Alternative splicing controls the mechanisms of FAK autophosphorylation - Wikidata - wikimedia - TriplyDB

Alternative splicing controls the mechanisms of FAK autophosphorylation

Alternative splicing controls the mechanisms of FAK autophosphorylation

http://www.wikidata.org/entity/Q28118951

about

Structural basis for the autoinhibition of focal adhesion kinase Tuning cell migration: contractility as an integrator of intracellular signals from multiple cues Physical biology in cancer. 4. Physical cues guide tumor cell adhesion and migration Altering FAK-paxillin interactions reduces adhesion, migration and invasion processes FAK dimerization controls its kinase-dependent functions at focal adhesions Phosphatidylinositol 4,5-bisphosphate triggers activation of focal adhesion kinase by inducing clustering and conformational changes PIAS1-mediated sumoylation of focal adhesion kinase activates its autophosphorylation FAK deficiency in cells contributing to the basal lamina results in cortical abnormalities resembling congenital muscular dystrophies Mechanism of Focal Adhesion Kinase Mechanosensing Depolarization activates ERK and proline-rich tyrosine kinase 2 (PYK2) independently in different cellular compartments in hippocampal slices Focal adhesion kinase: in command and control of cell motility Tyrosine phosphorylation of cortactin by the FAK-Src complex at focal adhesions regulates cell motility FERM domain interaction promotes FAK signaling.Organization and post-transcriptional processing of focal adhesion kinase gene.Activation of endogenous FAK via expression of its amino terminal domain in Xenopus embryos Role of focal adhesion kinase in oocyte-follicle communication.New insights into FAK phosphorylation based on a FAT domain-defective mutation Alternative splicing in oncogenic kinases: from physiological functions to cancer How focal adhesion kinase achieves regulation by linking ligand binding, localization and action Thioredoxin reductase linked to cytoskeleton by focal adhesion kinase reverses actin S-nitrosylation and restores neutrophil β(2) integrin function Src, p130Cas, and Mechanotransduction in Cancer Cells Visualizing and manipulating focal adhesion kinase regulation in live cells.Regulation of focal adhesion kinase activation, breast cancer cell motility, and amoeboid invasion by the RhoA guanine nucleotide exchange factor Net1.pHocal adhesion kinase regulation is on a FERM foundation.FERM control of FAK function: implications for cancer therapy.Reconciling the roles of FAK in osteoblast differentiation, osteoclast remodeling, and bone regeneration.Dilated cardiomyopathy caused by tissue-specific ablation of SC35 in the heart.A non-canonical role for Rgnef in promoting integrin-stimulated focal adhesion kinase activation.Autophosphorylation-independent and -dependent functions of focal adhesion kinase during development.Targeting focal adhesion kinase in fibrotic diseases.RhoGEFs in cell motility: novel links between Rgnef and focal adhesion kinase.How to find a leucine in a haystack? Structure, ligand recognition and regulation of leucine-aspartic acid (LD) motifs.The diverse roles and multiple forms of focal adhesion kinase in brain.Integrin-FAK signaling rapidly and potently promotes mitochondrial function through STAT3 Integrin adhesions: who's on first? What's on second? Connections between FAK and talin.Spatial and temporal regulation of focal adhesion kinase activity in living cells.Regulation of focal adhesion kinase by its amino-terminal domain through an autoinhibitory interaction.Residues within the first subdomain of the FERM-like domain in focal adhesion kinase are important in its regulation.Calcium rises locally trigger focal adhesion disassembly and enhance residency of focal adhesion kinase at focal adhesions.β1-Integrin cytoskeletal signaling regulates sensory neuron response to matrix dimensionality.

