Site-specific phosphorylation induces disassembly of vimentin filaments in vitro
about
Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory proteinIntermediate Filaments Play a Pivotal Role in Regulating Cell Architecture and FunctionAltered phosphorylation and distribution status of vimentin in rat seminiferous epithelium following 17β-estradiol treatmentPhosphorylation of keratin intermediate filaments by protein kinase C, by calmodulin-dependent protein kinase and by cAMP-dependent protein kinaseMajor phosphorylation site (Ser55) of neurofilament L by cyclic AMP-dependent protein kinase in rat primary neuronal culture.Enterovirus 71 VP1 activates calmodulin-dependent protein kinase II and results in the rearrangement of vimentin in human astrocyte cells.The intermediate filament protein vimentin is a new target for epigallocatechin gallate.Site-directed spin labeling and electron paramagnetic resonance determination of vimentin head domain structure.Regulation of intermediate filament organization during cytokinesis: possible roles of Rho-associated kinase.Phosphorylation of a novel cytoskeletal protein (RsmP) regulates rod-shaped morphology in Corynebacterium glutamicum.Evidence that formation of vimentin mitogen-activated protein kinase (MAPK) complex mediates mast cell activation following FcεRI/CC chemokine receptor 1 cross-talk.A decade of site- and phosphorylation state-specific antibodies: recent advances in studies of spatiotemporal protein phosphorylation.Vimentin as an integral regulator of cell adhesion and endothelial sprouting.The dermatan sulfate proteoglycan decorin modulates α2β1 integrin and the vimentin intermediate filament system during collagen synthesisPhosphorylation of glial fibrillary acidic protein and vimentin by cytoskeletal-associated intermediate filament protein kinase activity in astrocytes.Intermediate filaments in Sertoli cells.Intermediate filament dynamics: What we can see now and why it matters.The differential expression of proteins in the cortical cells of wool and hair fibres.Cellular intermediate filament networks and their derangement in alcoholic hepatitis.Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis.The regulation of neurofilament protein dynamics by phosphorylation: clues to neurofibrillary pathobiology.Aggresomes resemble sites specialized for virus assembly.Dynamics of intermediate filaments. Recent progress and unanswered questions.Balance between activities of Rho kinase and type 1 protein phosphatase modulates turnover of phosphorylation and dynamics of desmin/vimentin filaments.Alterations of intermediate filaments in various histopathological conditions.Purification and characterization of a vimentin-specific protease in mouse myeloid leukemia cells. Regulation during differentiation and identity with cathepsin G.Myofibril breakdown during atrophy is a delayed response requiring the transcription factor PAX4 and desmin depolymerization.Cdk5 mediates vimentin Ser56 phosphorylation during GTP-induced secretion by neutrophils.Protein phosphatase inhibitor calyculin A induces hyperphosphorylation of cytokeratins and inhibits amylase exocytosis in the rat parotid acini.Head and rod 1 interactions in vimentin: identification of contact sites, structure, and changes with phosphorylation using site-directed spin labeling and electron paramagnetic resonance.Induction of adipose conversion in 3T3-L1 cells is associated with an early phosphorylation of a protein partly homologous with mouse vimentin.Protein kinases required for segregation of vimentin filaments in mitotic process.The differential role of protein kinase C isozymes in the rapid induction of neurofilament phosphorylation by nerve growth factor and phorbol esters in PC12 cells.Immunoelectron microscopical localization of the catalytic subunit of cAMP-dependent protein kinases in brain microtubules and neurofilaments.Opioid peptides modulate the organization of vimentin filaments, phagocytic activity, and expression of surface molecules in monocytes.Binding of nucleic acids to intermediate filaments of the vimentin type and their effects on filament formation and stability.Intracellular delivery of protein kinase C-alpha or -epsilon isoform-specific antibodies promotes acquisition of a morphologically differentiated phenotype in neuroblastoma cells.Neurofilament subunits can undergo axonal transport without incorporation into Triton-insoluble structures.Identification of a vimentin-like function associated molecule (FAM) on rat NK cells: evidence for receptor function.Histopathological changes at central nodes of Ranvier after stretch-injury.
