Evidence map›Paper›PMID 28879238›Full record

ArticleScience advances2017

Mechanistic basis for the recognition of laminin-511 by α6β1 integrin.

Mamoru Takizawa, Takao Arimori, Yukimasa Taniguchi, Yu Kitago, Erika Yamashita, Junichi Takagi, Kiyotoshi Sekiguchi

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

36 citing papers in PubMed, 60 citations in OpenAlex.

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  15. Leucine-Rich Repeat in Polycystin-1 Suppresses Cystogenesis in a Zebrafish (International journal of molecular sciences · 2024
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  18. Peptide location fingerprinting identifies structural alterations within basement membrane components in ageing kidney.Matrix biology : journal of the International Society for Matrix Biology · 2023
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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 1 institution in 1 country.

Mamoru TakizawaDivision of Matrixome Research and Application, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.ORCID 0000-0001-9041-2786
Takao ArimoriLaboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.ORCID 0000-0002-6063-5572
Yukimasa TaniguchiDivision of Matrixome Research and Application, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.ORCID 0000-0003-4433-3432
Yu KitagoLaboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.ORCID 0000-0003-2325-6917
Erika YamashitaDivision of Matrixome Research and Application, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.ORCID 0000-0002-3973-9529
Junichi TakagiLaboratory of Protein Synthesis and Expression, Institute for Protein Research, Osaka University, Suita, Osaka 565-0871, Japan.ORCID 0000-0002-1219-475X
Kiyotoshi SekiguchiDivision of Matrixome Research and Application, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.ORCID 0000-0002-6433-1410
Protein Research Foundation · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Laminins regulate diverse cellular functions through interaction with integrins. Two regions of laminins-three laminin globular domains of the α chain (LG1-3) and the carboxyl-terminal tail of the γ chain (γ-tail)-are required for integrin binding, but it remains unclear how the γ-tail contributes to the binding. We determined the crystal structure of the integrin binding fragment of laminin-511, showing that the γ-tail extends to the bottom face of LG1-3. Electron microscopic imaging combined with biochemical analyses showed that integrin binds to the bottom face of LG1-3 with the γ1-tail apposed to the metal ion-dependent adhesion site (MIDAS) of integrin β1. These findings are consistent with a model in which the γ-tail coordinates the metal ion in the MIDAS through its Glu residue.

Indexed as

Binding SitesIntegrin alpha6beta1IonsLamininMetalsModels, MolecularProtein BindingProtein ConformationProtein MultimerizationRecombinant ProteinsStructure-Activity RelationshipIntegrin alpha6beta1IonsLamininlaminin-511, humanMetalsRecombinant Proteins

Identifiers

PMID28879238
PMCPMC5580876
OpenAlexW2751537783

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.