Evidence map›Paper›PMID 33754701›Full record

ArticleJournal of the American Society for Mass Spectrometry2021

Mesh Fragmentation Improves Dissociation Efficiency in Top-down Proteomics.

Lei Lu, Mark Scalf, Michael R Shortreed, Lloyd M Smith

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Top-down proteomics.Nature reviews. Methods primers · 2024
    Article
  5. 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

4 authors.

Lei LuDepartment of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, United States.ORCID http://orcid.org/0000-0001-7097-1505
Mark ScalfDepartment of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, United States.
Michael R ShortreedDepartment of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, United States.ORCID http://orcid.org/0000-0003-4626-0863
Lloyd M SmithDepartment of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, United States.

Funding

Revealing Proteoforms: The Primary Effectors of Biological FunctionR35GM126914 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Lloyd M Smith · 2018 to 2026
$6.2M
NIGMS NIH HHS R35 GM126914
6 · The paper itself

Abstract

Top-down proteomics is a key mass spectrometry-based technology for comprehensive analysis of proteoforms. Proteoforms exhibit multiple high charge states and isotopic forms in full MS scans. The dissociation behavior of proteoforms in different charge states and subjected to different collision energies is highly variable. The current widely employed data-dependent acquisition (DDA) method selects a narrow

Indexed as

SoftwareMass SpectrometryProteinsProteomicsSaccharomyces cerevisiae ProteinsProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID33754701
PMCPMC8783543

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.