Characterization of palladin, a novel protein localized to stress fibers and cell adhesions.
about
Palladin mutation causes familial pancreatic cancer and suggests a new cancer mechanismMyopalladin, a novel 145-kilodalton sarcomeric protein with multiple roles in Z-disc and I-band protein assembliesCharacterization of human palladin, a microfilament-associated proteinDisruption of alpha-actinin-integrin interactions at focal adhesions renders osteoblasts susceptible to apoptosisIdentification of four gene variants associated with myocardial infarction.Focal adhesion kinase and p130Cas mediate both sarcomeric organization and activation of genes associated with cardiac myocyte hypertrophyPalladin interacts with SH3 domains of SPIN90 and Src and is required for Src-induced cytoskeletal remodelingPalladin is overexpressed in the non-neoplastic stroma of infiltrating ductal adenocarcinomas of the pancreas, but is only rarely overexpressed in neoplastic cellsActin binding proteins, spermatid transport and spermiationPalladin is upregulated in kidney disease and contributes to epithelial cell migration after injuryStructure and function of palladin's actin binding domain.Molecular analysis of the interaction between palladin and alpha-actininThe proline-rich protein palladin is a binding partner for profilinA class III PDZ binding motif in the myotilin and FATZ families binds enigma family proteins: a common link for Z-disc myopathiesRole of palladin phosphorylation by extracellular signal-regulated kinase in cell migrationSyndecan-4 associates with alpha-actininHypoxia inhibits differentiation of lineage-specific Rcho-1 trophoblast giant cellsBiallelic Mutations in MYPN, Encoding Myopalladin, Are Associated with Childhood-Onset, Slowly Progressive Nemaline MyopathyActin polymerization is stimulated by actin cross-linking protein palladin.The actin associated protein palladin in smooth muscle and in the development of diseases of the cardiovasculature and in cancer.The actin associated protein palladin is important for the early smooth muscle cell differentiation.The actin-associated protein Palladin is required for development of normal contractile properties of smooth muscle cells derived from embryoid bodies.The actin-bundling protein palladin is an Akt1-specific substrate that regulates breast cancer cell migrationZyxin is not colocalized with vasodilator-stimulated phosphoprotein (VASP) at lamellipodial tips and exhibits different dynamics to vinculin, paxillin, and VASP in focal adhesions.Target deletion of the cytoskeleton-associated protein palladin does not impair neurite outgrowth in miceIsoform-specific upregulation of palladin in human and murine pancreas tumors.Hypoxia-inducible factor 1alpha (HIF1A) mediates distinct steps of rat trophoblast differentiation in gradient oxygen.A role for the cytoskeleton-associated protein palladin in neurite outgrowth.Elevated expression of stromal palladin predicts poor clinical outcome in renal cell carcinoma.The key feature for early migratory processes: Dependence of adhesion, actin bundles, force generation and transmission on filopodiaThe glomerulus--a view from the outside--the podocyte.Arousal of cancer-associated stroma: overexpression of palladin activates fibroblasts to promote tumor invasion.Akt2 regulates expression of the actin-bundling protein palladinDynamic regulation of sarcomeric actin filaments in striated muscleMorphology and viscoelasticity of actin networks formed with the mutually interacting crosslinkers: palladin and alpha-actinin.DIM-1, a novel