Evidence map›Paper›PMID 39332818›Full record

SynthesisJournal of the American Society for Mass Spectrometry2024

Mass Spectral Feature Analysis of Ubiquitylated Peptides Provides Insights into Probing the Dark Ubiquitylome.

Regina M Edgington, Damien B Wilburn

Abstract readMeta-Analysis
In one paragraph

Synthesis in Journal of the American Society for Mass Spectrometry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Regina M EdgingtonDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, United States.
Damien B WilburnDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, United States.ORCID 0000-0002-1255-9982

Funding

Integration of biophysics and deep learning to understand species-specificity of fertilization and the rapid evolution of protein disorderR35GM150583 · NIGMS · OHIO STATE UNIVERSITY · PI Damien Beau Wilburn · 2023 to 2026
$1.5M
Integrating 'omics', evolution, and biochemistry to understand fertilizationR00HD090201 · NICHD · OHIO STATE UNIVERSITY · PI WILBURN, DAMIEN BEAU · 2022 to 2024
$745k
NICHD NIH HHS R00 HD090201NIGMS NIH HHS R35 GM150583
6 · The paper itself

Abstract

Ubiquitylation is a structurally and functionally diverse post-translational modification that involves the covalent attachment of the small protein ubiquitin to other protein substrates. Trypsin-based proteomics is the most common approach for globally identifying ubiquitylation sites. However, we estimate that such methods are unable to detect ∼40% of ubiquitylation sites in the human proteome,

Indexed as

PeptidesProteomicsUbiquitinationComputational BiologyHumansMass SpectrometryProtein Processing, Post-TranslationalProteomeTandem Mass SpectrometryUbiquitinUbiquitinated ProteinsPeptidesProteomeUbiquitinUbiquitinated Proteins

Identifiers

PMID39332818
PMCPMC11623170

What OpenQuestion holds

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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.