Evidence map›Paper›PMID 20195578›Full record

ReviewAnalytical and bioanalytical chemistry2010

Hydrogen exchange mass spectrometry: what is it and what can it tell us?

Sean R Marcsisin, John R Engen

Abstract readReview
In one paragraph

Review in Analytical and bioanalytical chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing 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

105 citing papers in PubMed.

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  16. Review
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  20. Article

45 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

2 authors.

Sean R MarcsisinThe Department of Chemistry & Chemical Biology and The Barnett Institute of Chemical & Biological Analysis, Northeastern University, Boston, MA 02115, USA.
John R Engen

Funding

Protein conformational change upon membrane associationR01GM086507 · NIGMS · NORTHEASTERN UNIVERSITY · PI ENGEN, JOHN R · 2009 to 2012
$1.6M
Structural Dynamics of Src-Family Kinase ActivationR01GM070590 · NIGMS · UNIVERSITY OF NEW MEXICO · PI ENGEN, JOHN R · 2004 to 2008
$1.5M
NIGMS NIH HHS GM070590NIGMS NIH HHS R01 GM070590NIGMS NIH HHS R01 GM086507NIGMS NIH HHS R01-GM086507
6 · The paper itself

Abstract

Proteins are undoubtedly some of the most essential molecules of life. While much is known about many proteins, some aspects still remain mysterious. One particularly important aspect of understanding proteins is determining how structure helps dictate function. Continued development and implementation of biophysical techniques that provide information about protein conformation and dynamics is essential. In this review, we discuss hydrogen exchange mass spectrometry and how this method can be used to learn about protein conformation and dynamics. The basic concepts of the method are described, the workflow illustrated, and a few examples of its application are provided.

Indexed as

AnimalsHumansHydrogenMass SpectrometryProtein ConformationProteinsHydrogenProteins

Identifiers

PMID20195578
PMCPMC2868954

What OpenQuestion holds

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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.