P2860
Q24290130-E4FA0D24-3602-40E4-B7EA-3D347EABDC63Q26865818-83C632B3-B6D2-4D6F-848A-EC79AC1FC6BEQ28572281-DA4F8C75-5BE2-4903-A0F1-05A01DB29562Q28574166-81D47E9B-C156-4993-84BF-88223868CBA6Q30842586-EC3ECBA9-3659-40DD-BE81-FF64B03BB6EFQ31140321-0F210552-979C-4B4D-98DF-B56C5A0B1B9CQ33211958-C1216333-F401-4CDA-9CF1-1FCAFE8ECB5CQ33832679-CC66A1BB-9BC3-4F50-AE0F-CE9D29C1BBA2Q33921474-6B2DD9E8-A6E5-4AC7-B580-AC41AEEF9CF5Q34121598-E3C74807-53AD-43E5-B0D4-67079453362EQ34276341-E558CD80-D2F2-46FB-BAA6-E5E09EA0ABFDQ34352878-5410C97C-5274-4360-95B8-DA040F962807Q34395548-8B7DF53A-C29D-4417-A099-5752F7CAA8BEQ34506615-2DD47EE5-371E-4091-ACDD-9F54E6B12BC2Q34608963-AB5B415D-B62F-4A57-877C-A8CBCBA37EC1Q35323742-A1A1BB23-BC82-4D77-99AC-F95AAE1C6518Q36635435-E08975BC-DF0E-45B4-97EC-EFD99CC8827AQ36909560-09D9E29F-C17C-4601-B636-EB2FCA8EF946Q37794533-01EAE9EF-D601-437E-8947-17C3FAC7B405Q40356177-091A2B84-8553-4199-910F-F0FCB2B1AC6FQ40384992-76D54F3A-C7D8-4F11-8287-D92AFE5A763EQ40603651-B20F54BB-2F95-4E5D-91B2-4CA70A88A27CQ40879798-B2675B3A-B529-4E4C-A57C-6DC5728A322EQ40915834-7D7FE284-40F9-4750-B68B-0A80767913FEQ41037907-DBF3E949-CA20-4987-926F-784B0B456000Q41625635-AA246D58-1A5B-416F-B049-6CCE9E18B9BAQ41943570-B005A71D-3F23-46DD-B00C-E2DAF8B69B9EQ41974981-86C78415-6FB0-44E6-9658-B7842C4A5378Q42483224-161BABD6-A2A2-4AC0-B24C-EAF1EDD725DFQ42736271-7AB7A2EB-96A9-4B68-B196-C9BDFBC71691Q42805523-B1C34D78-4FF1-413F-8A35-3AC92A1296F8Q43649372-13801B00-2D99-43D5-BC44-8BD9FFFC508AQ43694319-B45D2E4E-1A43-4C9F-9232-9145BC54131DQ44232524-1313EB03-3798-4F42-8DE0-F0074FDE0DEDQ44341623-C88D577D-13E3-4BD3-A472-11EC1DBFE170Q44949252-6264CCA0-E6A1-4328-B5A4-6456F26D9738Q45515547-408D78AE-2A2F-4E5A-9EDA-8CC73D71FD8BQ48029252-86F66CC3-B6FC-42E3-B37D-94A13C8ADC2FQ48134730-034CF95C-20A6-4546-AD23-4C42D9DAE8F5Q48942464-CBC82275-3212-491F-9D56-E60DAA0575FD
P2860
Site-specific phosphorylation induces disassembly of vimentin filaments in vitro
description
article publié dans la revue scientifique Nature
@fr
scientific article published in Nature
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в Nature в серпні 1987
@uk
name
Site-specific phosphorylation induces disassembly of vimentin filaments in vitro
@en
Site-specific phosphorylation induces disassembly of vimentin filaments in vitro
@nl
type
label
Site-specific phosphorylation induces disassembly of vimentin filaments in vitro
@en
Site-specific phosphorylation induces disassembly of vimentin filaments in vitro
@nl
prefLabel
Site-specific phosphorylation induces disassembly of vimentin filaments in vitro
@en
Site-specific phosphorylation induces disassembly of vimentin filaments in vitro
@nl
P2093
P356
P1433
P1476
Site-specific phosphorylation induces disassembly of vimentin filaments in vitro
@en
P2093
P2888
P304
P356
10.1038/328649A0
P407
P577
1987-08-01T00:00:00Z
P6179
1040519540