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Structure of a HIV-1 IN-Allosteric inhibitor complex at 2.93 Å resolution: Routes to inhibitor optim...

Structure of a HIV-1 IN-Allosteric inhibitor complex at 2.93 Å resolution: Routes to inhibitor optim...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_2802052797

Structure of a HIV-1 IN-Allosteric inhibitor complex at 2.93 Å resolution: Routes to inhibitor optimization

About this item

Full title

Structure of a HIV-1 IN-Allosteric inhibitor complex at 2.93 Å resolution: Routes to inhibitor optimization

Publisher

United States: Public Library of Science

Journal title

PLoS pathogens, 2023-03, Vol.19 (3), p.e1011097

Language

English

Formats

Publication information

Publisher

United States: Public Library of Science

More information

Scope and Contents

Contents

HIV integrase (IN) inserts viral DNA into the host genome and is the target of the strand transfer inhibitors (STIs), a class of small molecules currently in clinical use. Another potent class of antivirals is the allosteric inhibitors of integrase, or ALLINIs. ALLINIs promote IN aggregation by stabilizing an interaction between the catalytic core...

Alternative Titles

Full title

Structure of a HIV-1 IN-Allosteric inhibitor complex at 2.93 Å resolution: Routes to inhibitor optimization

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_plos_journals_2802052797

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_2802052797

Other Identifiers

ISSN

1553-7374,1553-7366

E-ISSN

1553-7374

DOI

10.1371/journal.ppat.1011097

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