A phosphorylation-motif for tuneable helix stabilisation in intrinsically disordered proteins – Lessons from the sodium proton exchanger 1 (NHE1)-Reference-Cited by-同舟云学术

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A phosphorylation-motif for tuneable helix stabilisation in intrinsically disordered proteins – Lessons from the sodium proton exchanger 1 (NHE1)

Published:2017-09 Issue: Volume:37 Page:40-51
ISSN:0898-6568
Container-title:Cellular Signalling
language:en
Short-container-title:Cellular Signalling

Author:

Hendus-Altenburger Ruth,Lambrughi Matteo,Terkelsen Thilde,Pedersen Stine F.,Papaleo Elena,Lindorff-Larsen Kresten,Kragelund Birthe B.

Funder

ISCRA-CINECA HPC

Danish National Research Council

Novo Nordisk Foundation

Publisher

Elsevier BV

Subject

Cell Biology

Reference89 articles.

1. Linking folding and binding;Wright;Curr. Opin. Struct. Biol.,2009

2. Coupling of folding and binding for unstructured proteins;Dyson;Curr. Opin. Struct. Biol.,2002

3. Interplay between partner and ligand facilitates the folding and binding of an intrinsically disordered protein;Rogers;Proc. Natl. Acad. Sci. U. S. A.,2014

4. Folding and binding of an intrinsically disordered protein: fast, but not ‘diffusion-limited’';Rogers;J. Am. Chem. Soc.,2013

5. Mechanism of coupled folding and binding of an intrinsically disordered protein;Sugase;Nature,2007

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