Standard Binding Free Energy and Membrane Desorption Mechanism for a Phospholipase C-Reference-Cited by-同舟云学术

Standard Binding Free Energy and Membrane Desorption Mechanism for a Phospholipase C

Published:2022-03-28 Issue:24 Volume:62 Page:6602-6613
ISSN:1549-9596
Container-title:Journal of Chemical Information and Modeling
language:en
Short-container-title:J. Chem. Inf. Model.

Author:

Moutoussamy Emmanuel E.¹²,Khan Hanif M.¹²^ORCID,Roberts Mary F.³^ORCID,Gershenson Anne⁴^ORCID,Chipot Christophe⁵⁶^ORCID,Reuter Nathalie²⁷^ORCID

Affiliation:

1. Department of Biological Sciences, University of Bergen, N-5020 Bergen, Norway

2. Computational Biology Unit, Department of Informatics, University of Bergen, N-5020 Bergen, Norway

3. Department of Chemistry, Boston College, Chestnut Hill, Massachusetts 02467, United States

4. Department of Biochemistry and Molecular Biology, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States

5. Laboratoire International Associé Centre National de la Recherche Scientifique et University of Illinois at Urbana−Champaign, Unité Mixte de Recherche n 7019, Université de Lorraine, BP 70239, 54506 Vandœuvre-lès-Nancy cedex, France

6. Department of Physics, University of Illinois, Urbana, Illinois 61801, United States

7. Department of Chemistry, University of Bergen, N-5020 Bergen, Norway

Funder

Norges Forskningsr?d

Publisher

American Chemical Society (ACS)

Subject

Library and Information Sciences,Computer Science Applications,General Chemical Engineering,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jcim.1c01543

Reference75 articles.

1. Description of Loxtox protein family and identification of a new group of Phospholipases D from Loxosceles similis venom gland

2. Structure of a novel class II phospholipase D: Catalytic cleft is modified by a disulphide bridge

3. Brown spiders and loxoscelism

4. Membrane-Protein Interactions in Cell Signaling and Membrane Trafficking

5. Amphitropic proteins: regulation by reversible membrane interactions (Review)

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