Conformational Plasticity in an HIV-1 Antibody Epitope-Reference-Cited by-同舟云学术

Conformational Plasticity in an HIV-1 Antibody Epitope

Published:2010-05-21 Issue:23 Volume:114 Page:7942-7950
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Tulip P. R.¹,Gregor C. R.¹,Troitzsch R. Z.¹,Martyna G. J.¹,Cerasoli E.¹,Tranter G.¹,Crain J.¹

Affiliation:

1. School of Physics, The University of Edinburgh, Mayfield Road, Edinburgh, EH9 3JZ, U.K., IBM T.J. Watson Research Center, Yorktown Heights, New York, 10598, and National Physical Laboratory, Hampton Road, Teddington, TW11 0LW, U.K.

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/jp100929n

Reference47 articles.

1. A Monomeric 310-Helix Is Formed in Water by a 13-Residue Peptide Representing the Neutralizing Determinant of HIV-1 on gp41,

2. A Conserved Tryptophan-Rich Motif in the Membrane-Proximal Region of the Human Immunodeficiency Virus Type 1 gp41 Ectodomain Is Important for Env-Mediated Fusion and Virus Infectivity

3. Enhancement of α-Helicity in the HIV-1 Inhibitory Peptide DP178 Leads to an Increased Affinity for Human Monoclonal Antibody 2F5 but Does Not Elicit Neutralizing Responses in Vitro

4. Cross-clade neutralization of primary isolates of human immunodeficiency virus type 1 by human monoclonal antibodies and tetrameric CD4-IgG

5. Anti-Human Immunodeficiency Virus Type 1 (HIV-1) Antibodies 2F5 and 4E10 Require Surprisingly Few Crucial Residues in the Membrane-Proximal External Region of Glycoprotein gp41 To Neutralize HIV-1

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