Evidence map›Paper›PMID 22528203›Full record

ArticleJournal of the American Society for Mass Spectrometry2012

Improved sequence resolution by global analysis of overlapped peptides in hydrogen/deuterium exchange mass spectrometry.

Piotr G Fajer, George M Bou-Assaf, Alan G Marshall

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.6field-weighted citation impact, top 11% of its field
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

11 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Gas-Phase Hydrogen/Deuterium Scrambling in Negative-Ion Mode Tandem Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2019
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Analytical Aspects of Hydrogen Exchange Mass Spectrometry.Annual review of analytical chemistry (Palo Alto, Calif.) · 2015
    Review
  9. Protein hydrogen exchange at residue resolution by proteolytic fragmentation mass spectrometry analysis.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  10. Article
  11. 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

3 authors at 2 institutions in 1 country.

Piotr G FajerInstitute of Molecular Biophysics, Biological Sciences Department, Florida State University, Tallahassee, FL 32306, USA. pfajer@fsu.edu
George M Bou-Assaf
Alan G Marshall
Florida State University · USNational High Magnetic Field Laboratory · US

Funding

Structural Mapping of Protein Complexes by Hydrogen/Deuterium ExchangeR01GM078359 · NIGMS · FLORIDA STATE UNIVERSITY · PI MARSHALL, ALAN G · 2006 to 2009
$1.2M
NIGMS NIH HHS GM 78359
6 · The paper itself

Abstract

Management of the enormous amount of data produced during solution-phase hydrogen/deuterium exchange monitored by mass spectrometry has stimulated software analysis development. The proteolysis step of the experiment generates multiple peptide fragments, most of which overlap. Prior automated data reduction algorithms extract the deuteration level for individual peptides, but do not exploit the additional information arising from fragment overlap. Here, we describe an algorithm that determines discrete rate constant values to each of the amide hydrogens in overlapped fragments. By considering all of the overlapped peptide segments simultaneously, sequence resolution can be improved significantly, sometimes to the individual amino acid level. We have validated the method with simulated deuterium uptake data for seven overlapped fragments of a poly-Ala nonapeptide, and then applied it to extract rate constant values for the first 29 N-terminal amino acids of C22A FK506-binding protein.

Indexed as

AlgorithmsAmino Acid SequenceComputer SimulationDeuterium Exchange MeasurementMass SpectrometryMolecular Sequence DataPeptide FragmentsProteolysisReproducibility of ResultsSequence Analysis, ProteinPeptide Fragments

Identifiers

PMID22528203
OpenAlexW2088531582

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.