immunoglobulin superfamily protein in Caenorhabditis elegans, is necessary for maintaining bodywall muscle integrityCaenorhabditis elegans kettin, a large immunoglobulin-like repeat protein, binds to filamentous actin and provides mechanical stability to the contractile apparatuses in body wall muscle.Dual roles of palladin protein in in vitro myogenesis: inhibition of early induction but promotion of myotube maturation.Stromal Palladin Expression Is an Independent Prognostic Factor in Pancreatic Ductal AdenocarcinomaRedox-Sensitive Regulation of Myocardin-Related Transcription Factor (MRTF-A) Phosphorylation via Palladin in Vascular Smooth Muscle Cell Differentiation Marker Gene Expression
P2860
Q21144683-334A1E59-C224-4E91-B632-19FDFFA32F7EQ24291134-D6D3DAE7-DD8B-4943-B6BC-6B0B6F0089B0Q24291793-13D75C18-A86E-4150-9BD5-DAF5A0F6633BQ24294897-C0845494-A439-4F83-A049-F1979D1A6E68Q24536320-23A98552-D793-4191-908B-9A86DF42C3F2Q24555199-4CF0F3BD-AB72-4D30-9EF9-C8327A5EB749Q24564764-D052B5D9-6932-45A7-B7F0-4828DB06F697Q24628890-0363422C-F29F-4C03-9E3A-AC62A9201CEFQ27001537-DD4A69F0-B457-43EE-B014-AC7969EC9E3EQ27309161-72355876-475A-4C91-93A5-A963B68F3412Q27678831-F65A4868-0B08-4064-824B-8E845F4A7D92Q28262161-04CC9404-A82C-4EC0-9293-8D90DFE439CCQ28287889-CE583BE7-3114-4211-A958-7E7A867F168FQ28302336-53E68DAB-DA4E-494A-B8B7-4FA39A5FB01BQ28478612-AFC6A278-F711-4306-BB8C-EB316FC76F1BQ28565623-618C504D-35A3-4150-8DD7-FAFA6E7091BFQ28578458-9DA258F0-C158-4D7E-B38B-3462F3C23B6EQ29147433-3C8EFD6A-5AA4-433F-988C-702EC8B2CD91Q30278021-660ECDBD-383E-44A0-BE57-CCC4D4A0B2F7Q30425751-3080F8E7-F3BF-4756-8363-5BBE9CC3D9FDQ30434710-CCF936E4-5C63-4447-8EF1-98FCC994F21CQ30437315-841844FE-3CBF-4B57-ABA9-EE532B49F697Q30494570-F6A33539-2673-44F3-B6E8-F0A31DB694F1Q30856960-B9C86DAE-71EF-4839-8AE6-71CD9A76A11AQ33500156-0C087D02-577C-447E-ACB5-1738D0BF5D0BQ33570447-A2E073CC-1011-45CB-8275-C905C34F69A5Q33583688-036D89B0-A999-42B0-ADD1-0AC9BEB4FB1DQ33946710-A79A1774-FE26-494F-871C-51A59A4D9C88Q33954959-FFC901DB-1488-400C-8EE2-E3F52AB1F8B4Q33977473-D0BB0B1B-D907-4357-899C-9D4BD93EB0FDQ34020798-6A85C50F-63E5-4320-8925-5EA0990C87AAQ34145927-B958D045-0130-4F2C-AA50-303396F29E7EQ34148087-25E7772A-B03C-4737-AB42-B053C071FC65Q34235998-E4BCEFFC-797A-4D82-AECC-C86E9C34C615Q34391013-6D6A4E58-E3BA-41C8-9285-EA9B220F8FAAQ34617142-D71D541E-9405-46EB-AB5C-D698124B2825Q34661750-DD4EB383-607C-4E4B-87EE-6B24682403A1Q35413803-68B92099-6EDC-4A63-8C9E-DAF336FC2055Q35972678-F01E9A9B-7C6B-4A84-B242-D2CFA6272A66Q35992443-74EA8E9A-D0EE-499C-9986-949417467108
P2860
Characterization of palladin, a novel protein localized to stress fibers and cell adhesions.
description
2000 nî lūn-bûn
@nan
2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Characterization of palladin, ...... ress fibers and cell adhesions
@nl
Characterization of palladin, ...... ess fibers and cell adhesions.
@ast
Characterization of palladin, ...... ess fibers and cell adhesions.
@en
type
label
Characterization of palladin, ...... ress fibers and cell adhesions
@nl
Characterization of palladin, ...... ess fibers and cell adhesions.
@ast
Characterization of palladin, ...... ess fibers and cell adhesions.
@en
prefLabel
Characterization of palladin, ...... ress fibers and cell adhesions
@nl
Characterization of palladin, ...... ess fibers and cell adhesions.
@ast
Characterization of palladin, ...... ess fibers and cell adhesions.
@en
P2860
P3181
P356
P1476
Characterization of palladin, ...... ess fibers and cell adhesions.
@en
P2093
P2860
P304
P3181
P356
10.1083/JCB.150.3.643
P407
P577
2000-08-01T00:00:00Z