Evidence map›Paper›PMID 26791986›Full record

ArticleMethods in enzymology2016

Hydrogen Exchange Mass Spectrometry.

Leland Mayne

Abstract read
In one paragraph

Article in Methods in enzymology, 2016. 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. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Mapping HDX-MS Data to Protein Conformations through Training Ensemble-Based Models.Journal of the American Society for Mass Spectrometry · 2023
    Article
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  14. Review
  15. Article
  16. Review
  17. Article
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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

1 author.

Leland MayneJohnson Research Foundation, Department of Biochemistry and Biophysics, Perelman School of Medicine, The University of Pennsylvania, Philadelphia, Pennsylvania, USA. Electronic address: mayne@mail.med.upenn.edu.

Funding

Protein structure and function by hydrogen exchange mass spectrometry analysisR01GM031847 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI ENGLANDER, S. WALTER · 1985 to 2017
$6.3M
NIGMS NIH HHS R01 GM031847
6 · The paper itself

Abstract

Hydrogen exchange (HX) methods can reveal much about the structure, energetics, and dynamics of proteins. The addition of mass spectrometry (MS) to an earlier fragmentation-separation HX analysis now extends HX studies to larger proteins at high structural resolution and can provide information not available before. This chapter discusses experimental aspects of HX labeling, especially with respect to the use of MS and the analysis of MS data.

Indexed as

Deuterium Exchange MeasurementHydrogenMass SpectrometryMolecular WeightProteinsStaining and LabelingHydrogenProteinsEpitope mappingHDX-MSHX-MSHydrogen–deuterium exchangeHydrogen exchangeMass spectrometryProtein dynamicsProtein foldingProtein stabilityProtein structure

Identifiers

PMID26791986
PMCPMC5858910

What OpenQuestion holds

Textmetadata
LicenceTDM
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.