Efavirenz enhances the proteolytic processing of an HIV-1 pol polyprotein precursor and reverse transcriptase homodimer formation (Q45218379)

10 December 2017

title

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

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10 December 2017

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Gilda Tachedjian

1

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Nicolas Sluis-Cremer

series ordinal

4

object named as

Nicolas Sluis-Cremer

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10 December 2017

Katie L Moore

2

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10 December 2017

Stephen P Goff

series ordinal

3

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10 December 2017

language of work or name

English

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publication date

1 January 2005

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10 December 2017

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10 December 2017

volume

579

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10 December 2017

issue

2

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10 December 2017

page(s)

379-384

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Characterization of highly immunogenic p66/p51 as the reverse transcriptase of HTLV-III/LAV.

10 December 2017

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Crystal structure of human immunodeficiency virus type 1 reverse transcriptase complexed with double-stranded DNA at 3.0 A resolution shows bent DNA

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Structural basis of asymmetry in the human immunodeficiency virus type 1 reverse transcriptase heterodimer

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In vivo processing of Pr160gag-pol from human immunodeficiency virus type 1 (HIV) in acutely infected, cultured human T-lymphocytes

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The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of GagPol cleavage

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Hydrophilic Peptides Derived from the Transframe Region of Gag-Pol Inhibit the HIV-1 Protease

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Autoprocessing of the HIV-1 protease using purified wild-type and mutated fusion proteins expressed at high levels in Escherichia coli

21 January 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

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The role of non-nucleoside reverse transcriptase inhibitors (NNRTIs) in the therapy of HIV-1 infection.

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Structure of the binding site for nonnucleoside inhibitors of the reverse transcriptase of human immunodeficiency virus type 1

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Locations of anti-AIDS drug binding sites and resistance mutations in the three-dimensional structure of HIV-1 reverse transcriptase. Implications for mechanisms of drug inhibition and resistance

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Nonnucleoside reverse transcriptase inhibitors are chemical enhancers of dimerization of the HIV type 1 reverse transcriptase

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Analysis of mutations and suppressors affecting interactions between the subunits of the HIV type 1 reverse transcriptase

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Rapid purification of homodimer and heterodimer HIV-1 reverse transcriptase by metal chelate affinity chromatography.

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Role of residues in the tryptophan repeat motif for HIV-1 reverse transcriptase dimerization

21 January 2018

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Purification and characterization of human immunodeficiency virus type 1 reverse transcriptase

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Conformational stability of dimeric HIV-1 and HIV-2 reverse transcriptases

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Human immunodeficiency virus type 1 reverse transcriptase dimer destabilization by 1-[Spiro[4"-amino-2",2" -dioxo-1",2" -oxathiole-5",3'-[2', 5'-bis-O-(tert-butyldimethylsilyl)-beta-D-ribofuranosyl]]]-3-ethylthy mine

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Human immunodeficiency virus type 1 Gag proteins are processed in two cellular compartments

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Overexpression of the HIV-1 gag-pol polyprotein results in intracellular activation of HIV-1 protease and inhibition of assembly and budding of virus-like particles

21 January 2018

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Human immunodeficiency virus proteinase dimer as component of the viral polyprotein prevents particle assembly and viral infectivity

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21 January 2018

Identifiers

DOI

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10 December 2017

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