Evidence map›Paper›PMID 23360928›Full record

ArticleChemical communications (Cambridge, England)2013

Measuring protein reduction potentials using 15N HSQC NMR spectroscopy.

Samantha L Taylor, Harriet Crawley-Snowdon, Jane L Wagstaff, Michelle L Rowe, Mark Shepherd, Richard A Williamson, Mark J Howard

Abstract read
In one paragraph

Article in Chemical communications (Cambridge, England), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

7 authors.

Samantha L TaylorSchool of Bioscience, University of Kent, Canterbury, Kent, CT2 7NJ, UK.
Harriet Crawley-Snowdon
Jane L Wagstaff
Michelle L Rowe
Mark Shepherd
Richard A Williamson
Mark J Howard

Funding

Wellcome Trust 091163/Z/10/ZWellcome Trust 093125Wellcome Trust 093125/B/10/Z
6 · The paper itself

Abstract

NMR spectroscopy was used to measure reduction potentials of four redox proteins by following multiple (15)N HSQC protein resonances across a titration series using mixtures of oxidised and reduced glutathione. Results for PDI a, PDI ab and DsbA agree with the literature and our result for ERp18 confirms this protein as an oxidoreductase of comparable or greater reducing strength than PDI a.

Indexed as

Nuclear Magnetic Resonance, BiomolecularEscherichia coli ProteinsGlutathioneNitrogen IsotopesOxidation-ReductionProtein Disulfide-IsomerasesdsbA protein, E coliEscherichia coli ProteinsGlutathioneNitrogen IsotopesProtein Disulfide-Isomerases

Identifiers

PMID23360928
PMCPMC4340554

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.