Glycosylation Affects both the Three-Dimensional Structure and Antibody Binding Properties of the HIV-1IIIB GP120 Peptide RP135-Reference-Cited by-同舟云学术

Glycosylation Affects both the Three-Dimensional Structure and Antibody Binding Properties of the HIV-1IIIB GP120 Peptide RP135

Published:1997-09-01 Issue:36 Volume:36 Page:10846-10856
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Huang Xiaolin¹,Barchi, Joseph J.¹,Lung Feng-Di T.¹,Roller Peter P.¹,Nara Peter L.¹,Muschik Jeff¹,Garrity Robert R.¹

Affiliation:

1. Laboratory of Medicinal Chemistry, Division of Basic Sciences, National Cancer Institute, Bethesda, Maryland 20892, and Vaccine Resistant Diseases Section, Division of Basic Sciences, Frederick Cancer Research and Development Center, National Cancer Institute, Frederick, Maryland 21702

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi9703655

Reference73 articles.

1. The effects of glycosylation on peptide backbone conformation

2. Human immunodeficiency virus type 1 envelope glycoprotein is modified by O-linked oligosaccharides

3. CHARMM: A program for macromolecular energy, minimization, and dynamics calculations

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