Mechanism of inhibition of HIV-1 integrase by G-tetrad-forming oligonucleotides in Vitro (Q38312462)

2 September 2017

title

Mechanism of inhibition of HIV-1 integrase by G-tetrad-forming oligonucleotides in Vitro (English)

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2 September 2017

Jing N

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2 September 2017

Marchand C

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2 September 2017

Liu J

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2 September 2017

Mitra R

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2 September 2017

Hogan ME

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2 September 2017

Pommier Y

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2 September 2017

language of work or name

English

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publication date

1 July 2000

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Journal of Biological Chemistry

2 September 2017

published in

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2 September 2017

volume

275

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2 September 2017

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2 September 2017

page(s)

21460-21467

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Toward improved anti-HIV chemotherapy: therapeutic strategies for intervention with HIV infections

2 September 2017

cites work

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Suppression of human immunodeficiency virus type 1 activity in vitro by oligonucleotides which form intramolecular tetrads

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Ion Selective Folding of Loop Domains in a Potent Anti-HIV Oligonucleotide

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Potassium-induced loop conformational transition of a potent anti-HIV oligonucleotide

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Structure-activity of tetrad-forming oligonucleotides as a potent anti-HIV therapeutic drug

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Stability-activity relationships of a family of G-tetrad forming oligonucleotides as potent HIV inhibitors. A basis for anti-HIV drug design

21 January 2018

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Solution structure of the N-terminal zinc binding domain of HIV-1 integrase

21 January 2018

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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

21 January 2018

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Molecular surface recognition: determination of geometric fit between proteins and their ligands by correlation techniques

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Long-distance potentials: an approach to the multiple-minima problem in ligand-receptor interaction.

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A DNA aptamer which binds to and inhibits thrombin exhibits a new structural motif for DNA.

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Three-dimensional solution structure of the thrombin-binding DNA aptamer d(GGTTGGTGTGGTTGG)

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Domains of the integrase protein of human immunodeficiency virus type 1 responsible for polynucleotidyl transfer and zinc binding

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Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases

21 January 2018

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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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Molecular mechanisms in retrovirus DNA integration

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Retroviral integrases and their cousins

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

21 January 2018

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Identification of a nucleotide binding site in HIV-1 integrase

21 January 2018

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Characterization of the DNA-binding activity of HIV-1 integrase using a filter binding assay

21 January 2018

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Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity

21 January 2018

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Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type I integrase protein

21 January 2018

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Characterization of a DNA binding domain in the C-terminus of HIV-1 integrase by deletion mutagenesis

21 January 2018

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Solution structure of the DNA binding domain of HIV-1 integrase

21 January 2018

1 reference

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The DNA-binding domain of HIV-1 integrase has an SH3-like fold

21 January 2018

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Mode of Interaction of G-Quartets with the Integrase of Human Immunodeficiency Virus Type 1

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M001436200

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2 September 2017

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