P2860

37659b8b0639b01cad1d26a6734ac906f37acf46 dc9efe7ac88b519438a5bb552215f03cdda00527

P248

Q24678318-CB92F883-6149-4AF4-8766-3D77BB303860 Q26742035-EBB6AAC2-A03A-4A88-9FC1-964C3F2C4780 Q26863598-3DEF6B2A-8982-48CE-812F-BE443FE90404 Q27314883-4885C0BA-F6C7-46DC-BA2E-83A02FF2C4B1 Q27681534-D934942B-62E3-4BE1-ADBD-1709B2E25507 Q27684765-65510F20-C345-439A-B3FE-E6624FA9819C Q28204032-7EC15EC7-EBA4-4C7D-A0B5-09B02164D99F Q28511784-26996B8E-183E-478A-A0AF-375ECD559B12 Q28550745-E8DC8729-BE09-434D-87AD-44D2F81BD2EF Q28566318-03A0A292-8D43-4133-BBE3-0A5F6CD93736 Q29615192-789449C4-AA9A-4599-95F4-9C4EC8ADB493 Q30010209-9F0CD993-A9CA-41CA-AFBB-3D230DA645E7 Q30449206-C2AE5544-7679-4545-B450-D79A24291DD3 Q33252921-CB57A602-F358-4AC4-8B40-AD8E59F07306 Q34374368-147554DA-724B-4E00-8C92-1A80EA780A43 Q35072913-DAC6F68B-B75D-418A-B7E1-BAA84F0304D9 Q35255826-8FA30A20-CD0A-417B-BF67-9187577AC730 Q35295203-221C8B0E-4844-402F-A42F-68BC510C4B72 Q35597027-A7D1317C-DC6A-4F61-A9D2-9858A897E53E Q36216366-9EB0677E-DB9D-4703-97CC-01B121F46E94 Q36443416-F0F038A8-C91B-49A3-B9AD-8145AEF90D75 Q36724913-F6C9EE96-025E-46C6-98EE-BCBEB1EF13E4 Q36978333-75C06293-D464-4EDF-921F-6401CD98E00F Q37180585-8752AC21-0CDD-4BD4-8259-EAECE41636D8 Q37234240-5F2C533B-A7A2-411D-9BB5-DE206316EB58 Q37234953-3976DB33-249C-41C9-83EC-B91F5A10C28D Q37259559-73E3660E-2E1F-4DC0-8106-7D841C4519A2 Q37287392-AE8E143E-7FBB-4F21-B92D-E02CB1F816BF Q37454238-B9F1E8BC-4F0F-48E8-82D4-7BFA1F9CE770 Q38074882-C8E54BB0-1040-43C0-A1E8-F7BAB1BBAB76 Q38182132-053C434F-0548-453D-B1B2-691FBA952E2C Q38215562-BCBB892B-A316-4099-B358-BF6D543A902E Q38255120-2CDD0609-1FCC-4775-96F2-4A5696148CFC Q38726100-0143A03A-A620-406F-A2C4-6342EE8F445E Q39277662-3C29C9B9-B4F6-44E4-8C9E-18E2CF476B2F Q40060648-91423515-02AA-4642-A018-B9EE3CDDFF00 Q40172193-0B282FBA-70CF-403F-B043-56D8FBABE8BE Q40478503-5D843C6C-B120-4A86-ADF0-24BE8E0E91DE Q40563935-86A70467-0DAD-460D-9BE8-770683C3A003 Q42015808-D4358720-2D50-43F9-B7B0-B3D2CC2FF173

P2860

Alternative splicing controls the mechanisms of FAK autophosphorylation

http://www.wikidata.org/entity/Q28118951

description

2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

artículu científicu espublizáu en 2002

@ast

im November 2002 veröffentlichter wissenschaftlicher Artikel

@de

scientific journal article

@en

vedecký článok (publikovaný 2002/11/01)

@sk

vědecký článek publikovaný v roce 2002

@cs

wetenschappelijk artikel (gepubliceerd op 2002/11/01)

@nl

наукова стаття, опублікована в листопаді 2002

@uk

مقالة علمية (نشرت في نوفمبر 2002)

