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HIV-1 reverse transcriptase and integrase enzymes physically interact and inhibit each other


Tasara, T; Maga, G; Hottiger, M O; Hübscher, U (2001). HIV-1 reverse transcriptase and integrase enzymes physically interact and inhibit each other. FEBS Letters, 507(1):39-44.

Abstract

Ordered molecular interactions and structural changes must take place within the human immunodeficiency virus type 1 (HIV-1) preintegration complex at various stages for successful viral replication. We demonstrate both physical and biochemical interactions between HIV-1 reverse transcriptase and integrase enzymes. This interaction may have implications on the in vivo functions of the two enzymes within the HIV-1 replication complex. It may be one of the various molecular interactions, which facilitate efficient HIV-1 replication within the target cells.

Abstract

Ordered molecular interactions and structural changes must take place within the human immunodeficiency virus type 1 (HIV-1) preintegration complex at various stages for successful viral replication. We demonstrate both physical and biochemical interactions between HIV-1 reverse transcriptase and integrase enzymes. This interaction may have implications on the in vivo functions of the two enzymes within the HIV-1 replication complex. It may be one of the various molecular interactions, which facilitate efficient HIV-1 replication within the target cells.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:05 Vetsuisse Faculty > Department of Molecular Mechanisms of Disease
07 Faculty of Science > Department of Molecular Mechanisms of Disease
Dewey Decimal Classification:570 Life sciences; biology
Scopus Subject Areas:Life Sciences > Biophysics
Life Sciences > Structural Biology
Life Sciences > Biochemistry
Life Sciences > Molecular Biology
Life Sciences > Genetics
Life Sciences > Cell Biology
Language:English
Date:19 October 2001
Deposited On:11 Feb 2008 12:18
Last Modified:23 Jan 2022 08:38
Publisher:Elsevier
ISSN:0014-5793
OA Status:Closed
Publisher DOI:https://doi.org/10.1016/S0014-5793(01)02945-3
Related URLs:http://www.sciencedirect.com/science/journal/00145793
PubMed ID:11682056
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