The effect of charged residue substitutions on the thermodynamics of protein‐surface interactions-Reference-Cited by-同舟云学术

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The effect of charged residue substitutions on the thermodynamics of protein‐surface interactions

Published:2021-11-08 Issue:12 Volume:30 Page:2408-2417
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Ortega Gabriel¹²³⁴^ORCID,Aguilar Miguel A.¹^ORCID,Gautam Bishal K.¹^ORCID,Plaxco Kevin W.¹²^ORCID

Affiliation:

1. Department of Chemistry and Biochemistry University of California Santa Barbara Santa Barbara California USA

2. Center for Bioengineering University of California Santa Barbara Santa Barbara California USA

3. Precision Medicine and Metabolism Laboratory CIC bioGUNE, Basque Research and Technology Alliance, Parque Tecnológico de Bizkaia Derio Spain

4. Ikerbasque Basque Foundation for Science Bilbao, Bizkaia Spain

Funder

Ikerbasque, Basque Foundation for Science

National Institutes of Health

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.4215

Reference35 articles.

1. Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments

2. WickyBIM GuptaK KwanTOC RobinsonCV ClarkeJ.Spontaneous oligomerization of BAK/BAX is suppressed by hetero‐dimerization with MCL‐1. bioRxiv. 2019;756874.

3. The role of protein kinase C in cell surface signal transduction and tumour promotion

4. Membrane-Protein Interactions in Cell Signaling and Membrane Trafficking

5. HIV gp41–mediated membrane fusion occurs at edges of cholesterol-rich lipid domains

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