Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding.
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Interaction of Hic-5, A senescence-related protein, with focal adhesion kinaseEPLIN, epithelial protein lost in neoplasmPaxillin localizes to the lymphocyte microtubule organizing center and associates with the microtubule cytoskeletonStructural basis for paxillin binding and focal adhesion targeting of β-parvinTRIP6 enhances lysophosphatidic acid-induced cell migration by interacting with the lysophosphatidic acid 2 receptorLeupaxin, a novel coactivator of the androgen receptor, is expressed in prostate cancer and plays a role in adhesion and invasion of prostate carcinoma cellsLeupaxin is a novel LIM domain protein that forms a complex with PYK2Brk activates rac1 and promotes cell migration and invasion by phosphorylating paxillinCell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesionsLeupaxin is similar to paxillin in focal adhesion targeting and tyrosine phosphorylation but has distinct roles in cell adhesion and spreading.Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesions involves a multistep activation pathwayInteraction of zyxin, a focal adhesion protein, with the e6 protein from human papillomavirus type 6 results in its nuclear translocationFine mapping of the alpha-actinin binding site within cysteine-rich proteinLPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacityHic-5-reduced cell spreading on fibronectin: competitive effects between paxillin and Hic-5 through interaction with focal adhesion kinaseCoupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassemblyFocal adhesion kinase and p130Cas mediate both sarcomeric organization and activation of genes associated with cardiac myocyte hypertrophyA truncated isoform of the PP2A B56 subunit promotes cell motility through paxillin phosphorylationLasp-1, a novel type of actin-binding protein accumulating in cell membrane extensionsPaxillin comes of ageRegulation of the formation of osteoclastic actin rings by proline-rich tyrosine kinase 2 interacting with gelsolinPhosphorylation of actopaxin regulates cell spreading and migrationPaxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling.Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesionRecruitment of focal adhesion kinase and paxillin to beta1 integrin promotes cancer cell migration via mitogen activated protein kinase activationFAK and paxillin, two potential targets in pancreatic cancerLIM domains target actin regulators paxillin and zyxin to sites of stress fiber strainPaxillin and Focal Adhesion Kinase (FAK) Regulate Cardiac Contractility in the Zebrafish HeartStructural insight into the mechanisms of targeting and signaling of focal adhesion kinase.NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding modelGIT1 Paxillin-binding Domain Is a Four-helix Bundle, and It Binds to Both Paxillin LD2 and LD4 MotifsStructural Analysis of the Interactions Between Paxillin LD Motifs and α-ParvinMolecular Recognition of Leucine-Aspartate Repeat (LD) Motifs by the Focal Adhesion Targeting Homology Domain of Cerebral Cavernous Malformation 3 (CCM3)FAK dimerization controls its kinase-dependent functions at focal adhesionsPxl1p, a paxillin-like protein in Saccharomyces cerevisiae, may coordinate Cdc42p and Rho1p functions during polarized growth.The PXL1 gene of Saccharomyces cerevisiae encodes a paxillin-like protein functioning in polarized cell