About: Negative regulators of integrin activity

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scientific article published on 20 July 2012

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в липні 2012 (uk) im Juli 2012 veröffentlichter wissenschaftlicher Artikel (de) scientific article published on 20 July 2012 (en) artículu científicu espublizáu en xunetu de 2012 (ast)
publication date	wds:Q60340536-AA6A3587-4718-44D6-8913-C36CF76130ED
publication date	2012-07-20 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q60340536-B28F2A8D-F6C3-49D6-B279-50F73E450945
language of work or name	English
cites work	wds:Q60340536-5FD08F7C-8F1A-47BA-96E5-C387634E702A wds:Q60340536-9B1EEB5F-A195-46C6-AAF0-47675FC9E061 wds:Q60340536-A7551E26-44E9-4FB7-BEEF-2F60E4E655A7
cites work	Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics Site-directed perturbation of protein kinase C- integrin interaction blocks carcinoma cell chemotaxis. SHARPIN is an endogenous inhibitor of β1-integrin activation
author name string	wds:Q60340536-03CF1F6F-2A4D-4DE0-B89B-F5DCE069D514
author name string	Jonna Nevo
rdfs:label	Negative regulators of integrin activity (en) Negative regulators of integrin activity (nl)
skos:prefLabel	Negative regulators of integrin activity (en) Negative regulators of integrin activity (nl)
name	Negative regulators of integrin activity (en) Negative regulators of integrin activity (nl)
author	wds:Q60340536-2A5DFD75-04F6-49CF-9761-DC6853ADF03B wds:Q60340536-591618B8-3FFF-4615-9BAB-793791722C04 wds:Q60340536-6D131230-F76D-4F23-A02F-0A61D8A584D8 wds:Q60340536-D7701F0D-9F29-40E2-9AF9-129E7D644F2A
author	Johanna Ivaska Jari Ylänne Jeroen Pouwels Teijo Pellinen
title	wds:Q60340536-4089474E-C6F6-4902-84C4-BD146773F040
title	Negative regulators of integrin activity (en)
page(s)	wds:Q60340536-C3E8C7EF-59E3-4FE5-BC7A-AD3C7B09D92D
page(s)	3271-3280
instance of	wds:Q60340536-0457A314-41F0-482E-A4B6-EFE4765CBF7F
instance of	scholarly article
PubMed ID	wds:Q60340536-6066EA28-5898-4E31-9CB3-3EE8DD3140E7
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/22822081
PubMed ID	22822081
published in	wds:Q60340536-4A48A01B-7096-4DC8-8EAF-8C50131FDAF4
published in	Journal of Cell Science
issue	wds:Q60340536-92360AD6-A460-438C-8D93-8235FBA9DEAB
volume	wds:Q60340536-005CDE33-10D6-4EE0-8D5A-DFD072910D75
issue	Pt 14
volume	125
DOI	wds:Q60340536-630D5B50-C20B-4546-850B-0D98E86653EF
DOI	http://dx.doi.org/10.1242/JCS.093641
DOI	10.1242/JCS.093641
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q60340536
is cites work of	Leukocyte arrest: Biomechanics and molecular mechanisms of β2 integrin activation Integrin α5β1, the Fibronectin Receptor, as a Pertinent Therapeutic Target in Solid Tumors. Talins and kindlins: partners in integrin-mediated adhesion. Epithelial polarity--generating and integrating signals from the ECM with integrins Endothelial exocytosis of angiopoietin-2 resulting from CCM3 deficiency contributes to cerebral cavernous malformation SHARPIN controls the development of regulatory T cells Talin and kindlin: the one-two punch in integrin activation Integrin cytoplasmic tail interactions Integrin inactivators: balancing cellular functions in vitro and in vivo Insulin-like growth factor binding protein-3 inhibits cell adhesion via suppression of integrin β4 expression Mechanotransduction of matrix stiffness in regulation of focal adhesion size and number: reciprocal regulation of caveolin-1 and β1 integrin. The dual structural roles of the membrane distal region of the α-integrin cytoplasmic tail during integrin inside-out activation Phosphorylation of the α-chain in the integrin LFA-1 enables β2-chain phosphorylation and α-actinin binding required for cell adhesion Integrin-beta3 clusters recruit clathrin-mediated endocytic machinery in the absence of traction force Modeling the Kinetics of Integrin Receptor Binding to Hepatic Extracellular Matrix Proteins A novel gammaretroviral shuttle vector insertional mutagenesis screen identifies SHARPIN as a breast cancer metastasis gene and prognostic biomarker Proteomic Dissection of Nanotopography-Sensitive Mechanotransductive Signaling Hubs that Foster Neuronal Differentiation in PC12 Cells. Functional Effect of the Mutations Similar to the Cleavage during Platelet Activation at Integrin β3 Cytoplasmic Tail when Expressed in Mouse Platelets The bioenergetics of integrin-based adhesion, from single molecule dynamics to stability of macromolecular complexes
is cites work of	wds:Q27320491-ADF28CB6-D1D9-4DE4-A00C-4D5CCED87138 wds:Q42008500-F093A172-BAF6-4F6A-8015-D834A5A84443 wds:Q58199122-4EA79280-2091-4D0C-9750-6D02BCAE3145 wds:Q36545417-8C836C4E-21E7-40A6-9A7C-ADC779FD5EF5 wds:Q38110421-1F0475B3-8289-4EE0-B3F8-C96D6CFE377B wds:Q36194061-6F0B05DF-CEBE-423D-8E1A-911CF0DBD969 wds:Q36020955-A1F42DEA-18C6-4389-88D9-00469768E9F6 wds:Q40771683-A9B4A764-7F62-46FE-BB94-75C6B63C03D0 wds:Q90013704-D9175A82-A60B-469A-BA49-A76E3F35FBE6 wds:Q33978054-2DD6CE2B-3918-4B2D-BA8F-5FF4D657FF92 wds:Q46863609-3350A535-E963-4CFC-8841-3C83C3409E34 wds:Q26825041-8E171AC1-1560-462B-BB71-E926EC49B988 wds:Q26823123-4C2F1636-465B-4D31-A505-2469019AFC74 wds:Q37239068-AC8490B8-7383-4F45-8EC6-D90AB99D4813 wds:Q38161726-FA9F0205-B978-4037-B498-39F320842D69 wds:Q36908674-2D5789FB-EBBA-4D79-904D-42265C271971 wds:Q38183284-843DE948-119C-4141-92DA-4127EDFC634E wds:Q41271593-673F6798-8BEE-489A-9DE0-06756E18370F wds:Q49178074-CE808B25-C164-4F54-9728-2A440F39E3E5

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