Inhibition of HIV-1 protease in infected T-lymphocytes by synthetic peptide analogues (Q28323197)

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D M Lambert

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G B Dreyer

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T J Carr

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T A Tomaszek

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M L Moore

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J E Strickler

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L J Hyland

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T J Matthews

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Meek TD

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29 October 2022

Lambert DM

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Dreyer GB

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Carr TJ

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Tomaszek TA Jr

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Moore ML

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Strickler JE

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Debouck C

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Hyland LJ

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Matthews TJ

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full work available at URL

29 October 2022

language of work or name

English

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publication date

4 January 1990

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http://www.nature.com/articles/343090a0

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https://api.crossref.org/works/10.1038/343090A0

http://www.nature.com/articles/343090a0.pdf

29 October 2022

file format

Portable Document Format

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29 October 2022

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343

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issue

6253

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page(s)

90-2

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Human immunodeficiency virus has an aspartic-type protease that can be inhibited by pepstatin A

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Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1

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Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease

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Synthetic and enzyme inhibition studies of pepstatin analogues containing hydroxyethylene and ketomethylene dipeptide isosteres

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HIV-1 protease specificity of peptide cleavage is sufficient for processing of gag and pol polyproteins

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Interaction between the human T-cell lymphotropic virus type IIIB envelope glycoprotein gp120 and the surface antigen CD4: role of carbohydrate in binding and cell fusion

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Detection, Isolation, and Continuous Production of Cytopathic Retroviruses (HTLV-III) from Patients with AIDS and Pre-AIDS

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Dimensions Publication ID

Identifiers

DOI

10.1038/343090A0

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1014472614

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