Evidence map›Paper›PMID 10220384›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Protein footprinting at cysteines: probing ATP-modulated contacts in cysteine-substitution mutants of yeast DNA topoisomerase II.

B P Tu, J C Wang

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Protein Structural Analysis via Mass Spectrometry-Based Proteomics.Advances in experimental medicine and biology · 2016
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Isotope-coded affinity tags with tunable reactivities for protein footprinting.Angewandte Chemie (International ed. in English) · 2008
    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.

B P TuDepartment of Molecular and Cellular Biology, Harvard University, 7 Divinity Avenue, Cambridge, MA 02138, USA.
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 GM24544NIGMS NIH HHS R01 GM024544NIGMS NIH HHS R37 GM024544
6 · The paper itself

Abstract

Cysteine-substitution mutants of yeast DNA topoisomerase II were used to test footprinting of the enzyme by 2-nitro-5-thiocyanobenzoate, which cyanylates exposed cysteines in a native protein for peptide cleavage at the cyanylated sites upon unfolding and incubating the protein at pH 9. For a mutant enzyme containing a single cysteine, the extent of peptide cleavage was found to reflect the accessibility of the residue in the native protein. For proteins with multiple cysteines, however, such a correlation was obscured by the transfer of cyano groups from modified to unmodified cysteines during incubation of the unfolded protein at pH 9; accessibilities of the cysteinyl residues in a native protein could be assessed only if cyano shuffling was prevented by blocking uncyanylated sulfhydryls with a second thiol reagent. The successive use of two reagents in cysteine footprinting was applied in probing the ATP-modulated formation of contacts in yeast DNA topoisomerase II.

Indexed as

Amino Acid SubstitutionCysteineDNA FootprintingDNA Topoisomerases, Type IIFungal ProteinsMutationSaccharomyces cerevisiaeCysteineDNA Topoisomerases, Type IIFungal Proteins

Identifiers

PMID10220384
PMCPMC21782

What OpenQuestion holds

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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.