Elucidating Residue-Level Determinants Affecting Dimerization of Ebola Virus Matrix Protein Using High-Throughput Site Saturation Mutagenesis and Biophysical Approaches-Reference-Cited by-同舟云学术

Elucidating Residue-Level Determinants Affecting Dimerization of Ebola Virus Matrix Protein Using High-Throughput Site Saturation Mutagenesis and Biophysical Approaches

Published:2023-07-17 Issue:29 Volume:127 Page:6449-6461
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Narkhede Yogesh B.¹,Bhardwaj Atul¹,Motsa Balindile B.²,Saxena Roopashi²,Sharma Tej,Chapagain Prem P.^ORCID,Stahelin Robert V.²,Wiest Olaf¹^ORCID

Affiliation:

1. Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States

2. Department of Medicinal Chemistry & Molecular Pharmacology, Purdue Institute of Inflammation, Immunology, and Infectious Disease, Purdue University, West Lafayette, Indiana 47907, United States

Funder

NIH Office of the Director

National Institute of Allergy and Infectious Diseases

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.3c01759

Reference74 articles.

1. The Pathogenesis of Ebola Virus Disease

2. Structural characterization and membrane binding properties of the matrix protein VP40 of ebola virus

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