integrase

(redirected from Integrases)
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integrase

[′int·ə‚grās]
(biochemistry)
An enzyme that facilitates prophage integration into or excision from a bacterial chromosome.
References in periodicals archive ?
58%) and none of Class 1~3 integrases gene was detected in the studied isolates.
None of Class 1~3 integrases gene was detected in the studied isolates using the primers including the internal primers for Class 2 integron.
Three pair primers were used to obtain the converse regions sequence of the three classes integrase genes respectively while the variable region of the integrons were determined with another pair primers.
IntI1F###ACGAGCGCAAGGTTTCGGT###Class 1 integrase gene###565###[14]
Up-to-date, it has been reported that all known retroviral integrases present three domains: i) the zinc binding N-terminal (His12, His16, Cys40 and Cys43), ii) the catalytic core (Asp64, Asp116 and Glu152), and iii) the dsDNA-binding C-terminal domain (11, 12).
DCQAs have low cytotoxicity, present low molecular weight, have drug-like properties and are considered as promising inhibitors towards HIV-1 and HTLV-I integrases (23, 24).
Re-docking procedure for the three integrases models were performed afterwards to obtain the GlideScore data.
The book's first 12 chapters deal with the basic biology and structural understanding of HIV-1 integrase, with descriptions of the HIV life cycle, targets for anti-HIV agents, and integrase mechanisms and functions, along with a review of structural studies of retroviral integrases.
The papers focus on a range of chromosomal mutagenesis techniques for both prokaryotic and eukaryotic organisms, and present a variety of state-of-the-art methods in step-by-step laboratory format, including insertional gene disruptions, gene knockouts, stimulated homologous recombination techniques and novel tools based on integrases, eukaryotic transposons, triplex forming oligonucleotides, group II introns, and engineered site-directed nucleases.
This book comprehensively covers the mechanisms of action and inhibitor design for HIV-1 integrase.
But this book fills that gap and offers a valuable introduction to the field for the interdisciplinary scientists who will need to work together to design drugs that target HIV-1 integrase.
The pleiotropic nature of human immunodeficiency virus type 1 integrase mutations