Kinetic versus thermodynamic control of mutational effects on protein homeostasis: A perspective from computational modeling and experiment-Reference-Cited by-同舟云学术

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Kinetic versus thermodynamic control of mutational effects on protein homeostasis: A perspective from computational modeling and experiment

Published:2019-05-24 Issue:7 Volume:28 Page:1324-1339
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Pobre Kristine Faye R.¹,Powers David L.²,Ghosh Kingshuk³,Gierasch Lila M.¹^ORCID,Powers Evan T.⁴^ORCID

Affiliation:

1. Departments of Biochemistry & Molecular Biology and Chemistry University of Massachusetts‐Amherst Amherst Massachusetts 01003

2. Department of Mathematics Clarkson University Potsdam New York 13699

3. Department of Physics and Astronomy University of Denver Denver Colorado 80208

4. Department of Chemistry The Scripps Research Institute La Jolla California 92037

Funder

National Institute of General Medical Sciences

National Science Foundation

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.3639

Reference78 articles.

1. Adapting Proteostasis for Disease Intervention

2. Proteostasis impairment in protein-misfolding and -aggregation diseases

3. Biological and Chemical Approaches to Diseases of Proteostasis Deficiency

4. THE HEAT-SHOCK RESPONSE

5. Proteostasis control by the unfolded protein response

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1. Reconstituted Cell-free Translation Systems for Exploring Protein Folding and Aggregation;Journal of Molecular Biology;2024-10

2. The use of pharmacological chaperones in rare diseases caused by reduced protein stability;PROTEOMICS;2022-10-19

3. The Proteome Folding Problem and Cellular Proteostasis;Journal of Molecular Biology;2021-10

4. Protein folding stability and binding interactions through the lens of evolution: a dynamical perspective;Current Opinion in Structural Biology;2021-02

5. Programmed Trade-offs in Protein Folding Networks;Structure;2020-12

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