Evidence map›Paper›PMID 23099262›Full record

ReviewBiochimica et biophysica acta2013

Hydrogen-exchange mass spectrometry for the study of intrinsic disorder in proteins.

Deepa Balasubramaniam, Elizabeth A Komives

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

45 citing papers in PubMed.

  1. Article
  2. Hyperactive 20Science advances · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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.

Deepa BalasubramaniamDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0378, USA.
Elizabeth A Komives

Funding

STRUCTURE AND STABILITY OF IKB/NF-KB COMPLEXESP01GM071862 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 2006 to 2016
$14.9M
MALDI TOF-TOF MASS SPECTROMETER: PROTEOMICSS10RR019897 · NCRR · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI KOMIVES, ELIZABETH A. · 2005 to 2005
$758k
2D NANO-FLOW MASS SPECTROMETRY SYSTEMS10RR022420 · NCRR · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 2006 to 2006
$500k
NCRR NIH HHS S10 RR019897NCRR NIH HHS S10 RR022420NIGMS NIH HHS P01 GM071862NIGMS NIH HHS P01-GM071862
6 · The paper itself

Abstract

Amide hydrogen/deuterium exchange detected by mass spectrometry (HXMS) is seeing wider use for the identification of intrinsically disordered parts of proteins. In this review, we discuss examples of how discovery of intrinsically disordered regions and their removal can aid in structure determination, biopharmaceutical quality control, the characterization of how post-translational modifications affect weak structuring of disordered regions, the study of coupled folding and binding, and the characterization of amyloid formation. This article is part of a Special Issue entitled: Mass spectrometry in structural biology.

Indexed as

Amino Acid SequenceDeuteriumDeuterium Exchange MeasurementHumansHydrogenMass SpectrometryMolecular Sequence DataProtein ConformationProtein FoldingProteinsDeuteriumHydrogenProteins

Identifiers

PMID23099262
PMCPMC3600394

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.