Evidence map›Paper›PMID 23436701›Full record

ReviewProtein science : a publication of the Protein Society2013

Mass spectrometry-based methods to study protein architecture and dynamics.

Igor A Kaltashov, Cedric E Bobst, Rinat R Abzalimov

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. Article
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  7. Review
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  11. Article
  12. Review
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  15. Review
  16. Article
  17. Reference Parameters for Protein Hydrogen Exchange Rates.Journal of the American Society for Mass Spectrometry · 2018
    Article
  18. Article
  19. Co(II) and Ni(II) binding of theThe Journal of biological chemistry · 2018
    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

3 authors.

Igor A KaltashovDepartment of Chemistry, University of Massachusetts-Amherst, Amherst, Massachusetts, USA. Kaltashov@chem.umass.edu
Cedric E Bobst
Rinat R Abzalimov

Funding

PROTEIN FOLDING DYNAMICS BY MASS SPECTROMETRYR01GM061666 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI KALTASHOV, IGOR A · 2000 to 2013
$3.4M
NIGMS NIH HHS R01 GM061666
6 · The paper itself

Abstract

Mass spectrometry is now an indispensable tool in the armamentarium of molecular biophysics, where it is used for tasks ranging from protein sequencing and mapping of post-translational modifications to studies of higher order structure, conformational dynamics, and interactions of proteins with small molecule ligands and other biopolymers. This mini-review highlights several popular mass spectrometry-based tools that are now commonly used for structural studies of proteins beyond their covalent structure with a particular emphasis on hydrogen exchange and direct electrospray ionization mass spectrometry.

Indexed as

AnimalsDeuterium Exchange MeasurementHumansModels, MolecularProtein ConformationProtein Interaction MappingProteinsSpectrometry, Mass, Electrospray IonizationProteins

Identifiers

PMID23436701
PMCPMC3649255

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.