Literature DB >> 23277046

Superfamily 1 helicases .

Neville Surain Gilhooly1, Emma Jane Gwynn, Mark Simon Dillingham.   

Abstract

Superfamily 1 helicases are nucleic acid motor proteins that couple ATP hydrolysis to translocation along, and concomitant unwinding of, DNA or RNA. This is central to many aspects of cellular DNA and RNA metabolism and, accordingly, they are implicated in a wide range of nucleic acid processing events including DNA replication, recombination and repair as well as many aspects of RNA metabolism. This review discusses our current understanding of the structure, function and mechanism of Superfamily 1 helicases.

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Year:  2013        PMID： 23277046     DOI： 10.2741/s367

Source DB:  PubMed          Journal:  Front Biosci (Schol Ed)        ISSN： 1945-0516


  21 in total

Review 1.  Bacterial Transcription as a Target for Antibacterial Drug Development.

Authors:  Cong Ma; Xiao Yang; Peter J Lewis
Journal:  Microbiol Mol Biol Rev       Date:  2016-01-13       Impact factor: 11.056

2.  A parallel quadruplex DNA is bound tightly but unfolded slowly by pif1 helicase.

Authors:  Alicia K Byrd; Kevin D Raney
Journal:  J Biol Chem       Date:  2015-01-14       Impact factor: 5.157

3.  Direct Fluorescent Imaging of Translocation and Unwinding by Individual DNA Helicases.

Authors:  T L Pavankumar; J C Exell; S C Kowalczykowski
Journal:  Methods Enzymol       Date:  2016-10-18       Impact factor: 1.600

Review 4.  Mechanistic and biological considerations of oxidatively damaged DNA for helicase-dependent pathways of nucleic acid metabolism.

Authors:  Jack D Crouch; Robert M Brosh
Journal:  Free Radic Biol Med       Date:  2016-11-22       Impact factor: 7.376

5.  Molecular and Functional Characterization of RecD, a Novel Member of the SF1 Family of Helicases, from Mycobacterium tuberculosis.

Authors:  Shivendra Singh Dewhare; T G Umesh; K Muniyappa
Journal:  J Biol Chem       Date:  2015-03-23       Impact factor: 5.157

6.  Chemical modifications of DNA for study of helicase mechanisms.

Authors:  Kevin D Raney
Journal:  Bioorg Med Chem       Date:  2014-06-02       Impact factor: 3.641

7.  Mycobacterium tuberculosis DinG is a structure-specific helicase that unwinds G4 DNA: implications for targeting G4 DNA as a novel therapeutic approach.

Authors:  Roshan Singh Thakur; Ambika Desingu; Shivakumar Basavaraju; Shreelakshmi Subramanya; Desirazu N Rao; Ganesh Nagaraju
Journal:  J Biol Chem       Date:  2014-07-24       Impact factor: 5.157

8.  Human HELB is a processive motor protein that catalyzes RPA clearance from single-stranded DNA.

Authors:  Silvia Hormeno; Oliver J Wilkinson; Clara Aicart-Ramos; Sahiti Kuppa; Edwin Antony; Mark S Dillingham; Fernando Moreno-Herrero
Journal:  Proc Natl Acad Sci U S A       Date:  2022-04-06       Impact factor: 12.779

9.  Analysis of the PcrA-RNA polymerase complex reveals a helicase interaction motif and a role for PcrA/UvrD helicase in the suppression of R-loops.

Authors:  Inigo Urrutia-Irazabal; James R Ault; Frank Sobott; Nigel J Savery; Mark S Dillingham
Journal:  Elife       Date:  2021-07-19       Impact factor: 8.140

Review 10.  Discovering new medicines targeting helicases: challenges and recent progress.

Authors:  William R Shadrick; Jean Ndjomou; Rajesh Kolli; Sourav Mukherjee; Alicia M Hanson; David N Frick
Journal:  J Biomol Screen       Date:  2013-03-27
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