Evidence map›Paper›PMID 29088312›Full record

ArticleBioinformatics (Oxford, England)2018

TMEM132: an ancient architecture of cohesin and immunoglobulin domains define a new family of neural adhesion molecules.

Luis Sanchez-Pulido, Chris P Ponting

Abstract read
In one paragraph

Article in Bioinformatics (Oxford, England), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed.

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  8. SMARCA4 Loss and Mutated β-Catenin Induce Proliferative Lesions in the Murine Embryonic Cerebellum.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
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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

2 authors.

Luis Sanchez-PulidoMedical Research Council Human Genetics Unit, IGMM, University of Edinburgh, Edinburgh EH4 2XU, UK.
Chris P PontingMedical Research Council Human Genetics Unit, IGMM, University of Edinburgh, Edinburgh EH4 2XU, UK.

Funding

Medical Research Council MC_PC_15075Medical Research Council MC_UU_00007/15Medical Research Council MC_UU_12008/1
6 · The paper itself

Abstract

Summary: The molecular functions of TMEM132 genes remain poorly understood and under-investigated despite their mutations associated with non-syndromic hearing loss, panic disorder and cancer. Here we show the full domain architecture of human TMEM132 family proteins solved using in-depth sequence and structural analysis. We reveal them to be five previously unappreciated cell adhesion molecules whose domain architecture has an early holozoan origin prior to the emergence of choanoflagellates and metazoa. The extra-cellular portions of TMEM132 proteins contain five conserved domains including three tandem immunoglobulin domains, and a cohesin domain homologue, the first such domain found in animals. These findings strongly predict a cellular adhesion function for TMEM132 family, connecting the extracellular medium with the intracellular actin cytoskeleton. Contact: luis.sanchez-pulido@igmm.ed.ac.uk. Supplementary information: Supplementary data are available at Bioinformatics online.

Indexed as

Multigene FamilyAmino Acid SequenceAnimalsCell Adhesion MoleculesCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsHumansImmunoglobulin DomainsMembrane ProteinsProtein DomainsSequence Analysis, ProteinCell Adhesion MoleculesCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsMembrane ProteinsTMEM132A protein, humanTMEM132B protein, humanTMEM132C protein, humanTMEM132D protein, humanTMEM132E protein, human

Identifiers

PMID29088312
PMCPMC6030884

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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.