The N-termini of FAK and JAKs contain divergent band 4.1 domains.
about
Metallo-beta-lactamase fold within nucleic acids processing enzymes: the beta-CASP family.Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domainTyrosine phosphorylation of p97 regulates transitional endoplasmic reticulum assembly in vitroPrediction of the general transcription factors associated with RNA polymerase II in Plasmodium falciparum: conserved features and differences relative to other eukaryotesFAK and paxillin, two potential targets in pancreatic cancerStructural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex.Structural Basis for Small G Protein Effector Interaction of Ras-related Protein 1 (Rap1) and Adaptor Protein Krev Interaction Trapped 1 (KRIT1)FAK dimerization controls its kinase-dependent functions at focal adhesionsStructure of the pseudokinase-kinase domains from protein kinase TYK2 reveals a mechanism for Janus kinase (JAK) autoinhibitionAutophosphorylation of JAK2 on tyrosines 221 and 570 regulates its activityAlternative splicing controls the mechanisms of FAK autophosphorylationPIAS1-mediated sumoylation of focal adhesion kinase activates its autophosphorylationThe phosphotyrosine binding-like domain of talin activates integrinsNovel regulators of endothelial barrier functionDifferential biological activity of disease-associated JAK2 mutantsD53 is a novel endosomal SNARE-binding protein that enhances interaction of syntaxin 1 with the synaptobrevin 2 complex in vitroCrystal structure of the FERM domain of focal adhesion kinase.Matrix survival signaling: from fibronectin via focal adhesion kinase to c-Jun NH(2)-terminal kinase.Conformational dynamics of the focal adhesion targeting domain control specific functions of focal adhesion kinase in cells.Targeting Pyk2 to beta 1-integrin-containing focal contacts rescues fibronectin-stimulated signaling and haptotactic motility defects of focal adhesion kinase-null cellsFERM domain interaction promotes FAK signaling.Organization and post-transcriptional processing of focal adhesion kinase gene.Interleukin-2 signaling and inherited immunodeficiency.Molecular interactions of EphA4, growth hormone receptor, Janus kinase 2, and signal transducer and activator of transcription 5B.Interleukin (IL)-7 induces rapid activation of Pyk2, which is bound to Janus kinase 1 and IL-7Ralpha.Interleukin-7 compartmentalizes its receptor signaling complex to initiate CD4 T lymphocyte response.Targeting Pyk2 for therapeutic interventionThe Kindler syndrome protein is regulated by transforming growth factor-beta and involved in integrin-mediated adhesion.The JAK/STAT pathway and Drosophila development.Regulation of the Jak2 tyrosine kinase by its pseudokinase domainThe pseudokinase domain is required for suppression of basal activity of Jak2 and Jak3 tyrosine kinases and for cytokine-inducible activation of signal transduction.FERM domain mutations induce gain of function in JAK3 in adult T-cell leukemia/lymphomaHow focal adhesion kinase achieves regulation by linking ligand binding, localization and actionTyrosine 201 is required for constitutive activation of JAK2V617F and efficient induction of myeloproliferative disease in miceThe glycosylphosphatidyl inositol-anchored adhesion molecule F3/contactin is required for surface transport of paranodin/contactin-associated protein (caspr)Phosphorylation of human Jak3 at tyrosines 904 and 939 positively regulates its activityMUC16 contributes to the metastasis of pancreatic ductal adenocarcinoma through focal adhesion mediated signaling mechanism.The use of structural biology in Janus kinase targeted drug discovery.FERM control of FAK function: implications for cancer therapy.Focal adhesion kinase and its signaling pathways in cell migration and angiogenesis.
