Evidence map›Paper›PMID 23076210›Full record

ReviewCell adhesion & migration

Laminin α5 guides tissue patterning and organogenesis.

Caroline Spenlé, Patricia Simon-Assmann, Gertraud Orend, Jeffrey H Miner

Open access · goldAbstract readReview
In one paragraph

Review in Cell adhesion & migration. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

30 citing papers in PubMed, 74 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

4 authors at 2 institutions in 2 countries.

Caroline SpenléInserm U682, Université de Strasbourg, Strasbourg, France. caroline.spenle@inserm.fr
Patricia Simon-Assmann
Gertraud Orend
Jeffrey H Miner
Inserm · FRWashington University in St. Louis · US

Funding

LAMININS AND GLOMERULAR FILTRATIONR01DK078314 · NIDDK · WASHINGTON UNIVERSITY · PI MINER, JEFFREY H · 2008 to 2021
$5.4M
ASSEMBLY AND FUNCTION OF BASEMENT MEMBRANE PROTEINSR01GM060432 · NIGMS · WASHINGTON UNIVERSITY · PI MINER, JEFFREY H · 2000 to 2008
$1.8M
NIDDK NIH HHS R01 DK078314NIDDK NIH HHS R01DK078314NIGMS NIH HHS R01 GM060432NIGMS NIH HHS R01GM060432
6 · The paper itself

Abstract

Laminins (LM) are extracellular matrix molecules that contribute to and are required for the formation of basement membranes. They participate in the modulation of epithelial/mesenchymal interactions and are implicated in organogenesis and maintenance of organ homeostasis. Among the LM molecules, the LM α5 chain (LMα5) is one of the most widely distributed LM in the developing and mature organism. Its presence in some basement membranes during embryogenesis is absolutely required for maintenance of basement membrane integrity and thus for proper organogenesis. LMα5 also regulates the expression of genes important for major biological processes, in part by repressing or activating signaling pathways, depending upon the physiological context.

Indexed as

Body PatterningGene Expression Regulation, DevelopmentalOrganogenesisAnimalsBasement MembraneBinding SitesCell DifferentiationCell MovementExtracellular MatrixLamininMiceProtein BindingStem CellsSyndecan-4Wnt Signaling PathwayLamininlaminin alpha5Sdc4 protein, mouseSyndecan-4

Identifiers

PMID23076210
PMCPMC3544791
OpenAlexW2149107731

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.