Folding of HIV‐1 Envelope glycoprotein involves extensive isomerization of disulfide bonds and conformation‐dependent leader peptide cleavage-Reference-Cited by-同舟云学术

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Folding of HIV‐1 Envelope glycoprotein involves extensive isomerization of disulfide bonds and conformation‐dependent leader peptide cleavage

Published:2003-06 Issue:9 Volume:17 Page:1058-1067
ISSN:0892-6638
Container-title:The FASEB Journal
language:en
Short-container-title:FASEB j.

Author:

LAND AAFKE¹,ZONNEVELD DUCO²,BRAAKMAN INEKE¹

Affiliation:

1. Department of Bio-Organic Chemistry 1Utrecht UniversityUtrecht

2. Department of BiochemistryAcademic Medical CenterAmsterdamThe Netherlands

Publisher

Wiley

Subject

Genetics,Molecular Biology,Biochemistry,Biotechnology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1096/fj.02-0811com

Reference56 articles.

1. Major Glycoprotein Antigens That Induce Antibodies in AIDS Patients Are Encoded by HTLV-III

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;Salzwedel K.;J. Virol.,1999

3. Nucleotide sequence of the AIDS virus, LAV

4. Assignment of intra-chain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells;Leonard C. K.;J. Biol. Chem.,1990

5. Folding, interaction with GRP78-BiP, assembly, and transport of the human immunodeficiency virus type 1 envelope protein

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