The roles of the rod end and the tail in vimentin IF assembly and IF network formation.
about
Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assemblyA dysfunctional desmin mutation in a patient with severe generalized myopathyThe product of the ataxia-telangiectasia group D complementing gene, ATDC, interacts with a protein kinase C substrate and inhibitorMaking a connection: direct binding between keratin intermediate filaments and desmosomal proteinsOrder and disorder in intermediate filament proteinsVimentin filaments support extension of tubulin-based microtentacles in detached breast tumor cells.Identifying the role of specific motifs in the lens fiber cell specific intermediate filament phakosin.The Alexander disease-causing glial fibrillary acidic protein mutant, R416W, accumulates into Rosenthal fibers by a pathway that involves filament aggregation and the association of alpha B-crystallin and HSP27The basal keratin network of stratified squamous epithelia: defining K15 function in the absence of K14.Directed expression of keratin 16 to the progenitor basal cells of transgenic mouse skin delays skin maturation.The rod domain of NF-L determines neurofilament architecture, whereas the end domains specify filament assembly and network formationElectron paramagnetic resonance analysis of the vimentin tail domain reveals points of order in a largely disordered region and conformational adaptation upon filament assemblyGlial fibrillary acidic protein filaments can tolerate the incorporation of assembly-compromised GFAP-delta, but with consequences for filament organization and alphaB-crystallin association.Identification of phosphorylation-induced changes in vimentin intermediate filaments by site-directed spin labeling and electron paramagnetic resonance.Intermediate filament protein domain interactions as revealed by two-hybrid screens.The type I keratin 19 possesses distinct and context-dependent assembly properties.Determinants for intracellular sorting of cytoplasmic and nuclear intermediate filaments.Phosphorylation of vimentin head domain inhibits interaction with the carboxyl-terminal end of alpha-helical rod domain studied by surface plasmon resonance measurements.
P2860
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P2860
The roles of the rod end and the tail in vimentin IF assembly and IF network formation.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
The roles of the rod end and the tail in vimentin IF assembly and IF network formation.
@ast
The roles of the rod end and the tail in vimentin IF assembly and IF network formation.
@en
type
label
The roles of the rod end and the tail in vimentin IF assembly and IF network formation.
@ast
The roles of the rod end and the tail in vimentin IF assembly and IF network formation.
@en
prefLabel
The roles of the rod end and the tail in vimentin IF assembly and IF network formation.
@ast
The roles of the rod end and the tail in vimentin IF assembly and IF network formation.
@en
P2093
P2860
P356
P1476
The roles of the rod end and the tail in vimentin IF assembly and IF network formation.
@en
P2093
P2860
P304
P356
10.1083/JCB.122.2.395
P407
P577
1993-07-01T00:00:00Z