P2860
Q24538351-374DE0AB-A6EA-4682-A3A8-D9C38F52D9C1Q24598762-6EC1FAF7-761A-4207-981E-3EED7BC4270AQ24676902-0847C55B-39EB-4CCB-869B-6F5C4DFF8808Q24811411-2561E57F-3B81-42F5-980C-228F05165C5FQ26765360-F67A52CC-9A93-4E61-B475-D66F04E23E93Q27640373-6D50BCFC-33C7-4940-87BD-DA1C27DD4097Q27679017-BE7AEBC1-5677-4AA8-AF8F-EB5868730ADDQ27681534-A32CAC53-228A-46EC-A334-B29D95F6AE2BQ27683852-8A8A52BE-DB7F-4143-B073-C851044F0EF1Q28116068-B505D4DE-7E8F-4E6D-94E0-C23676FCF615Q28118951-96415012-5643-455A-9107-D8BFFE7BCDDCQ28204032-AE6F1F03-4B6E-4128-934E-E4D25B3E7697Q28212748-846CCEBC-A595-4FF7-9FDC-00E60FBF08E0Q28384398-3970915A-35DB-470F-BF3A-80215A728051Q28508045-C5BB9947-6602-425D-A478-370C90E9D031Q28590292-2569E4EF-1E01-4298-97D1-34096548D949Q30160113-26021B0E-92C8-4EC6-A34D-17CB0779EC95Q30175136-83C54107-D17E-431A-B52C-F10DECEED081Q30368603-09ACC759-149C-46C0-ABEC-87AB2B8F5384Q30442000-699EC127-3BD0-4404-A23F-E27B09F54077Q30449206-9A9F6B88-FB4D-45A1-B3C1-928905395504Q33252921-42709433-611D-4363-ADA8-028A30BD8DA1Q33693886-EB404300-5518-4593-937E-CA31EE669770Q33884280-FA16098A-EA2B-4ADA-8A21-5EDF7E6EE22BQ33892194-9BC523E8-6E0E-4378-9CF9-CD72E2C36D03Q34021307-FCA1B5CB-9EAD-41F3-9FFF-55AB591DD143Q34146883-2B030934-50FF-49B3-8F79-BAAA473D8E2CQ34278562-BB6E574F-EA63-48DD-A1A8-C7EA66F7B9A4Q34464680-C3BC259D-4E42-46C5-8CDA-933C1AA78EBFQ34508384-B8284C9B-D711-4DF9-95FE-01B2C53242C6Q34527668-79FBFE69-65EC-42DA-9042-C0FB39153BF7Q35346411-6AF0C41F-95BB-444E-ACB3-7F041B097607Q35597027-61A1DB53-5693-4DAE-82DE-AEC84203EC1EQ36206435-2A570917-9657-4012-AD75-FDCB258D9AD9Q36328347-3005B84C-AA9C-4033-AE42-77E56A50BC90Q36498064-0F7A4EEC-6112-417B-ACBD-E427CBFBE086Q37033307-47E7E6FF-8915-4208-98CE-9CF0A3DC28B0Q37206115-911DE056-087E-4E4B-99DE-AB22FC6DB444Q37234240-C47F4FE1-F17E-44A9-8761-D93D653D6BCEQ37813854-9D7C06DC-2690-4AF6-B1C0-560B7A149165
P2860
The N-termini of FAK and JAKs contain divergent band 4.1 domains.
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The N-termini of FAK and JAKs contain divergent band 4.1 domains.
@ast
The N-termini of FAK and JAKs contain divergent band 4.1 domains.
@en
The N-termini of FAK and JAKs contain divergent band 4.1 domains.
@nl
type
label
The N-termini of FAK and JAKs contain divergent band 4.1 domains.
@ast
The N-termini of FAK and JAKs contain divergent band 4.1 domains.
@en
The N-termini of FAK and JAKs contain divergent band 4.1 domains.
@nl
prefLabel
The N-termini of FAK and JAKs contain divergent band 4.1 domains.
@ast
The N-termini of FAK and JAKs contain divergent band 4.1 domains.
@en
The N-termini of FAK and JAKs contain divergent band 4.1 domains.
@nl
P2093
P1476
The N-termini of FAK and JAKs contain divergent band 4.1 domains.
@en
P2093
Callebaut I
Girault JA
P356
10.1016/S0968-0004(98)01331-0
P577
1999-02-01T00:00:00Z