Evidence map›Paper›PMID 27975228›Full record

ReviewAdvances in experimental medicine and biology2016

Protein Structural Analysis via Mass Spectrometry-Based Proteomics.

Antonio Artigues, Owen W Nadeau, Mary Ashley Rimmer, Maria T Villar, Xiuxia Du, Aron W Fenton, Gerald M Carlson

Abstract readReview
In one paragraph

Review in Advances in experimental medicine and biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

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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

7 authors.

Antonio ArtiguesDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS, USA. aartigues@kumc.edu.
Owen W NadeauDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS, USA.
Mary Ashley RimmerDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS, USA.
Maria T VillarDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS, USA.
Xiuxia DuDepartment of Bioinformatics and Genomics, University of North Carolina at Charlotte, Charlotte, NC, USA.
Aron W FentonDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS, USA.
Gerald M CarlsonDepartment of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS, USA.

Funding

Dissecting Allostery in Pyruvate KinaseR01GM115340 · NIGMS · UNIVERSITY OF KANSAS MEDICAL CENTER · PI FENTON, ARON W · 2016 to 2019
$1.4M
NIGMS NIH HHS R01 GM115340
6 · The paper itself

Abstract

Modern mass spectrometry (MS) technologies have provided a versatile platform that can be combined with a large number of techniques to analyze protein structure and dynamics. These techniques include the three detailed in this chapter: (1) hydrogen/deuterium exchange (HDX), (2) limited proteolysis, and (3) chemical crosslinking (CX). HDX relies on the change in mass of a protein upon its dilution into deuterated buffer, which results in varied deuterium content within its backbone amides. Structural information on surface exposed, flexible or disordered linker regions of proteins can be achieved through limited proteolysis, using a variety of proteases and only small extents of digestion. CX refers to the covalent coupling of distinct chemical species and has been used to analyze the structure, function and interactions of proteins by identifying crosslinking sites that are formed by small multi-functional reagents, termed crosslinkers. Each of these MS applications is capable of revealing structural information for proteins when used either with or without other typical high resolution techniques, including NMR and X-ray crystallography.

Indexed as

Databases, ProteinProteomeAlgorithmsAnimalsComputational BiologyCross-Linking ReagentsData MiningDeuterium Exchange MeasurementHigh-Throughput Screening AssaysHumansMass SpectrometryProtein ConformationProteinsProteolysisProteomicsReproducibility of ResultsCross-Linking ReagentsProteinsProteomeChemical Crosslinking (CX)Hydrogen/Deuterium Exchange (HDX)Limited proteolysisProtein structural analysis

Identifiers

PMID27975228
PMCPMC5271599

What OpenQuestion holds

Textmetadata
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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.