damage, and death;Kersse;Cytokine Growth Factor Rev,2011

4. NALPS: a novel protein family involved in inflammation;Tschopp;Nature Rev Mol Cell Biol,2003

5. NLRPs, microbiota, and gut homeostasis: unravelling the connection;Zambetti;J Pathol,2014

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