Terminal Interface Conformations Modulate Dimer Stability Prior to Amino Terminal Autoprocessing of HIV-1 Protease (Q27676717)

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Irene T Weber

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object named as

Irene T Weber

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author name string

Jane M Sayer

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John M Louis

Autocatalytic maturation, physical/chemical properties, and crystal structure of group N HIV-1 protease: Relevance to drug resistance

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language of work or name

English

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publication date

7 February 2012

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published in

Biochemistry

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volume

51

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issue

5

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page(s)

1041-50

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cites work

1 reference

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Efavirenz enhances the proteolytic processing of an HIV-1 pol polyprotein precursor and reverse transcriptase homodimer formation

27 November 2018

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Proteolytic processing of an HIV-1 pol polyprotein precursor: insights into the mechanism of reverse transcriptase p66/p51 heterodimer formation

27 November 2018

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High resolution crystal structures of HIV-1 protease with a potent non-peptide inhibitor (UIC-94017) active against multi-drug-resistant clinical strains

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Competitive inhibition of human immunodeficiency virus type-1 protease by the Gag-Pol transframe protein

27 November 2018

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Characterization of human immunodeficiency virus type-1 (HIV-1) particles that express protease-reverse transcriptase fusion proteins

27 November 2018

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Mutagenesis of the dimer interface residues of tethered and untethered HIV-1 protease result in differential activity and suggest multiple mechanisms of compensation

27 November 2018

1 reference

12 December 2020

Mutational and structural studies aimed at characterizing the monomer of HIV-1 protease and its precursor

1 reference

12 December 2020

Identification of amino acid residues in HIV-1 reverse transcriptase that are critical for the proteolytic processing of Gag-Pol precursors

1 reference

12 December 2020

Processing of X-ray diffraction data collected in oscillation mode

1 reference

12 December 2020

The structural stability of the HIV-1 protease

1 reference

12 December 2020

Identifiers

DOI

10.1021/BI201809S

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914495

914495

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1 reference