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Literature DB >> 9397680

A putative nucleic acid-binding domain in Bloom's and Werner's syndrome helicases.

V Morozov¹, A R Mushegian, E V Koonin, P Bork.

Abstract

Entities: Disease

Mesh：

Substances：
DNA
DNA Helicases

Year: 1997 PMID： 9397680 DOI： 10.1016/s0968-0004(97)01128-6

Source DB: PubMed Journal: Trends Biochem Sci ISSN： 0968-0004 Impact factor: 13.807

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Cited

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59 in total

1. Potent inhibition of werner and bloom helicases by DNA minor groove binding drugs.

Authors: R M Brosh; J K Karow; E J White; N D Shaw; I D Hickson; V A Bohr
Journal: Nucleic Acids Res Date: 2000-06-15 Impact factor: 16.971

2. Comparative genomics and evolution of proteins involved in RNA metabolism.

Authors: Vivek Anantharaman; Eugene V Koonin; L Aravind
Journal: Nucleic Acids Res Date: 2002-04-01 Impact factor: 16.971

3. Domain mapping of Escherichia coli RecQ defines the roles of conserved N- and C-terminal regions in the RecQ family.

Authors: Douglas A Bernstein; James L Keck
Journal: Nucleic Acids Res Date: 2003-06-01 Impact factor: 16.971

4. Structural and functional homology between the RNAP(I) subunits A14/A43 and the archaeal RNAP subunits E/F.

Authors: Hedije Meka; Gregoire Daoust; Kristine Bourke Arnvig; Finn Werner; Peter Brick; Silvia Onesti
Journal: Nucleic Acids Res Date: 2003-08-01 Impact factor: 16.971

5. Contribution of domain structure to the RNA 3' end processing and degradation functions of the nuclear exosome subunit Rrp6p.

Authors: Seasson Phillips; J Scott Butler
Journal: RNA Date: 2003-09 Impact factor: 4.942

A putative nucleic acid-binding domain in Bloom's and Werner's syndrome helicases.

1. Potent inhibition of werner and bloom helicases by DNA minor groove binding drugs.

2. Comparative genomics and evolution of proteins involved in RNA metabolism.

3. Domain mapping of Escherichia coli RecQ defines the roles of conserved N- and C-terminal regions in the RecQ family.

4. Structural and functional homology between the RNAP(I) subunits A14/A43 and the archaeal RNAP subunits E/F.

5. Contribution of domain structure to the RNA 3' end processing and degradation functions of the nuclear exosome subunit Rrp6p.

6. Analysis of the unwinding activity of the dimeric RECQ1 helicase in the presence of human replication protein A.

Review 7. RecQ helicases; at the crossroad of genome replication, repair, and recombination.

8. Recruitment of Bacillus subtilis RecN to DNA double-strand breaks in the absence of DNA end processing.

9. Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain.

10. High-resolution structure of the E.coli RecQ helicase catalytic core.