Potts Hamiltonian Models and Molecular Dynamics Free Energy Simulations for Predicting the Impact of Mutations on Protein Kinase Stability-Reference-Cited by-同舟云学术

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Potts Hamiltonian Models and Molecular Dynamics Free Energy Simulations for Predicting the Impact of Mutations on Protein Kinase Stability

Published:2024-02-13 Issue:7 Volume:128 Page:1656-1667
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Thakur Abhishek¹²^ORCID,Gizzio Joan¹²^ORCID,Levy Ronald M.¹²³^ORCID

Affiliation:

1. Center for Biophysics and Computational Biology, Temple University, Philadelphia, Pennsylvania 19122, United States

2. Department of Chemistry, Temple University, Philadelphia, Pennsylvania 19122, United States

3. Department of Physics, Temple University, Philadelphia, Pennsylvania 19122, United States

Funder

National Institutes of Health

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.3c08097

Reference53 articles.

1. Toward a Shared Vision for Cancer Genomic Data

2. Mutation in Abl kinase with altered drug-binding kinetics indicates a novel mechanism of imatinib resistance

3. Mutation effects predicted from sequence co-variation

4. Predicting and interpreting large-scale mutagenesis data using analyses of protein stability and conservation

5. Large scale free energy calculations for blind predictions of protein–ligand binding: the D3R Grand Challenge 2015

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1. Empowering AlphaFold2 for protein conformation selective drug discovery with AlphaFold2-RAVE;eLife;2024-09-06

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3. Empowering AlphaFold2 for protein conformation selective drug discovery with AlphaFold2-RAVE;2024-08-14

4. Evolutionary sequence and structural basis for the distinct conformational landscapes of Tyr and Ser/Thr kinases;Nature Communications;2024-08-02

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