Literature DB >> 12221296

Type IA DNA topoisomerases: strictly one step at a time.

James J Champoux1.   

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Year:  2002        PMID: 12221296      PMCID: PMC129386          DOI: 10.1073/pnas.202483499

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


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  11 in total

Review 1.  DNA topoisomerases: structure, function, and mechanism.

Authors:  J J Champoux
Journal:  Annu Rev Biochem       Date:  2001       Impact factor: 23.643

Review 2.  Cellular roles of DNA topoisomerases: a molecular perspective.

Authors:  James C Wang
Journal:  Nat Rev Mol Cell Biol       Date:  2002-06       Impact factor: 94.444

3.  The mechanism of type IA topoisomerases.

Authors:  N H Dekker; V V Rybenkov; M Duguet; N J Crisona; N R Cozzarelli; D Bensimon; V Croquette
Journal:  Proc Natl Acad Sci U S A       Date:  2002-08-07       Impact factor: 11.205

Review 4.  DNA topoisomerases.

Authors:  J C Wang
Journal:  Annu Rev Biochem       Date:  1996       Impact factor: 23.643

5.  Homologous pairing in stretched supercoiled DNA.

Authors:  T R Strick; V Croquette; D Bensimon
Journal:  Proc Natl Acad Sci U S A       Date:  1998-09-01       Impact factor: 11.205

6.  Vaccinia DNA topoisomerase I: evidence supporting a free rotation mechanism for DNA supercoil relaxation.

Authors:  J T Stivers; T K Harris; A S Mildvan
Journal:  Biochemistry       Date:  1997-04-29       Impact factor: 3.162

7.  Bacterial DNA topoisomerase I can relax positively supercoiled DNA containing a single-stranded loop.

Authors:  K Kirkegaard; J C Wang
Journal:  J Mol Biol       Date:  1985-10-05       Impact factor: 5.469

8.  Single-molecule analysis of DNA uncoiling by a type II topoisomerase.

Authors:  T R Strick; V Croquette; D Bensimon
Journal:  Nature       Date:  2000-04-20       Impact factor: 49.962

9.  Crystal structure of a complex of a type IA DNA topoisomerase with a single-stranded DNA molecule.

Authors:  A Changela; R J DiGate; A Mondragón
Journal:  Nature       Date:  2001-06-28       Impact factor: 49.962

10.  Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I.

Authors:  C D Lima; J C Wang; A Mondragón
Journal:  Nature       Date:  1994-01-13       Impact factor: 49.962

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  7 in total

1.  RMI1 promotes DNA replication fork progression and recovery from replication fork stress.

Authors:  Jay Yang; Lara O'Donnell; Daniel Durocher; Grant W Brown
Journal:  Mol Cell Biol       Date:  2012-05-29       Impact factor: 4.272

2.  A method to estimate the elastic energy stored in braided DNA molecules using hydrodynamic equations.

Authors:  Mónica Fernández-Sierra; Violeta Delgado-Martí; Jorge E Colón-García; Edwin Quiñones
Journal:  Chem Phys       Date:  2011-05-26       Impact factor: 2.348

3.  Defective p53 engagement after the induction of DNA damage in cells deficient in topoisomerase 3beta.

Authors:  Subhasis Mohanty; Terrence Town; Tomohito Yagi; Christina Scheidig; Kelvin Y Kwan; Heather G Allore; Richard A Flavell; Albert C Shaw
Journal:  Proc Natl Acad Sci U S A       Date:  2008-03-26       Impact factor: 11.205

Review 4.  DNA topoisomerase I inhibitors: chemistry, biology, and interfacial inhibition.

Authors:  Yves Pommier
Journal:  Chem Rev       Date:  2009-07       Impact factor: 60.622

5.  Investigating direct interaction between Escherichia coli topoisomerase I and RecA.

Authors:  Srikanth Banda; Purushottam Babu Tiwari; Yesim Darici; Yuk-Ching Tse-Dinh
Journal:  Gene       Date:  2016-03-19       Impact factor: 3.688

Review 6.  Closing the DNA replication cycle: from simple circular molecules to supercoiled and knotted DNA catenanes.

Authors:  Jorge B Schvartzman; Pablo Hernández; Dora B Krimer; Julien Dorier; Andrzej Stasiak
Journal:  Nucleic Acids Res       Date:  2019-08-22       Impact factor: 16.971

7.  Topoisomerase II inhibition involves characteristic chromosomal expression patterns.

Authors:  Susanne Reymann; Jürgen Borlak
Journal:  BMC Genomics       Date:  2008-07-08       Impact factor: 3.969

  7 in total

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