Structural Analysis of a Highly Glycosylated and Unliganded gp120-Based Antigen Using Mass Spectrometry-Reference-Cited by-同舟云学术

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Structural Analysis of a Highly Glycosylated and Unliganded gp120-Based Antigen Using Mass Spectrometry

Published:2010-10-01 Issue:42 Volume:49 Page:9032-9045
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Wang Liwen¹,Qin Yali²,Ilchenko Serguei¹,Bohon Jen¹³,Shi Wuxian¹³,Cho Michael W.²,Takamoto Keiji⁴,Chance Mark R.¹³

Affiliation:

1. Center for Proteomics and Bioinformatics, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106

2. Department of Biomedical Sciences, College of Veterinary Medicine, Iowa State University, Ames, Iowa 50011

3. Center for Synchrotron Biosciences, Brookhaven National Laboratory, Upton, New York 11973

4. Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi1011332

Reference71 articles.

1. Fv fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase

2. Probability Analysis of Variational Crystallization and Its Application to gp120, The Exterior Envelope Glycoprotein of Type 1 Human Immunodeficiency Virus (HIV-1)

3. Structure of a V3-Containing HIV-1 gp120 Core

4. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody

5. Structures of HIV-1 gp120 Envelope Glycoproteins from Laboratory-Adapted and Primary Isolates

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