Evidence map›Paper›PMID 39698111›Full record

ArticleFrontiers in molecular biosciences2024

The conformation of the nSrc specificity-determining loop in the Src SH3 domain is modulated by a WX conserved sequence motif found in SH3 domains.

Frederick Longshore-Neate, Caroline Ceravolo, Cole Masuga, Elise F Tahti, Jadon M Blount, Sarah N Smith, Jeanine F Amacher

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in molecular biosciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

7 authors.

Frederick Longshore-Neate *Department of Chemistry, Western Washington University, Bellingham, WA, United States.
Caroline Ceravolo *Department of Chemistry, Western Washington University, Bellingham, WA, United States.
Cole MasugaDepartment of Chemistry, Western Washington University, Bellingham, WA, United States.
Elise F TahtiDepartment of Chemistry, Western Washington University, Bellingham, WA, United States.
Jadon M BlountDepartment of Chemistry, Western Washington University, Bellingham, WA, United States.
Sarah N SmithDepartment of Chemistry, Western Washington University, Bellingham, WA, United States.
Jeanine F AmacherDepartment of Chemistry, Western Washington University, Bellingham, WA, United States.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular signaling networks are modulated by multiple protein-protein interaction domains that coordinate extracellular inputs and processes to regulate cellular processes. Several of these domains recognize short linear motifs, or SLiMs, which are often highly conserved and are closely regulated. One such domain, the Src homology 3 (SH3) domain, typically recognizes proline-rich SLiMs and is one of the most abundant SLiM-binding domains in the human proteome. These domains are often described as quite

Indexed as

protein-peptide interactionsprotein-protein interactionsSH3 domainsshort linear motifssignal transductionspecificity

Identifiers

PMID39698111
PMCPMC11653366

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.