@ar

name

Alternative splicing controls the mechanisms of FAK autophosphorylation

@ast

Alternative splicing controls the mechanisms of FAK autophosphorylation

@en

Alternative splicing controls the mechanisms of FAK autophosphorylation

@nl

type

label

Alternative splicing controls the mechanisms of FAK autophosphorylation

@ast

Alternative splicing controls the mechanisms of FAK autophosphorylation

@en

Alternative splicing controls the mechanisms of FAK autophosphorylation

@nl

prefLabel

Alternative splicing controls the mechanisms of FAK autophosphorylation

@ast

Alternative splicing controls the mechanisms of FAK autophosphorylation

@en

Alternative splicing controls the mechanisms of FAK autophosphorylation

@nl

P1433

Q28118951-385A2515-12F2-4256-956F-4A7D40EDD486

P1476

Q28118951-D64620E4-F5C6-43C2-B277-0595CDA3E76E

P2093

Q28118951-3EA9712D-007D-4851-8278-1AE007712601

Q28118951-663C056A-71AA-4005-806D-C407AFD6BED6

Q28118951-9073D49F-96BB-4330-8E5F-1BD897A52BF6

Q28118951-96C55CE1-A47C-424D-AE3E-098BD239DF62

Q28118951-9B14FA4E-74EC-466E-A882-FF5026299D8D

P2860

Q28118951-025B7FB8-4E14-4EC8-9896-FA3605833629

Q28118951-0889622A-B1FB-4E66-AD26-BA6F07290954

Q28118951-0CFCA033-0CD9-4919-A629-A90B992E5778

Q28118951-0DC1AAA9-787C-4D5D-BA3E-96E34A5D6EF9

Q28118951-1201712C-576E-4D4C-BE3D-74E0E5870E3B

Q28118951-14AA9235-3424-4FA2-B43E-888777EAF293

Q28118951-1D245024-C247-4D73-9285-0663A5AB4C42

Q28118951-1ED02667-2859-4FE0-8C62-440813928F21

Q28118951-29290910-BA68-4F9C-A60B-D1F095253554

Q28118951-2A57A184-8A06-4A85-A9CA-30057050A869

P304

Q28118951-9DA614F3-5907-4D2E-BCFA-5F4FF1E3F269

P31

Q28118951-69FB0249-68F9-4A48-9A0F-C1B00730E30A

P3181

Q28118951-ABED8BCD-9AB4-412D-B75F-0CF016F926CC

P356

Q28118951-DDCCD8CF-8722-439A-A7C8-426276A6D1AB

P407

Q28118951-C91A4CEA-E58B-42C5-9CAB-8713961F173F

P433

Q28118951-E49A228C-0EA6-46FD-9899-234228B7F013

P478

Q28118951-6D9FE6C7-8294-4F67-AA2C-3BE17803D169

P50

Q28118951-192CC905-E189-46B8-B1C5-900ED42E0E5F

P577

Q28118951-E76073E4-8AF4-412B-BA40-07C5554487BB

P698

Q28118951-E8BA850A-2A7F-4942-9197-4235E52F382D

P921

Q28118951-65A40096-3169-4721-AEDC-BB03E27B4CBD

Q28118951-9342FDAB-1DF2-4119-AA7E-8CAF81255372

P932

Q28118951-889B1BF2-BB65-48A3-8DE4-F5F63165E62B

P3181

P356

MCB.22.22.7731-7743.2002

P1433

Molecular and Cellular Biology

P1476

Alternative splicing controls the mechanisms of FAK autophosphorylation

@en

P2093

Alicia Costa

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

Gress Kadaré

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

Jeanne-Marie Studler

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

Madeleine Toutant

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

Michèle Carnaud

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

P2860

Interaction of Hic-5, A senescence-related protein, with focal adhesion kinase

Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases

Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK

Evidence for in vivo phosphorylation of the Grb2 SH2-domain binding site on focal adhesion kinase by Src-family protein-tyrosine kinases

pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions.

Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain

The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src

Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase.

An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase

P304

7731-7743

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

P31

scholarly article

P3181

4388803

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

P356

10.1128/MCB.22.22.7731-7743.2002

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

P407

P433

22

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

P478

22

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

P50

Jean-Antoine Girault

P577

2002-11-01T00:00:00Z

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

P698

12391143

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

P921

protein tyrosine kinase activity

Protein tyrosine kinase 2

P932

134714

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