Evidence map›Paper›PMID 1720543›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1991

Proteolysis patterns of epitopically labeled yeast DNA topoisomerase II suggest an allosteric transition in the enzyme induced by ATP binding.

J E Lindsley, J C Wang

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

35 citing papers in PubMed.

  1. Article
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  13. Protein footprinting at cysteines: probing ATP-modulated contacts in cysteine-substitution mutants of yeast DNA topoisomerase II.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  14. Structural similarities between topoisomerases that cleave one or both DNA strands.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  15. Modulation of gyrase-mediated DNA cleavage and cell killing by ATP.Antimicrobial agents and chemotherapy · 1998
    Article
  16. Proteolytic mapping of heat shock transcription factor domains.Protein science : a publication of the Protein Society · 1996
    Article
  17. Article
  18. Article
  19. Article
  20. Structure and conformational changes of DNA topoisomerase II visualized by electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

J E LindsleyDepartment of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.
J C Wang

Funding

DNA TOPOISOMERASES--BIOLOGICAL FUNCTIONS &MECHANISMSR01GM024544 · NIGMS · HARVARD UNIVERSITY · PI WANG, JAMES C · 1985 to 2003
$2.2M
DNA TOPOISOMERASES: BIOLOGICAL FUNCTIONS AND MECHANISMSR37GM024544 · NIGMS · HARVARD UNIVERSITY · PI WANG, JAMES C · 1990 to 1999
–
NIGMS NIH HHS GM-24544
6 · The paper itself

Abstract

A cloned yeast TOP2 gene was modified to produce yeast DNA topoisomerase II (EC 5.99.1.3) epitopically labeled at its amino or carboxyl terminus. Limited digestion with SV8 endoprotease shows three distinct protease-sensitive sites in each polypeptide of the dimeric enzyme. These sites were mapped by immunostaining of the end-labeled proteolytic fragments resolved by SDS/polyacrylamide gel electrophoresis; two of the mapped locations were confirmed by sequencing the amino ends of two unlabeled peptic fragments. Proteolytic cleavage by SV8 endoprotease at a pair of sites corresponding to the carboxyl sides of Glu-411 and Glu-680 is modulated by the binding of the nonhydrolyzable ATP analogs adenosine 5'-[beta, gamma-imido]triphosphate (5'-adenylyl imidodiphosphate) and adenosine 5'-[gamma-thio]triphosphate: in their absence cleavage occurs predominantly at Glu-411; in the presence of either analog, cleavage occurs predominantly at Glu-680. These results are interpreted in terms of allosteric interdomainal movements in the type II DNA topoisomerase following the binding of ATP.

Indexed as

Adenosine TriphosphateAllosteric RegulationAmino Acid SequenceBinding SitesCloning, MolecularDNA Topoisomerases, Type IIEndopeptidasesEpitopesMacromolecular SubstancesMolecular Sequence DataMutagenesis, Site-DirectedPeptide FragmentsSaccharomyces cerevisiaeAdenosine TriphosphateDNA Topoisomerases, Type IIEndopeptidasesEpitopesMacromolecular SubstancesPeptide Fragments

Identifiers

PMID1720543
PMCPMC52953

What OpenQuestion holds

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Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.