Protein kinase C regulates the recruitment of syndecan-4 into focal contacts - Wikidata - wikimedia - TriplyDB

Protein kinase C regulates the recruitment of syndecan-4 into focal contacts

Protein kinase C regulates the recruitment of syndecan-4 into focal contacts

http://www.wikidata.org/entity/Q34452929

about

Characterization of syntenin, a syndecan-binding PDZ protein, as a component of cell adhesion sites and microfilaments Direct binding of syndecan-4 cytoplasmic domain to the catalytic domain of protein kinase C alpha (PKC alpha) increases focal adhesion localization of PKC alpha Syndecans: multifunctional cell-surface co-receptors Cytoplasmic interactions of syndecan-4 orchestrate adhesion receptor and growth factor receptor signalling Heparan sulfate proteoglycans of the cardiovascular system. Specific structures emerge but how is synthesis regulated?The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreading Delayed wound repair and impaired angiogenesis in mice lacking syndecan-4 Syndecans in tumor cell adhesion and signaling Localization of the transmembrane proteoglycan syndecan-4 and its regulatory kinases in costameres of rat cardiomyocytes: a deconvolution microscopic study A role of chondroitin sulfate glycosaminoglycan binding site in alpha4beta1 integrin-mediated melanoma cell adhesion Transmembrane domain-induced oligomerization is crucial for the functions of syndecan-2 and syndecan-4 Multimerization of the cytoplasmic domain of syndecan-4 is required for its ability to activate protein kinase C Inhibition of PDGF-B induction and cell growth by syndecan-1 involves the ubiquitin and SUMO-1 ligase, Topors Protein kinase C binding partners.Integrin modulation by lateral association.Syndecans and the lymphoid system.Syndesmos, a syndecan-4 cytoplasmic domain interactor, binds to the focal adhesion adaptor proteins paxillin and Hic-5.Regulation of syndecan-4 phosphorylation in vivo.Heparan sulfate proteoglycans and human breast cancer epithelial cell tumorigenicity.Syndecan-4 signals cooperatively with integrins in a Rho-dependent manner in the assembly of focal adhesions and actin stress fibers Syndecan-1 and syndecan-4 are independent indicators in breast carcinoma Acquisition of anoikis resistance up-regulates syndecan-4 expression in endothelial cells.Breast and ovarian cancers: a survey and possible roles for the cell surface heparan sulfate proteoglycans.Integrin-specific signaling pathways controlling focal adhesion formation and cell migration.Fibroblast growth factor-specific modulation of cellular response by syndecan-4 Mechanoregulation of gene expression in fibroblasts.The extracellular matrix and blood vessel formation: not just a scaffold.Fibronectin regulates assembly of actin filaments and focal contacts in cultured cells via the heparin-binding site in repeat III13.Heparan sulfate proteoglycans are receptors for the cell-surface trafficking and biological activity of transglutaminase-2.Proteoglycan signaling co-receptors: roles in cell adhesion, migration and invasion.A single point mutation in the V3 region affects protein kinase Calpha targeting and accumulation at cell-cell contacts De-sulfation of MG-63 cell glycosaminoglycans delays in vitro osteogenesis, up-regulates cholesterol synthesis and disrupts cell cycle and the actin cytoskeleton.Src-/- fibroblasts are defective in their ability to disassemble focal adhesions in response to phorbol ester/hyaluronan treatment.A new phosphatidylinositol 4,5-bisphosphate-binding site located in the C2 domain of protein kinase Calpha.Soluble heparin-binding peptides regulate chemokinesis and cell adhesive forces.Human corneal epithelial cell adhesion to laminins.Identification of an adhesion site within the syndecan-4 extracellular protein domain.Cysteine-rich domain of human ADAM 12 (meltrin alpha) supports tumor cell adhesion In vivo regulation of syndecan-3 expression in the rat uterus by 17 beta-estradiol.Association of heparan sulfate proteoglycans SDC1 and SDC4 polymorphisms with breast cancer in an Australian Caucasian population.

