Evidence map›Paper›PMID 29723415›Full record

ReviewFEBS letters2018

The tale of two talins - two isoforms to fine-tune integrin signalling.

Rosemarie E Gough, Benjamin T Goult

Open access · hybridAbstract readReview
In one paragraph

Review in FEBS letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
8.1field-weighted citation impact, top 2% 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

61 citing papers in PubMed, 102 citations in OpenAlex.

  1. Article
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  8. Integrins in the kidney - beyond the matrix.Nature reviews. Nephrology · 2025
    Review
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  11. Review
  12. Review
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  20. Kindlin stabilizes the talin·integrin bond under mechanical load by generating an ideal bond.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article

1 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Rosemarie E GoughSchool of Biosciences, University of Kent, Canterbury, UK.
Benjamin T GoultSchool of Biosciences, University of Kent, Canterbury, UK.ORCID 0000-0002-3438-2807
University of Kent · GB

Funding

Biotechnology and Biological Sciences Research Council BB/N007336/1
6 · The paper itself

Abstract

Talins are cytoplasmic adapter proteins essential for integrin-mediated cell adhesion to the extracellular matrix. Talins control the activation state of integrins, link integrins to cytoskeletal actin, recruit numerous signalling molecules that mediate integrin signalling and coordinate recruitment of microtubules to adhesion sites via interaction with KANK (kidney ankyrin repeat-containing) proteins. Vertebrates have two talin genes, TLN1 and TLN2. Although talin1 and talin2 share 76% protein sequence identity (88% similarity), they are not functionally redundant, and the differences between the two isoforms are not fully understood. In this Review, we focus on the similarities and differences between the two talins in terms of structure, biochemistry and function, which hint at subtle differences in fine-tuning adhesion signalling.

Indexed as

AnimalsCell MembraneHumansIntegrinsModels, MolecularProtein ConformationProtein IsoformsSequence Homology, Amino AcidSignal TransductionTalinIntegrinsProtein IsoformsTalinintegrinmechanobiologytalin

Identifiers

PMID29723415
PMCPMC6032930
OpenAlexW2802947309

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.