Evidence map›Paper›PMID 26048552›Full record

ReviewAnnual review of analytical chemistry (Palo Alto, Calif.)2015

Analytical Aspects of Hydrogen Exchange Mass Spectrometry.

John R Engen, Thomas E Wales

Abstract readReview
In one paragraph

Review in Annual review of analytical chemistry (Palo Alto, Calif.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing 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

76 citing papers in PubMed.

  1. Article
  2. Modulating pseudokinase conformation from the ATP-binding site.Structure (London, England : 1993) · 2026
    Article
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  16. Review
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  19. Review
  20. Article

16 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.

John R EngenDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts 02115; email: j.engen@neu.edu.
Thomas E Wales

Funding

Extending the applications of hydrogen exchange mass spectrometryR01GM101135 · NIGMS · NORTHEASTERN UNIVERSITY · PI ENGEN, JOHN R · 2012 to 2015
$1.2M
NIGMS NIH HHS R01 GM101135NIGMS NIH HHS R01-GM101135
6 · The paper itself

Abstract

This article reviews the analytical aspects of measuring hydrogen exchange by mass spectrometry (HX MS). We describe the nature of analytical selectivity in hydrogen exchange, then review the analytical tools required to accomplish fragmentation, separation, and the mass spectrometry measurements under restrictive exchange quench conditions. In contrast to analytical quantitation that relies on measurements of peak intensity or area, quantitation in HX MS depends on measuring a mass change with respect to an undeuterated or deuterated control, resulting in a value between zero and the maximum amount of deuterium that can be incorporated. Reliable quantitation is a function of experimental fidelity and to achieve high measurement reproducibility, a large number of experimental variables must be controlled during sample preparation and analysis. The method also reports on important qualitative aspects of the sample, including conformational heterogeneity and population dynamics.

Indexed as

Deuterium Exchange MeasurementHydrogenMass SpectrometryThermodynamicsHydrogenbiopharmaceuticaldeuteriumfragment separation methodprotein conformationprotein dynamics

Identifiers

PMID26048552
PMCPMC4989240

What OpenQuestion holds

Textmetadata
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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.