Evidence map›Paper›PMID 24019478›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Protein hydrogen exchange at residue resolution by proteolytic fragmentation mass spectrometry analysis.

Zhong-Yuan Kan, Benjamin T Walters, Leland Mayne, S Walter Englander

Abstract readEvaluation Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing 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

81 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. HXMS: a standardized file format for HX-MS data.Bioinformatics (Oxford, England) · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Structure-resolved dynamics of type 2M von Willebrand disease.Journal of thrombosis and haemostasis : JTH · 2025
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Probing Antibody Structures by Hydrogen/Deuterium Exchange Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  19. Article
  20. Article

21 more citing papers are in PubMed but not listed here.

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

4 authors.

Zhong-Yuan KanJohnson Research Foundation, Department of Biochemistry and Biophysics, and Graduate Group in Biochemistry and Molecular Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104.
Benjamin T Walters
Leland Mayne
S Walter Englander

Funding

Protein structure and function by hydrogen exchange mass spectrometry analysisR01GM031847 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI ENGLANDER, S. WALTER · 1985 to 2017
$6.3M
STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008275 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2018
$6.0M
NIGMS NIH HHS GM031847NIGMS NIH HHS GM0827NIGMS NIH HHS R01 GM031847NIGMS NIH HHS T32 GM008275
6 · The paper itself

Abstract

Hydrogen exchange technology provides a uniquely powerful instrument for measuring protein structural and biophysical properties, quantitatively and in a nonperturbing way, and determining how these properties are implemented to produce protein function. A developing hydrogen exchange-mass spectrometry method (HX MS) is able to analyze large biologically important protein systems while requiring only minuscule amounts of experimental material. The major remaining deficiency of the HX MS method is the inability to deconvolve HX results to individual amino acid residue resolution. To pursue this goal we used an iterative optimization program (HDsite) that integrates recent progress in multiple peptide acquisition together with previously unexamined isotopic envelope-shape information and a site-resolved back-exchange correction. To test this approach, residue-resolved HX rates computed from HX MS data were compared with extensive HX NMR measurements, and analogous comparisons were made in simulation trials. These tests found excellent agreement and revealed the important computational determinants.

Indexed as

SoftwareAmino Acid SequenceBiophysicsHydrogenMagnetic Resonance SpectroscopyMass SpectrometryProteinsHydrogenProteinsHDX-MSisotope patternprotein biophysics

Identifiers

PMID24019478
PMCPMC3799349

What OpenQuestion holds

Textmetadata
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.