Measuring protein structural changes on a proteome-wide scale using limited proteolysis-coupled mass spectrometry-Reference-Cited by-同舟云学术

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Measuring protein structural changes on a proteome-wide scale using limited proteolysis-coupled mass spectrometry

Published:2017-10-26 Issue:11 Volume:12 Page:2391-2410
ISSN:1754-2189
Container-title:Nature Protocols
language:en
Short-container-title:Nat Protoc

Author:

Schopper Simone,Kahraman Abdullah,Leuenberger Pascal,Feng Yuehan,Piazza Ilaria,Müller Oliver,Boersema Paul J,Picotti Paola

Publisher

Springer Science and Business Media LLC

Subject

General Biochemistry, Genetics and Molecular Biology

Link

http://www.nature.com/articles/nprot.2017.100.pdf

Reference60 articles.

1. Walther, T.C. & Mann, M. Mass spectrometry-based proteomics in cell biology. J. Cell Biol. 190, 491–500 (2010).

2. Feng, Y. et al. Global analysis of protein structural changes in complex proteomes. Nat. Biotechnol. 32, 1036–1044 (2014).

3. Leuenberger, P. et al. Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability. Science 355, eaai7825 (2017).

4. Stauffer, S. et al. Stepwise priming by acidic pH and a high K+ concentration is required for efficient uncoating of influenza A virus cores after penetration. J. Virol. 88, 13029–13046 (2014).

5. Geiger, R. et al. L-arginine modulates T cell metabolism and enhances survival and anti-tumor activity. Cell 167, 829–842 (2016).

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