Calyculin A-induced vimentin phosphorylation sequesters 14-3-3 and displaces other 14-3-3 partners in vivo
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The growth-promoting activity of the Bad protein in chicken embryo fibroblasts requires binding to protein 14-3-3Proteomic and biochemical analysis of 14-3-3-binding proteins during C2-ceramide-induced apoptosisIdentification of cofilin and LIM-domain-containing protein kinase 1 as novel interaction partners of 14-3-3 zetaKeratin binding to 14-3-3 proteins modulates keratin filaments and hepatocyte mitotic progressionInteraction with 14-3-3 proteins promotes functional expression of the potassium channels TASK-1 and TASK-3Intermediate Filaments Play a Pivotal Role in Regulating Cell Architecture and FunctionBinding and transcriptional regulation by 14-3-3 (Bmh) proteins requires residues outside of the canonical motif.The acid-sensitive, anesthetic-activated potassium leak channel, KCNK3, is regulated by 14-3-3β-dependent, protein kinase C (PKC)-mediated endocytic trafficking.DNA-PK target identification reveals novel links between DNA repair signaling and cytoskeletal regulationA keratin cytoskeletal protein regulates protein synthesis and epithelial cell growthIdentification of Raf-1 S471 as a novel phosphorylation site critical for Raf-1 and B-Raf kinase activities and for MEK bindingMethods for Determining the Cellular Functions of Vimentin Intermediate FilamentsSlow vacuolar channels from barley mesophyll cells are regulated by 14-3-3 proteins.Bimodal regulation of FoxO3 by AKT and 14-3-3Raf-1 activation disrupts its binding to keratins during cell stress.Roles of vimentin and 14-3-3 zeta/delta in the inhibitory effects of heparin on PC-3M cell proliferation and B16-F10-luc-G5 cells metastasisDimerization is essential for 14-3-3zeta stability and function in vivoPhosphorylation-dependent protein interaction with Trypanosoma brucei 14-3-3 proteins that display atypical target recognitionVimentin induces changes in cell shape, motility, and adhesion during the epithelial to mesenchymal transition.Keratin 23, a novel DPC4/Smad4 target gene which binds 14-3-3ε.Identification of potential protein targets of isothiocyanates by proteomicsDynamic multiprotein assemblies shape the spatial structure of cell signalingGenetic networks in the mouse retina: growth associated protein 43 and phosphatase tensin homolog network.The 14-3-3 protein epsilon isoform expressed in reactive astrocytes in demyelinating lesions of multiple sclerosis binds to vimentin and glial fibrillary acidic protein in cultured human astrocytesVimentin in cancer and its potential as a molecular target for cancer therapy.The coordinate cellular response to insulin-like growth factor-I (IGF-I) and insulin-like growth factor-binding protein-2 (IGFBP-2) is regulated through vimentin binding to receptor tyrosine phosphatase β (RPTPβ)Quantitative Proteomics Analysis Reveals Novel Insights into Mechanisms of Action of Long Noncoding RNA Hox Transcript Antisense Intergenic RNA (HOTAIR) in HeLa CellsDynamic interactions between 14-3-3 proteins and phosphoproteins regulate diverse cellular processes.14-3-3 proteins: a number of functions for a numbered protein.Phosphorylation at carboxyl-terminal S373 and S375 residues and 14-3-3 binding are not required for mouse p53 functionCytoskeletal organization of the developing mouse olfactory nerve layer.Significance of 14-3-3 self-dimerization for phosphorylation-dependent target binding.Providing cellular signposts--post-translational modifications of intermediate filaments.Na+/H+ exchanger NHE1 regulation modulates metastatic potential and epithelial-mesenchymal transition of triple-negative breast cancer cells.Structural changes in intermediate filament networks alter the activity of insulin-degrading enzyme.Downregulation of vimentin expression increased drug resistance in ovarian cancer cells.The role of vimentin intermediate filaments in the progression of lung cancer.14-3-3 proteins as signaling integration points for cell cycle control and apoptosis.Oligomeric structure of 14-3-3 protein: what do we know about monomers?Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation.
P2860
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P2860
Calyculin A-induced vimentin phosphorylation sequesters 14-3-3 and displaces other 14-3-3 partners in vivo
description
2000 nî lūn-bûn
@nan
2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
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2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված
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2000年の論文
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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
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2000年论文
@wuu
name
Calyculin A-induced vimentin p ...... other 14-3-3 partners in vivo
@ast
Calyculin A-induced vimentin p ...... other 14-3-3 partners in vivo
@en
Calyculin A-induced vimentin p ...... other 14-3-3 partners in vivo
@nl
type
label
Calyculin A-induced vimentin p ...... other 14-3-3 partners in vivo
@ast
Calyculin A-induced vimentin p ...... other 14-3-3 partners in vivo
@en
Calyculin A-induced vimentin p ...... other 14-3-3 partners in vivo
@nl
prefLabel
Calyculin A-induced vimentin p ...... other 14-3-3 partners in vivo
@ast
Calyculin A-induced vimentin p ...... other 14-3-3 partners in vivo
@en
Calyculin A-induced vimentin p ...... other 14-3-3 partners in vivo
@nl
P2093
P3181
P356
P1476
Calyculin A-induced vimentin p ...... other 14-3-3 partners in vivo
@en
P2093
P304
P3181
P356
10.1074/JBC.M001207200
P407
P577
2000-09-22T00:00:00Z