Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural Determinants for HIV-1 Integrase Inhibition by β-Diketo Acids

1 Apr 2002

Abstract excerpt

Among all the HIV-1 integrase inhibitors, the beta-diketo acids (DKAs) represent a major lead in anti-HIV-1 integrase drug design. These derivatives inhibit the integration reaction in vitro with a strong specificity for the 3'-end joining step. They are also antiviral and inhibit integration in vivo. The aim of the present study has been to investigate the molecular interactions between DKAs and HIV-1 integrase....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biochemical and Molecular Research
Share to HIV/AIDS drug development and treatment
Share to HIV Research and Treatment

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 11805103
DOI: 10.1074/jbc.m110758200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural Determinants for HIV-1 Integrase Inhibition by β-Diketo AcidsPMID 11805103Read ↗

Azido-Containing Diketo Acid Derivatives Inhibit Human Immunodeficiency Virus Type 1 Integrase In Vivo and Influence the Frequency of Deletions at Two-Long-Terminal-Repeat-Circle JunctionsSemantic proximity Read ↗

Inhibitors of strand transfer that prevent integration and inhibit HIV-1 replication in cells.Semantic proximity Read ↗

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

The Hunt for HIV-1 Integrase InhibitorsSemantic proximity Read ↗

<i>N</i>-Substituted Quinolinonyl Diketo Acid Derivatives as HIV Integrase Strand Transfer Inhibitors and Their Activity against RNase H Function of Reverse TranscriptaseSemantic proximity Read ↗

Development of resistance against diketo derivatives of human immunodeficiency virus type 1 by progressive accumulation of integrase mutations.Semantic proximity Read ↗

Modeling, analysis, and validation of a novel HIV integrase structure provide insights into the binding modes of potent integrase inhibitors.Semantic proximity Read ↗

Human immunodeficiency virus type 1 (HIV-1) integrase: resistance to diketo acid integrase inhibitors impairs HIV-1 replication and integration and confers cross-resistance to L-chicoric acid.Semantic proximity Read ↗

Dihydroxythiophenes are novel potent inhibitors of human immunodeficiency virus integrase with a diketo acid-like pharmacophore.Semantic proximity Read ↗

HIV Integrase, a Brief Overview from Chemistry to TherapeuticsSemantic proximity Read ↗

The Integrase: An Overview of a Key Player Enzyme in the Antiviral ScenarioSemantic proximity Read ↗

Structure-Activity Relationships of HIV-1 Integrase Inhibitors - Enzyme- Ligand InteractionsSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.