HIV-1 gp41 and gp160 are hyperthermostable proteins in a mesophilic environment. Characterization of gp41 mutants. (Q30341167)

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26 December 2019

title

HIV-1 gp41 and gp160 are hyperthermostable proteins in a mesophilic environment. Characterization of gp41 mutants (English)

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26 December 2019

1

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26 December 2019

author name string

Frédéric Greco

2

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26 December 2019

Olivier Engel

3

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26 December 2019

Jean Dubayle

4

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26 December 2019

Joseline Dubayle

5

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26 December 2019

Audrey Kennel

6

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26 December 2019

Benoit Charloteaux

7

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26 December 2019

Robert Brasseur

8

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26 December 2019

Michel Chevalier

9

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26 December 2019

Regis Sodoyer

10

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26 December 2019

Raphaëlle El Habib

11

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26 December 2019

language of work or name

English

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publication date

1 April 2004

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26 December 2019

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26 December 2019

volume

271

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26 December 2019

issue

8

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26 December 2019

page(s)

1566-1579

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Expression, purification, and characterization of recombinant HIV gp140. The gp41 ectodomain of HIV or simian immunodeficiency virus is sufficient to maintain the retroviral envelope glycoprotein as a trimer

26 December 2019

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Helical interactions in the HIV-1 gp41 core reveal structural basis for the inhibitory activity of gp41 peptides

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HIV-1 gp41 tertiary structure studied by EPR spectroscopy

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The crystal structure of the SIV gp41 ectodomain at 1.47 A resolution

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Interactions between HIV-1 gp41 core and detergents and their implications for membrane fusion

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Functional analysis of the disulfide-bonded loop/chain reversal region of human immunodeficiency virus type 1 gp41 reveals a critical role in gp120-gp41 association

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The prefusogenic intermediate of HIV-1 gp41 contains exposed C-peptide regions.

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Immunization with recombinant canarypox vectors expressing membrane-anchored glycoprotein 120 followed by glycoprotein 160 boosting fails to generate antibodies that neutralize R5 primary isolates of human immunodeficiency virus type 1.

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[37] Reaction of protein sulfhydryl groups with Ellman's reagent.

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