(Q27666603)

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Fragment-based design of ligands targeting a novel site on the integrase enzyme of human immunodeficiency virus 1

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title

Fragment-based design of ligands targeting a novel site on the integrase enzyme of human immunodeficiency virus 1 (English)

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main subject

HIV type 1

object named as

human immunodeficiency virus 1

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Jerome Wielens

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Martin J Scanlon

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David K Chalmers

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Michael W Parker

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Stephen J Headey

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John J Deadman

series ordinal

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David I Rhodes

series ordinal

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Giang T Le

series ordinal

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publication date

7 February 2011

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258-61

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cites work

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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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HIV resistance to raltegravir

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Rational design of small-molecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication

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A decade of fragment-based drug design: strategic advances and lessons learned

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Crystal structure of the HIV-1 integrase core domain in complex with sucrose reveals details of an allosteric inhibitory binding site

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Discovering high-affinity ligands for proteins: SAR by NMR

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

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Solution conformation and dynamics of the HIV-1 integrase core domain

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Class II integrase mutants with changes in putative nuclear localization signals are primarily blocked at a postnuclear entry step of human immunodeficiency virus type 1 replication

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HIV-1 integrase is capable of targeting DNA to the nucleus via an importin alpha/beta-dependent mechanism.

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Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies.

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Peptide HIV-1 integrase inhibitors from HIV-1 gene products.

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Four-tiered pi interaction at the dimeric interface of HIV-1 integrase critical for DNA integration and viral infectivity.

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Ligand efficiency: a useful metric for lead selection

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Characterization of Ligand Binding by Saturation Transfer Difference NMR Spectroscopy

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7 January 2021

based on heuristic

inferred from DOI database lookup

Structure-based mutagenesis of the catalytic domain of human immunodeficiency virus type 1 integrase.

1 reference

stated in

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reference URL

https://api.crossref.org/works/10.1002%2FCMDC.201000483

retrieved

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based on heuristic

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Identifiers

DOI

10.1002/CMDC.201000483

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PubMed publication ID

21275048

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ResearchGate publication ID

49792668

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