Evidence map›Paper›PMID 28369144›Full record

ArticlePloS one2017

ANKRD54 preferentially selects Bruton's Tyrosine Kinase (BTK) from a Human Src-Homology 3 (SH3) domain library.

Manuela O Gustafsson, Dara K Mohammad, Erkko Ylösmäki, Hyunseok Choi, Subhash Shrestha, Qing Wang, Beston F Nore, Kalle Saksela, C I Edvard Smith

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 48% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Review
  3. Generating FN3-Based Affinity Reagents Through Phage Display.Current protocols in chemical biology · 2018
    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

9 authors at 2 institutions in 3 countries.

Manuela O GustafssonDepartment of Laboratory Medicine, Clinical Research Center, Karolinska Institutet, Karolinska University Hospital Huddinge, SE Stockholm, Sweden.ORCID http://orcid.org/0000-0002-0268-9476
Dara K MohammadDepartment of Laboratory Medicine, Clinical Research Center, Karolinska Institutet, Karolinska University Hospital Huddinge, SE Stockholm, Sweden.
Erkko YlösmäkiDepartment of Virology, University of Helsinki and Helsinki University Hospital, Helsinki, Finland.
Hyunseok ChoiDepartment of Virology, University of Helsinki and Helsinki University Hospital, Helsinki, Finland.
Subhash ShresthaDepartment of Virology, University of Helsinki and Helsinki University Hospital, Helsinki, Finland.
Qing WangDepartment of Laboratory Medicine, Clinical Research Center, Karolinska Institutet, Karolinska University Hospital Huddinge, SE Stockholm, Sweden.
Beston F NoreDepartment of Laboratory Medicine, Clinical Research Center, Karolinska Institutet, Karolinska University Hospital Huddinge, SE Stockholm, Sweden.
Kalle SakselaDepartment of Virology, University of Helsinki and Helsinki University Hospital, Helsinki, Finland.
C I Edvard SmithDepartment of Laboratory Medicine, Clinical Research Center, Karolinska Institutet, Karolinska University Hospital Huddinge, SE Stockholm, Sweden.
Karolinska University Hospital · SEUniversity of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bruton's Tyrosine Kinase (BTK) is a cytoplasmic protein tyrosine kinase with a fundamental role in B-lymphocyte development and activation. The nucleocytoplasmic shuttling of BTK is specifically modulated by the Ankyrin Repeat Domain 54 (ANKRD54) protein and the interaction is known to be exclusively SH3-dependent. To identify the spectrum of the ANKRD54 SH3-interactome, we applied phage-display screening of a library containing all the 296 human SH3 domains. The BTK-SH3 domain was the prime interactor. Quantitative western blotting analysis demonstrated the accuracy of the screening procedure. Revealing the spectrum and specificity of ANKRD54-interactome is a critical step toward functional analysis in cells and tissues.

Indexed as

Agammaglobulinaemia Tyrosine KinaseAnimalsB-LymphocytesCell Line, TumorChlorocebus aethiopsCOS CellsHEK293 CellsHumansMutationNuclear ProteinsPeptide LibraryProtein BindingProtein-Tyrosine KinasesSignal Transductionsrc Homology DomainsAgammaglobulinaemia Tyrosine KinaseANKRD54 protein, humanBTK protein, humanNuclear ProteinsPeptide LibraryProtein-Tyrosine Kinases

Identifiers

PMID28369144
PMCPMC5378395
OpenAlexW2605124976

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.