Evidence map›Paper›PMID 29630925›Full record

ReviewMethods (San Diego, Calif.)2018

Covalent labeling-mass spectrometry with non-specific reagents for studying protein structure and interactions.

Patanachai Limpikirati, Tianying Liu, Richard W Vachet

Abstract readReview
In one paragraph

Review in Methods (San Diego, Calif.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
6.8field-weighted citation impact, top 2% of its field
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

68 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
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  16. The Use of Dansyl Chloride to Probe Protein Structure and Dynamics.International journal of molecular sciences · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Review

8 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

3 authors at 1 institution in 1 country.

Patanachai LimpikiratiDepartment of Chemistry, University of Massachusetts Amherst, MA 01003, United States.
Tianying LiuDepartment of Chemistry, University of Massachusetts Amherst, MA 01003, United States.
Richard W VachetDepartment of Chemistry, University of Massachusetts Amherst, MA 01003, United States. Electronic address: rwvachet@chem.umass.edu.
University of Massachusetts Amherst · US

Funding

Copper-Induced Amyloidosis Studied by Mass SpectrometryR01GM075092 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI VACHET, RICHARD W · 2005 to 2020
$4.0M
Higher Order Structure Analysis of Protein Therapeutics by Covalent Labeling MSR43GM116211 · NIGMS · RECLAIM PHARMACEUTICAL WASTE MANAGEMENT · PI GRABAN, ERIC · 2016 to 2016
$277k
NIGMS NIH HHS R01 GM075092NIGMS NIH HHS R43 GM116211
6 · The paper itself

Abstract

Using mass spectrometry (MS) to obtain information about a higher order structure of protein requires that a protein's structural properties are encoded into the mass of that protein. Covalent labeling (CL) with reagents that can irreversibly modify solvent accessible amino acid side chains is an effective way to encode structural information into the mass of a protein, as this information can be read-out in a straightforward manner using standard MS-based proteomics techniques. The differential reactivity of proteins under two or more conditions can be used to distinguish protein topologies, conformations, and/or binding sites. CL-MS methods have been effectively used for the structural analysis of proteins and protein complexes, particularly for systems that are difficult to study by other more traditional biochemical techniques. This review provides an overview of the non-specific CL approaches that have been combined with MS with a particular emphasis on the reagents that are commonly used, including hydroxyl radicals, carbenes, and diethylpyrocarbonate. We describe the reagent and protein factors that affect the reactivity of amino acid side chains. We also include details about experimental design and workflow, data analysis, recent applications, and some future prospects of CL-MS methods.

Indexed as

Protein ConformationBinding SitesMass SpectrometryProtein Interaction MappingProteinsProteomicsProteinsCarbenesCovalent labelingDiethylpyrocarbonateHydroxyl radicalsMass spectrometryProtein higher-order structure

Identifiers

PMID29630925
PMCPMC6051898
OpenAlexW2795922219

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.