growth.Homologues of oxysterol-binding proteins affect Cdc42p- and Rho1p-mediated cell polarization in Saccharomyces cerevisiae.Intact LIM 3 and LIM 4 domains of paxillin are required for the association to a novel polyproline region (Pro 2) of protein-tyrosine phosphatase-PESTHic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domainCharacterization of two isoforms of the skeletal muscle LIM protein 1, SLIM1. Localization of SLIM1 at focal adhesions and the isoform slimmer in the nucleus of myoblasts and cytoplasm of myotubes suggests distinct roles in the cytoskeleton and in n
P2860
Q22003881-35239BAD-BCE4-4DCA-B49C-2B10554739E1Q22011008-DBDF51E3-D795-4D00-9E95-E04ED7A2C8F7Q22254255-63FFAE48-F2B4-4A5A-98AD-319C9689EEACQ24295139-5D63425E-FF84-46AF-BE2E-23DF8DCCBF6FQ24302424-C950BD36-B7A5-4D8D-841E-15DFC2594E2FQ24308733-47C39D18-1691-4A5F-9469-8715EFB11E68Q24310713-BC2B38F0-1491-43FA-BADD-D7645EFD0885Q24318315-A0ED561B-5DAA-4372-A93B-3A1AE24EBB7BQ24318621-69AFD728-F8C8-43D5-91A3-DCA780090CF9Q24319896-73A72768-1E17-4852-805A-5A0E90C21D9DQ24524132-B8C24CF6-7C1B-49F4-A655-145BFCB71378Q24529358-4D1703F3-39DC-44EB-BC78-EA8BFFC2D8D5Q24532122-B11158B7-2FDA-4978-8D41-B999C983EC95Q24548041-267A782A-4D4E-4037-9747-155013758D1EQ24550885-C3FBAD4B-78A0-4E11-A974-D12EB6953724Q24552051-C27EC78D-DD3B-49D4-ABE0-4D8906047D04Q24555199-550CE4B4-7C13-4F24-A778-1D8EDC7D16C8Q24601280-49323010-CA4B-4041-9D6B-648AEF51C04AQ24654369-B8E33D7E-190B-4967-A430-0E1C805E6DD7Q24657852-063E9385-AC5F-42DC-B89D-72FF183D46C8Q24671967-6BEE27C5-45F2-4DA7-B3F0-4072AAF51180Q24676994-E4245E32-43D0-436B-AD93-61D60DFFE4FFQ24682031-F7B92D3C-53B5-45AD-B011-D0D47B5DA76BQ24685749-A0393A39-3B90-48D8-925B-8EAE2AC0C1DCQ24801842-E6C6C9AB-35A8-4C19-92CD-41394CE14B97Q26765360-CEE9A5CE-8E72-4E02-8F5E-5A789A985DBCQ27311146-4BC45492-CEDC-4598-A2A8-7E3D4A3488D4Q27319877-91665A0D-80B0-4E11-9F09-08525BF70E9BQ27638457-47272ABB-59BC-4E05-B582-E90A80880AA0Q27642755-35AE91D9-D9D1-4D60-B99B-D641E8A12044Q27650491-131A9744-9BEE-4BDC-8AB1-813A53C36829Q27652592-C679C46F-BF21-4F45-9A9D-2A25A94CF094Q27668126-2BADC160-56A4-42C1-A560-AA0A1AC36E24Q27681534-B6582166-6293-43B1-A447-81353739AC00Q27933264-77EE8DBE-CC22-48FA-8D44-AA21E1059AABQ27934723-27E6894E-A2B8-4B14-B9FD-025377A31201Q27938690-9F669B76-0AEB-48A6-8725-B9F403136BE5Q28139276-133A78A4-C92D-4DAB-B260-803BD7595B70Q28139714-98664FEC-E309-4E10-BC1C-84B6E5705B89Q28144167-D7BEFE6D-E806-4DC9-AAE0-6125BBB2EED1
P2860
Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding.
description
1996 nî lūn-bûn
@nan
1996 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Identification of LIM3 as the ...... focal adhesion kinase binding
@nl
Identification of LIM3 as the ...... focal adhesion kinase binding.
@ast
Identification of LIM3 as the ...... focal adhesion kinase binding.
@en
type
label
Identification of LIM3 as the ...... focal adhesion kinase binding
@nl
Identification of LIM3 as the ...... focal adhesion kinase binding.
@ast
Identification of LIM3 as the ...... focal adhesion kinase binding.
@en
prefLabel
Identification of LIM3 as the ...... focal adhesion kinase binding
@nl
Identification of LIM3 as the ...... focal adhesion kinase binding.
@ast
Identification of LIM3 as the ...... focal adhesion kinase binding.
@en
P2093
P2860
P3181
P356
P1476
Identification of LIM3 as the ...... focal adhesion kinase binding.
@en
P2093
C E Turner
J A Perrotta
P2860
P304
P3181
P356
10.1083/JCB.135.4.1109
P407
P577
1996-11-01T00:00:00Z