(Q40666094)

English

Human immunodeficiency virus type-1 integrase containing a glycine to serine mutation at position 140 is attenuated for catalysis and resistant to integrase inhibitors

scientific article published on February 2003

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Human immunodeficiency virus type-1 integrase containing a glycine to serine mutation at position 140 is attenuated for catalysis and resistant to integrase inhibitors (English)

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

author name string

Peter J King

1

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Deborah J Lee

2

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Ryan A Reinke

3

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Joseph G Victoria

4

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Keola Beale

5

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

W Edward Robinson

6

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

language of work or name

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publication date

1 February 2003

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

306

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

1

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

147-161

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

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Structural determinants of metal-induced conformational changes in HIV-1 integrase

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A metal-induced conformational change and activation of HIV-1 integrase

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HIV-1 integrase inhibitors that compete with the target DNA substrate define a unique strand transfer conformation for integrase

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Three new structures of the core domain of HIV-1 integrase: an active site that binds magnesium

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The mobility of an HIV-1 integrase active site loop is correlated with catalytic activity

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Inhibitors of strand transfer that prevent integration and inhibit HIV-1 replication in cells

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Photo-cross-linking studies suggest a model for the architecture of an active human immunodeficiency virus type 1 integrase-DNA complex

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Critical contacts between HIV-1 integrase and viral DNA identified by structure-based analysis and photo-crosslinking

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Computer analysis of retroviral pol genes: assignment of enzymatic functions to specific sequences and homologies with nonviral enzymes

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Structure-activity relationships: analogues of the dicaffeoylquinic and dicaffeoyltartaric acids as potent inhibitors of human immunodeficiency virus type 1 integrase and replication

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Residues critical for retroviral integrative recombination in a region that is highly conserved among retroviral/retrotransposon integrases and bacterial insertion sequence transposases

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Structure of the catalytic domain of avian sarcoma virus integrase with a bound HIV-1 integrase-targeted inhibitor

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Crystal structures of the catalytic domain of HIV-1 integrase free and complexed with its metal cofactor: high level of similarity of the active site with other viral integrases

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Intermolecular disintegration and intramolecular strand transfer activities of wild-type and mutant HIV-1 integrase

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Lamellarin alpha 20-sulfate, an inhibitor of HIV-1 integrase active against HIV-1 virus in cell culture

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Dicaffeoyltartaric acid analogues inhibit human immunodeficiency virus type 1 (HIV-1) integrase and HIV-1 replication at nontoxic concentrations

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Structure of the termini of DNA intermediates in the integration of retroviral DNA: dependence on IN function and terminal DNA sequence

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Biochemical Characterization of the HIV-1 Integrase 3‘-Processing Activity and Its Inhibition by Phosphorothioate Oligonucleotides†

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Resistance to the anti-human immunodeficiency virus type 1 compound L-chicoric acid results from a single mutation at amino acid 140 of integrase

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Identifiers

10.1016/S0042-6822(02)00042-9

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

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