P2860

Q24290826-B6523BCC-B640-4430-9AB4-205A2212920E Q24294223-D9CF3EC7-749A-4069-99B1-FB876629C122 Q24530478-3B7682F9-4F31-437E-9532-060CC4E3A06B Q24534902-D5A1D292-38EB-4B5F-B445-9DA802D5AE41 Q24561731-885C74E8-0C5A-47C4-98BE-030022524D0A Q24669779-2566A0C0-D264-42AA-83D7-2EA69029C2D8 Q24681644-6C57DF91-C57A-474F-9E6A-25F06423A9B3 Q24807364-CCBFD72B-0CE8-4892-98A4-BA26BD226773 Q28220451-7EEC703B-710E-4D44-BF3B-389EF5B2D382 Q28263713-A69CAA30-5254-42B9-B052-2D36ED08EE5E Q28279306-41AEF97B-55AC-4ABF-9213-CF66D49944DA Q28634029-D576A5BB-DF43-4962-82B4-C6CA8EBFFA28 Q31086903-CADC3199-5DAA-4485-8911-52440EA9E102 Q33843447-C4D2B88A-D7A4-41D1-8FCC-AD9859FF2FCE Q33912935-6B107C84-9724-492F-9FCD-46D684A51FBF Q33929819-2A740E0B-57B7-4C53-B2E3-BA6BB3C8ADAC Q34110646-AB8E892A-CD37-4551-90D6-E49D7F0393F7 Q34465265-55D35040-68C1-4F6D-A691-7E03E945304D Q34475894-34F19A09-AC62-4361-BF92-EF3A1600FA0D Q35061017-E8D49FFA-EF69-421E-A508-F83334C81BAA Q35441324-D6512B17-D728-4F51-96D7-72CD6E54AD1D Q35535743-84EE81F9-4FF7-473B-9CEF-1529D03CF796 Q35768137-9139F7CF-5B24-48FD-9D17-102CECBDBFC6 Q36323393-C5F1B43A-7FA7-4597-AF54-688897970A71 Q36325233-0574D0DD-C5DA-4C2F-9BA7-7C477DF27CCC Q36748725-C294CC9B-8127-4280-AE7E-0E670E504BC1 Q36815331-54CDACF2-66DB-4BD0-9448-3B40A96E1DF9 Q36867742-B223BB1D-974A-4828-8E0A-F18226CC7974 Q37258548-40CA1BCB-D100-41C6-88B6-0D1620CE2AE9 Q37475741-6D8E440E-29DE-4F3B-A01A-298E2072760B Q39530397-226B0BBA-AF07-422D-B28B-92F1031B889B Q39895619-ABD63E47-F7DA-415F-AB48-EE114E9723CF Q40648094-7FA65E0C-7B02-4624-B71B-346061BB8E03 Q40690959-D33EE472-55D9-4004-A4D5-DB2C1D544B9F Q40806631-6974A9F7-408A-4C78-93D7-B892A77C6AAE Q40939688-A591773E-DBB2-405D-B5EE-78954079390F Q41109997-A44379DF-3183-401B-9FBE-CDE53776E38A Q42048950-1BBDAB24-646D-4F49-9A7A-2492ABC6BC01 Q43508051-8798661F-B2AD-48EF-B173-D6BE45BEAEEC Q43752663-49951446-891A-448D-BE06-9192F26114D1

