Evidence map›Paper›PMID 28235806›Full record

ArticleThe Journal of biological chemistry2017

Molecular basis of interactions between SH3 domain-containing proteins and the proline-rich region of the ubiquitin ligase Itch.

Guillaume Desrochers, Laurent Cappadocia, Mathieu Lussier-Price, Anh-Tien Ton, Riham Ayoubi, Adrian Serohijos, James G Omichinski, Annie Angers

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

8 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. PACSIN proteins in vivo: Roles in development and physiology.Acta physiologica (Oxford, England) · 2022
    Review
  4. Article
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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

8 authors at 2 institutions in 2 countries.

Guillaume DesrochersFrom the Departments of Biological Sciences and.
Laurent CappadociaBiochemistry and Molecular Medicine, University of Montreal, Montreal, Quebec H3C 3J7, Canada.
Mathieu Lussier-PriceBiochemistry and Molecular Medicine, University of Montreal, Montreal, Quebec H3C 3J7, Canada.
Anh-Tien TonBiochemistry and Molecular Medicine, University of Montreal, Montreal, Quebec H3C 3J7, Canada.
Riham AyoubiFrom the Departments of Biological Sciences and.
Adrian SerohijosBiochemistry and Molecular Medicine, University of Montreal, Montreal, Quebec H3C 3J7, Canada.
James G OmichinskiBiochemistry and Molecular Medicine, University of Montreal, Montreal, Quebec H3C 3J7, Canada.
Annie AngersFrom the Departments of Biological Sciences and annie.angers@umontreal.ca.ORCID 0000-0003-0131-256X
Université de Montréal · CAUniversité d'Angers · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ligase Itch plays major roles in signaling pathways by inducing ubiquitylation-dependent degradation of several substrates. Substrate recognition and binding are critical for the regulation of this reaction. Like closely related ligases, Itch can interact with proteins containing a PP

Indexed as

Models, Molecularsrc Homology DomainsHEK293 CellsHumansProtein BindingRepressor ProteinsUbiquitin-Protein LigasesITCH protein, humanRepressor ProteinsUbiquitin-Protein Ligasesamphiphysincrystal structureendophilinisothermal titration calorimetry (ITC)Itchmolecular modelingpacsinproline-rich region (PRR)protein-protein interactionSrc homology 3 domain (SH3 domain)

Identifiers

PMID28235806
PMCPMC5391761
OpenAlexW2590519233

What OpenQuestion holds

Textmetadata
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.