Evidence map›Paper›PMID 32275420›Full record

ArticleJournal of the American Society for Mass Spectrometry2020

Top-Down Analysis of In-Source HDX of Native Protein Ions.

Nawaporn Sanguantrakun, Chamnongsak Chanthamontri, Michael L Gross

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

6 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Recent technological developments for native mass spectrometry.Biochimica et biophysica acta. Proteins and proteomics · 2022
    Review
  6. Review
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 2 institutions in 1 country.

Nawaporn SanguantrakunDepartment of Basic Sciences, St. Louis College of Pharmacy, St. Louis, Missouri 63110, United States.ORCID http://orcid.org/0000-0002-8874-2337
Chamnongsak ChanthamontriDepartment of Chemistry, Washington University, St. Louis, Missouri 63130, United States.
Michael L GrossDepartment of Chemistry, Washington University, St. Louis, Missouri 63130, United States.ORCID http://orcid.org/0000-0003-1159-4636
Washington University in St. Louis · USUniversity of Health Sciences and Pharmacy · US

Funding

TrainingP41GM103422 · NIGMS · WASHINGTON UNIVERSITY · PI YARASHESKI, KEVIN E · 2012 to 2019
$12.0M
A Biomedical Mass Spectrometry Resource: Ongoing Driving Biomedical ProjectsR24GM136766 · NIGMS · WASHINGTON UNIVERSITY · PI GROSS, MICHAEL L · 2020 to 2022
$2.3M
NIGMS NIH HHS P41 GM103422NIGMS NIH HHS R24 GM136766
6 · The paper itself

Abstract

Hydrogen/deuterium exchange (HDX) is used in protein biophysics to probe folding dynamics, intermolecular interactions, epitope and other mapping. A typical procedure often involves HDX in buffered D

Indexed as

DeuteriumDeuterium Exchange MeasurementHydrogenMyoglobinPepsin AProtein DenaturationProteinsSolutionsSpectrometry, Mass, Electrospray IonizationUbiquitinDeuteriumHydrogenMyoglobinPepsin AProteinsSolutionsUbiquitin

Identifiers

PMID32275420
PMCPMC7489294
OpenAlexW3015935884

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.