Lack of complex N-glycans on HIV-1 envelope glycoproteins preserves protein conformation and entry function-Reference-Cited by-同舟云学术

Lack of complex N-glycans on HIV-1 envelope glycoproteins preserves protein conformation and entry function

Published:2010-06 Issue:2 Volume:401 Page:236-247
ISSN:0042-6822
Container-title:Virology
language:en
Short-container-title:Virology

Author:

Eggink Dirk,Melchers Mark,Wuhrer Manfred,van Montfort Thijs,Dey Antu K.,Naaijkens Benno A.,David Kathryn B.,Le Douce Valentin,Deelder André M.,Kang Kenneth,Olson William C.,Berkhout Ben,Hokke Cornelis H.,Moore John P.,Sanders Rogier W.

Funder

AIDS fund (Amsterdam)

NIH

International AIDS Vaccine Initiative

Anton Meelmeijer fellowship

Organization for Scientific Research (NWO)

American Foundation for AIDS Research (amfAR)

Publisher

Elsevier BV

Subject

Virology

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3. Construction and characterization of soluble, cleaved, and stabilized trimeric Env proteins based on HIV type 1 Env subtype A;Beddows;AIDS Res. Hum. Retrovir.,2006

4. A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure;Binley;J. Virol.,2000

5. Enhancing the proteolytic maturation of human immunodeficiency virus type 1 envelope glycoproteins;Binley;J. Virol.,2002

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