HIV-1 Gag Processing Intermediates Trans-dominantly Interfere with HIV-1 Infectivity (original) (raw)

The virus-associated human immunodeficiency virus type 1 Gag-Pol carrying an active protease domain in the matrix region is severely defective both in autoprocessing and in trans processing of gag particles

Fu-der Wang

Virology, 2004

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Extensive Regions ofpolAre Required for Efficient Human Immunodeficiency Virus Polyprotein Processing and Particle Maturation

Andrew Borman

Virology, 1996

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Analysis of HIV particle formation using transient expression of subviral constructs in mammalian cells

Volker Brinkmann

Virology, 1992

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Induced maturation of human immunodeficiency virus

Jan Konvalinka

Journal of virology, 2014

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Removal of human immunodeficiency virus type 1 (HIV-1) protease inhibitors from preparations of immature HIV-1 virions does not result in an increase in infectivity or the appearance of mature morphology

TOMINAGA FUKAZAWA

Antimicrobial Agents and Chemotherapy, 1997

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Initial Cleavage of the Human Immunodeficiency Virus Type 1 GagPol Precursor by Its Activated Protease Occurs by an Intramolecular Mechanism

Ben Dunn

Journal of Virology, 2004

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Processing sites in the human immunodeficiency virus type 1 (HIV1) Gag-Pro-Pol precursor are cleaved by the viral protease at different rates

Steve Pettit

Retrovirology, 2005

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Constitutive production of nonenveloped human immunodeficiency virus type 1 particles by a mammalian cell line and effects of a protease inhibitor on particle maturation

Charles Craik

Antimicrobial Agents and Chemotherapy, 1994

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Ordered Processing of the Human Immunodeficiency Virus Type 1 GagPol Precursor Is Influenced by the Context of the Embedded Viral Protease

jose clemente

Journal of Virology, 2005

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Comparison of Human Immunodeficiency Virus Type 1 Pr55 Gag and Pr160 Gag-Pol Processing Intermediates That Accumulate in Primary and Transformed Cells Treated with Peptidic and Nonpeptidic Protease Inhibitors

Richard Collins III

Antimicrobial Agents and Chemotherapy, 2000

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Proteasome inhibition interferes with Gag polyprotein processing, release, and maturation of HIV-1 and HIV-2

Elena Chertova

Proceedings of the National Academy of Sciences, 2000

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Triggering HIV polyprotein processing by light using rapid photodegradation of a tight-binding protease inhibitor

Petr Pachl, Jiří Schimer, Jan Weber

Nature Communications, 2015

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HIV-1 Assembly, Release and Maturation

Nathalie Chazal

World Journal of AIDS, 2011

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Replacement of the P1 amino acid of human immunodeficiency virus type 1 Gag processing sites can inhibit or enhance the rate of cleavage by the viral protease

Steve Pettit

Journal of Virology, 2002

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Active human immunodeficiency virus protease is required for viral infectivity

Emilio Emini

Proceedings of the …, 1988

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A peptide inhibitor of HIV-1 assembly in vitro

Ursula Dietrich

Nature Structural & Molecular Biology, 2005

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Gag-Pol Processing during HIV-1 Virion Maturation: A Systems Biology Approach

Tamas Turanyi

PLoS Computational Biology, 2013

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Activity of Human Immunodeficiency Virus Type 1 Protease Inhibitors against the Initial Autocleavage in Gag-Pol Polyprotein Processing

David Davis, Ronald Desrosiers, Bruno Sargueil, Jules Deforges

Antimicrobial Agents and Chemotherapy, 2012

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Analysis of the initiating events in HIV-1 particle assembly and genome packaging

Sebla Döner

PLoS pathogens, 2010

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Conserved Cysteines of the Human Immunodeficiency Virus Type 1 Protease Are Involved in Regulation of Polyprotein Processing and Viral Maturation of Immature Virions

David Davis

Journal of Virology, 1999

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Trans-dominant inhibitory human immunodeficiency virus type 1 protease monomers prevent protease activation and virion maturation

Charles Craik

Proceedings of the National Academy of Sciences, 1995

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Vif Is Largely Absent from Human Immunodeficiency Virus Type 1 Mature Virions and Associates Mainly with Viral Particles Containing Unprocessed Gag

David Volsky

Journal of Virology, 2001

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The Initial Step in Human Immunodeficiency Virus Type 1 GagProPol Processing Can Be Regulated by Reversible Oxidation

David Davis, Erin Soule

PLoS ONE, 2010

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Positive and Negative Aspects of the Human Immunodeficiency Virus Protease: Development of Inhibitors versus Its Role in AIDS Pathogenesis

Ronald Luftig

Microbiology and Molecular Biology Reviews, 2000

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Human immunodeficiency virus protease expressed in Escherichia coli exhibits autoprocessing and specific maturation of the gag precursor

Thomas Meek

Proceedings of the National Academy of Sciences, 1987

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Preparation of recombinant HIV-1 gag protein and assembly of virus-like particles in vitro

Siddhartha Datta

Methods in molecular biology (Clifton, N.J.), 2009

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Proteolytic activity in vivo and encapsidation of recombinant human immunodeficiency virus type 1 proteinase expressed in baculovirus-infected cells

Bernard Gay

The Journal of general virology, 1997

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Proteolytic Processing of the Human Immunodeficiency Virus Envelope Glycoprotein Precursor Decreases Conformational Flexibility

Ignacio López Salas

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Modulation of HIV-like particle assembly in vitro by inositol phosphates

Stephen Fox

Proceedings of the National Academy of Sciences, 2001

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Elimination of Protease Activity Restores Efficient Virion Production to a Human Immunodeficiency Virus Type 1 Nucleocapsid Deletion Mutant

Elena Chertova

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Characterization of human immunodeficiency virus type 1 mutantswith decreased sensitivity to proteinase inhibitor Ro 31-8959

Jan Mous

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The Packaging and Maturation of the HIV-1 Pol Proteins

Gilda Tachedjian

Current HIV Research, 2005

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Functional RT and IN incorporated into HIV-1 particles independently of the Gag/Pol precursor protein

John Kappes

The EMBO Journal, 1997

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Time Course of Gag Protein Assembly in HIV-1-Infected Cells: A Study by Immunoelectron Microscopy

Fedor Ciampor

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Human immunodeficiency virus type 1 Vif binds the viral protease by interaction with its N-terminal region

marina hutoran

The Journal of general virology, 2002

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