Abnormal SDS-PAGE migration of cytosolic proteins can identify domains and mechanisms that control surfactant binding-Reference-Cited by-同舟云学术

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Abnormal SDS-PAGE migration of cytosolic proteins can identify domains and mechanisms that control surfactant binding

Published:2012-07-13 Issue:8 Volume:21 Page:1197-1209
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Shi Yunhua,Mowery Richard A.,Ashley Jonathan,Hentz Michelle,Ramirez Alejandro J.,Bilgicer Basar,Slunt-Brown Hilda,Borchelt David R.,Shaw Bryan F.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference51 articles.

1. Membrane recognition by phospholipid-binding domains;Lemmon;Nat Rev Mol Cell Biol,2008

2. Lysine acetylation can generate highly charged enzymes with increased resistance towards irreversible inactivation;Shaw;Protein Sci,2008

3. Protein-surfactant interactions: a tale of many states;Otzen;Biochim Biophys Acta,2011

4. Complexes of native Ubiquitin and dodecyl sulfate illustrate the nature of hydrophobic and electrostatic interactions in the binding of proteins and surfactants;Shaw;J Am Chem Soc,2011

5. SDS-induced fibrillation of alpha-synuclein: an alternative fibrillation pathway;Giehm;J Mol Biol,2010

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