Evidence map›Paper›PMID 20811987›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2010

Analysis of MAP kinases by hydrogen exchange mass spectrometry.

Kevin M Sours, Natalie G Ahn

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. 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.

Kevin M SoursDepartment of Chemistry and Biochemistry, University of Colorado, Boulder, CO, USA.
Natalie G Ahn

Funding

Regulation of Map Kinase by Protein MotionsR01GM074134 · NIGMS · UNIVERSITY OF COLORADO · PI AHN, NATALIE G. · 2007 to 2010
$993k
NIGMS NIH HHS R01 GM074134
6 · The paper itself

Abstract

Hydrogen exchange mass spectrometry (HX-MS) is an experimental technique that can be used to -examine solvent accessibility and conformational mobility in biological macromolecules. This chapter summarizes studies using HX-MS to examine the regulation of conformation, protein mobility, and ligand binding to MAP kinases. We describe the planning and design of HX-MS experiments, strategies for data analysis and interpretation, and available software.

Indexed as

ArtifactsDeuterium Exchange MeasurementEnzyme ActivationEnzyme AssaysMass SpectrometryMitogen-Activated Protein Kinase 1Mitogen-Activated Protein KinasesSoftwareMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinases

Identifiers

PMID20811987
PMCPMC3252998

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.