Evidence map›Paper›PMID 35518197›Full record

ArticleBiochemistry and biophysics reports2022

The first laminin G-like domain of protein S is essential for binding and activation of Tyro3 receptor and intracellular signalling.

Nour Al Kafri, Josefin Ahnström, Adrienn Teraz-Orosz, Ludovic Chaput, Natesh Singh, Bruno O Villoutreix, Sassan Hafizi

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

Article in Biochemistry and biophysics reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.4field-weighted citation impact, top 43% 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

6 citing papers in PubMed, 5 citations in OpenAlex.

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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

7 authors at 3 institutions in 2 countries.

Nour Al KafriSchool of Pharmacy and Biomedical Sciences, University of Portsmouth, Portsmouth, UK.
Josefin AhnströmFaculty of Medicine, Dept. of Immunology and Inflammation, Imperial College London, UK.
Adrienn Teraz-OroszFaculty of Medicine, Dept. of Immunology and Inflammation, Imperial College London, UK.
Ludovic ChaputUniversity of Lille, Inserm, Institut Pasteur de Lille, U1177 - Drugs and Molecules for Living Systems, F-59000, Lille, France.
Natesh SinghUniversity of Lille, Inserm, Institut Pasteur de Lille, U1177 - Drugs and Molecules for Living Systems, F-59000, Lille, France.
Bruno O VilloutreixUniversity of Lille, Inserm, Institut Pasteur de Lille, U1177 - Drugs and Molecules for Living Systems, F-59000, Lille, France.
Sassan HafiziSchool of Pharmacy and Biomedical Sciences, University of Portsmouth, Portsmouth, UK.
Inserm · FRImperial College London · GBUniversity of Portsmouth · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The homologous proteins Gas6 and protein S (ProS1) are both natural ligands for the TAM (Tyro3, Axl, MerTK) receptor tyrosine kinases. ProS1 selectively activates Tyro3; however, the precise molecular interface of the ProS1-Tyro3 contact has not been characterised. We used a set of chimeric proteins in which each of the

Indexed as

Gas6Homology modellingLaminin G domainLigand-receptor bindingMolecular dockingProtein-protein interactionProtein SProtein structureReceptor tyrosine kinaseSignal transductionTyro3

Identifiers

PMID35518197
PMCPMC9065593
OpenAlexW4225090994

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.