P2860

Protein kinase C regulates the recruitment of syndecan-4 into focal contacts

http://www.wikidata.org/entity/Q34452929

description

1995 nî lūn-bûn

@nan

1995 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

1995 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

1995年の論文

@ja

1995年論文

@yue

1995年論文

@zh-hant

1995年論文

@zh-hk

1995年論文

@zh-mo

1995年論文

@zh-tw

1995年论文

@wuu

name

Protein kinase C regulates the recruitment of syndecan-4 into focal contacts

@ast

Protein kinase C regulates the recruitment of syndecan-4 into focal contacts

@en

Protein kinase C regulates the recruitment of syndecan-4 into focal contacts

@nl

type

label

Protein kinase C regulates the recruitment of syndecan-4 into focal contacts

@ast

Protein kinase C regulates the recruitment of syndecan-4 into focal contacts

@en

Protein kinase C regulates the recruitment of syndecan-4 into focal contacts

@nl

prefLabel

Protein kinase C regulates the recruitment of syndecan-4 into focal contacts

@ast

Protein kinase C regulates the recruitment of syndecan-4 into focal contacts

@en

Protein kinase C regulates the recruitment of syndecan-4 into focal contacts

@nl

P1433

Q34452929-1F1382A5-3172-46F9-8C66-E0BE95B75BC9

P1476

Q34452929-895CC989-9366-4148-9588-B176E260A2BA

P2093

Q34452929-53E3487F-2701-4909-BF5D-75BFF05CD2C5

Q34452929-CDF7ADE6-3466-44AC-AB72-3E79369469F4

P2860

Q34452929-0156E38D-D952-4237-AB51-F696B3CB6D0E

Q34452929-06267780-470E-4917-9127-9DAB17C93DB7

Q34452929-0B8A4397-0AC7-468E-B97C-EC923AB64F6C

Q34452929-0EDF547B-9850-4760-97DB-96C8559CC6D4

Q34452929-1BB3D5AC-E9E5-4A6A-8B27-56B039073726

Q34452929-1D022F6C-F2D9-48CE-B4E6-FCF7DB7EEFB5

Q34452929-25483102-6663-4B52-8B5E-F6D3D0F710D7

Q34452929-283EFA79-3356-46DE-903B-469349BC1E37

Q34452929-2A027E7E-3EFF-467B-83FF-7A31BDD59E83

Q34452929-2CB8DEBD-7908-4085-98FE-C767657E9CB2

P304

Q34452929-6714228B-F177-4B39-8C84-EB118BC953F6

P31

Q34452929-0B8C3002-ABE1-416C-BA47-4A007BA69B78

P356

Q34452929-96E3A3C1-A1BF-45D6-A236-3345B757D9D6

P433

Q34452929-CEC86FF1-B310-4C62-B30E-82C9EEA3EE18

P478

Q34452929-BC94DC99-0D1C-4D8D-8708-E4475A309E08

P577

Q34452929-BBE76CF2-45F6-41FA-9376-C64D69596123

P5875

Q34452929-CAAC6C1C-AB69-49CC-8B0A-2BBFA59F26AB

P698

Q34452929-10110159-DAEA-4E39-9D9E-E9159822C91E

P932

Q34452929-BDCA7E0F-FE5B-4B6B-91A5-CA73967D7801

P356

P1433

Molecular Biology of the Cell

P1476

Protein kinase C regulates the recruitment of syndecan-4 into focal contacts

@en

P2093

P C Baciu

http://www.w3.org/2001/XMLSchema#string

P F Goetinck

http://www.w3.org/2001/XMLSchema#string

P2860

Syndecan 4 heparan sulfate proteoglycan is a selectively enriched and widespread focal adhesion component

Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly

The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors

Regulation of fibronectin receptor distribution

Identification of amino acid sequences in the integrin beta 1 cytoplasmic domain implicated in cytoskeletal association

Biology of the syndecans: a family of transmembrane heparan sulfate proteoglycans

Heparan sulfate fibroblast growth factor receptor complex: structure-function relationships

A 130K protein from chicken gizzard: its localization at the termini of microfilament bundles in cultured chicken cells

Function of the syndecans--a family of cell surface proteoglycans

Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin fragments

P304

1503-1513

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1091/MBC.6.11.1503

http://www.w3.org/2001/XMLSchema#string

P433

11

http://www.w3.org/2001/XMLSchema#string

P478

6

http://www.w3.org/2001/XMLSchema#string

P577

1995-11-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

14612001

http://www.w3.org/2001/XMLSchema#string

P698

8589452

http://www.w3.org/2001/XMLSchema#string

P932

301307

http://www.w3.org/2001/XMLSchema#string