Normal mode analysis of membrane protein dynamics using the vibrational subsystem analysis-Reference-Cited by-同舟云学术

Normal mode analysis of membrane protein dynamics using the vibrational subsystem analysis

Published:2021-05-21 Issue:19 Volume:154 Page:195102
ISSN:0021-9606
Container-title:The Journal of Chemical Physics
language:en
Short-container-title:J. Chem. Phys.

Author:

Zhang Yan¹^ORCID,Zhang She¹^ORCID,Xing Jianhua¹²^ORCID,Bahar Ivet¹^ORCID

Affiliation:

1. Department of Computational and Systems Biology, University of Pittsburgh, 800 Murdoch Bldg., 3420 Forbes Avenue, Pittsburgh, Pennsylvania 15260, USA

2. Department of Physics and Astronomy, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA

Funder

National Institutes of Health

Publisher

AIP Publishing

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

https://aip.scitation.org/doi/pdf/10.1063/5.0046710

Reference49 articles.

1. Membrane Protein Structure, Function, and Dynamics: a Perspective from Experiments and Theory

2. Membrane Protein Dynamics and Functional Implications in Mammalian Cells

3. Membrane protein misassembly in disease

4. Drugging Membrane Protein Interactions

5. Transmembrane helix-helix interactions involved in ErbB receptor signaling

Cited by 7 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Finely ordered intracellular domain harbors an allosteric site to modulate physiopathological function of P2X3 receptors;Nature Communications;2024-09-03

2. Anisotropic Network Analysis of Open/Closed HCN4 Channel Advocates Asymmetric Subunit Cooperativity in cAMP Modulation of Gating;Journal of Chemical Information and Modeling;2024-06-03

3. Scipion-EM-ProDy: A Graphical Interface for the ProDy Python Package within the Scipion Workflow Engine Enabling Integration of Databases, Simulations and Cryo-Electron Microscopy Image Processing;International Journal of Molecular Sciences;2023-09-18

4. Modeling protein–nucleic acid complexes with extremely large conformational changes using Flex‐LZerD;PROTEOMICS;2022-12-25

5. Domain-Based Protein Docking with Extremely Large Conformational Changes;Journal of Molecular Biology;2022-11