Global Dynamics Renders Protein Sites with High Functional Response-Reference-Cited by-同舟云学术

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Global Dynamics Renders Protein Sites with High Functional Response

Published:2021-04-29 Issue:18 Volume:125 Page:4734-4745
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Kutlu Yiǧit¹^ORCID,Ben-Tal Nir²,Haliloglu Turkan¹^ORCID

Affiliation:

1. Department of Chemical Engineering and Polymer Research Center, Bogazici University, Bebek, Istanbul 34342, Turkey

2. Department of Biochemistry and Molecular Biology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 6997801, Israel

Funder

North Atlantic Treaty Organization

Tel Aviv University

T?rkiye Bilimsel ve Teknolojik Arastirma Kurumu

Bogazi?i ?niversitesi

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.1c02511

Reference85 articles.

1. Loss of Protein Structure Stability as a Major Causative Factor in Monogenic Disease

2. Residue mutations and their impact on protein structure and function: detecting beneficial and pathogenic changes

3. Insights into Disease-Associated Mutations in the Human Proteome through Protein Structural Analysis

4. Making evolutionary biology a basic science for medicine

5. A natural upper bound to the accuracy of predicting protein stability changes upon mutations

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2. Exploring and Learning the Universe of Protein Allostery Using Artificial Intelligence Augmented Biophysical and Computational Approaches;Journal of Chemical Information and Modeling;2023-02-24

3. Subsets of Slow Dynamic Modes Reveal Global Information Sources as Allosteric Sites;Journal of Molecular Biology;2022-09

4. Prediction of allosteric communication pathways in proteins;Bioinformatics;2022-06-08

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