Evidence map›Paper›PMID 27590440›Full record

ReviewGene2016

Signaling via PINCH: Functions, binding partners and implications in human diseases.

Huamin Xu, Huiling Cao, Guozhi Xiao

Open access · greenAbstract readReview
In one paragraph

Review in Gene, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
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  16. Fluid shear stress modulates endothelial inflammation by targeting LIMS2.Experimental biology and medicine (Maywood, N.J.) · 2020
    Article
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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

3 authors at 1 institution in 2 countries.

Huamin XuDepartment of Physiology and Pathophysiology, Peking University Health Science Center, Beijing 100191, China; Department of Biology and Shenzhen Key Laboratory of Cell Microenvironment, Southern University of Science and Technology, Shenzhen 518055, China.
Huiling CaoDepartment of Biology and Shenzhen Key Laboratory of Cell Microenvironment, Southern University of Science and Technology, Shenzhen 518055, China.
Guozhi XiaoDepartment of Biology and Shenzhen Key Laboratory of Cell Microenvironment, Southern University of Science and Technology, Shenzhen 518055, China; Department of Biochemistry, Rush University Medical Center, Chicago, IL 60612, United States. Electronic address: xiaogz@sustc.edu.cn.
Southern University of Science and Technology · CN

Funding

Signaling Mechanisms of Focal Adhesion Protein Kindlin-2 in ChondrogenesisR01AR068950 · NIAMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HUANG, JIAN, WU, CHUANYUE · 2015 to 2019
$2.2M
Role of ATF-4 in the Anabolic Actions of PTH on BoneR01DK072230 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI XIAO, GUOZHI · 2007 to 2011
$1.4M
ATF4 and OsteoclastogenesisR01AR059647 · NIAMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI XIAO, GUOZHI · 2010 to 2013
$991k
A novel kindlin-2 regulatory pathway in bone remodelingR21AR064874 · NIAMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI WU, CHUANYUE, XIAO, GUOZHI · 2015 to 2016
$383k
NIAMS NIH HHS R01 AR059647NIAMS NIH HHS R01 AR068950NIAMS NIH HHS R21 AR064874NIDDK NIH HHS R01 DK072230
6 · The paper itself

Abstract

Particularly interesting new cysteine-histidine-rich protein (PINCH) is a LIM-domain-only adaptor that plays important roles in cytoskeletal organization and extracellular matrix adhesion, migration, proliferation and survival. Mammalian cells have two functional PINCH proteins, PINCH1 and PINCH2. PINCH not only binds to Nck2 and engages in the signaling of growth factor receptors, but also forms a ternary complex with ILK and parvin (IPP complex). Normally, the IPP complex locates to focal adhesions participating in the signaling of integrins and mediating the interaction of cytoskeleton and extracellular matrix (ECM). Accumulative evidence indicates that abnormalities in PINCH signaling are involved in the pathogenesis of important diseases, such as cancers, renal diseases, cardiomyopathy, and HIV. Therefore, clarifying the functions of PINCH and its interactions with key factors is important for better understanding of signaling events both in health and disease.

Indexed as

Signal TransductionAdaptor Proteins, Signal TransducingAnimalsCardiomegalyExtracellular MatrixFocal AdhesionsHIV InfectionsHumansKidney DiseasesLIM Domain ProteinsMembrane ProteinsMultiprotein ComplexesNeoplasm ProteinsNeoplasmsOncogene ProteinsAdaptor Proteins, Signal TransducingLIM Domain ProteinsLIMS1 protein, humanLIMS2 protein, humanMembrane ProteinsMultiprotein ComplexesNCK2 protein, humanNeoplasm ProteinsOncogene ProteinsAdhesionFocal adhesionILKIPP complexNck2PINCHProtein-protein interactionTumor

Identifiers

PMID27590440
PMCPMC5056850
OpenAlexW2517685755

What OpenQuestion holds

Textmetadata
LicenceTDM
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.