(Q27660224)

7

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David K. Chalmers

object named as

David K Chalmers

6

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Michael W Parker

object named as

Michael W Parker

8

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author name string

Stephen J Headey

2

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Dharshini Jeevarajah

3

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David I Rhodes

4

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John Deadman

Relationship between the oligomeric status of HIV-1 integrase on DNA and enzymatic activity

5

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language of work or name

English

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publication date

16 April 2010

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published in

FEBS Letters

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volume

584

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issue

8

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page(s)

1455-62

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cites work

1 reference

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Molecular mechanisms of HIV integration and therapeutic intervention

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Discovery of raltegravir, a potent, selective orally bioavailable HIV-integrase inhibitor for the treatment of HIV-AIDS infection

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Raltegravir, etravirine, and ritonavir-boosted darunavir: a safe and successful rescue regimen for multidrug-resistant HIV-1 infection.

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Potent inhibitors of HIV-1 integrase display a two-step, slow-binding inhibition mechanism which is absent in a drug-resistant T66I/M154I mutant

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Comparison of raltegravir and elvitegravir on HIV-1 integrase catalytic reactions and on a series of drug-resistant integrase mutants

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Discovery of a small-molecule HIV-1 integrase inhibitor-binding site

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In search of small molecules blocking interactions between HIV proteins and intracellular cofactors

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Symmetrical 1-pyrrolidineacetamide showing anti-HIV activity through a new binding site on HIV-1 integrase

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An allosteric mechanism for inhibiting HIV-1 integrase with a small molecule

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Identification of an inhibitor-binding site to HIV-1 integrase with affinity acetylation and mass spectrometry

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

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The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations

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Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: A model for viral DNA binding

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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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Identification of a small-molecule binding site at the dimer interface of the HIV integrase catalytic domain

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Solution structure of the His12 --> Cys mutant of the N-terminal zinc binding domain of HIV-1 integrase complexed to cadmium

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

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

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LEDGF/p75 interacts with divergent lentiviral integrases and modulates their enzymatic activity in vitro

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Identification of an evolutionarily conserved domain in human lens epithelium-derived growth factor/transcriptional co-activator p75 (LEDGF/p75) that binds HIV-1 integrase

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HIV-1 integrase forms stable tetramers and associates with LEDGF/p75 protein in human cells

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Globoidnan A: a lignan from Eucalyptus globoidea inhibits HIV integrase

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Structural definition of a conserved neutralization epitope on HIV-1 gp120

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Chicoric acid analogues as HIV-1 integrase inhibitors

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