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Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gpl60

Data up to Jan 2025

Published1992
Citations572
References22

Total Citations Per Year

Abstract

References (22)

The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus

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Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease.

1992 • 628 citations

Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus

1988 • 608 citations

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1991 • 590 citations

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1988 • 442 citations

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1990 • 378 citations

Oligomeric structure of the human immunodeficiency virus type 1 envelope glycoprotein.

1990 • 360 citations

Expression of a human proprotein processing enzyme: correct cleavage of the von Willebrand factor precursor at a paired basic amino acid site.

1990 • 296 citations

Structural homology between the human fur gene product and the subtilisin-like protease encoded by yeast KEX2

1990 • 202 citations

Intracellular processing of the gp160 HIV-1 envelope precursor. Endoproteolytic cleavage occurs in a cis or medial compartment of the Golgi complex.

1990 • 190 citations

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1988 • 162 citations

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1992 • 156 citations

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1990 • 131 citations

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1992 • 130 citations

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1992 • 119 citations

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1989 • 103 citations

Mutations within the human immunodeficiency virus type 1 gp160 envelope glycoprotein alter its intracellular transport and processing

1991 • 75 citations

Expression of the human immunodeficiency virus envelope glycoprotein is restricted to basolateral surfaces of polarized epithelial cells

1989 • 73 citations

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1990 • 71 citations

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1992 • 10 citations

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Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gpl60 (1992) – Nature | Metascience Observatory Explorer