Assembly of amino-terminally deleted desmin in vimentin-free cells.
about
A human keratin 14 "knockout": the absence of K14 leads to severe epidermolysis bullosa simplex and a function for an intermediate filament proteinA dysfunctional desmin mutation in a patient with severe generalized myopathyGenetic mutations in the K1 and K10 genes of patients with epidermolytic hyperkeratosis. Correlation between location and disease severityDual color photoactivation localization microscopy of cardiomyopathy-associated desmin mutantsIdentification of novel principles of keratin filament network turnover in living cellsSteady state dynamics of intermediate filament networks.Molecular characteristics of the novel intermediate filament protein paranemin. Sequence reveals EAP-300 and IFAPa-400 are highly homologous to paranemin.Desmin aggregate formation by R120G alphaB-crystallin is caused by altered filament interactions and is dependent upon network status in cellsSite-directed spin labeling and electron paramagnetic resonance determination of vimentin head domain structure.Deletions in epidermal keratins leading to alterations in filament organization in vivo and in intermediate filament assembly in vitroDynamics of keratin assembly: exogenous type I keratin rapidly associates with type II keratin in vivo.Neurofilaments are obligate heteropolymers in vivo.The roles of K5 and K14 head, tail, and R/K L L E G E domains in keratin filament assembly in vitro.The rod domain of NF-L determines neurofilament architecture, whereas the end domains specify filament assembly and network formationA novel peripherin isoform generated by alternative translation is required for normal filament network formation.De novo formation of cytokeratin filament networks originates from the cell cortex in A-431 cells.Dynamics of intermediate filaments. Recent progress and unanswered questions.Intermediate filaments: regulation of gene expression and assembly.Regulation of vimentin expression in cultured epithelial cells.Desmin/vimentin intermediate filaments are dispensable for many aspects of myogenesis.The domain organization of the bacterial intermediate filament-like protein crescentin is important for assembly and function.A synthetic peptide representing the consensus sequence motif at the carboxy-terminal end of the rod domain inhibits intermediate filament assembly and disassembles preformed filaments.Truncation of recombinant vimentin by ompT. Identification of a short motif in the head domain necessary for assembly of type III intermediate filament proteins.Nuclear A-type lamins are differentially expressed in human lung cancer subtypesIntermediate filaments formed de novo from tail-less cytokeratins in the cytoplasm and in the nucleus.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
Assembly of amino-terminally deleted desmin in vimentin-free cells.
description
1990 nî lūn-bûn
@nan
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
1990年论文
@zh
1990年论文
@zh-cn
name
Assembly of amino-terminally deleted desmin in vimentin-free cells.
@en
type
label
Assembly of amino-terminally deleted desmin in vimentin-free cells.
@en
prefLabel
Assembly of amino-terminally deleted desmin in vimentin-free cells.
@en
P2093
P2860
P356
P1476
Assembly of amino-terminally deleted desmin in vimentin-free cells.
@en
P2093
Bloemendal H
Ramaekers FC
Verrijp KN
Vree Egberts WT
P2860
P304
P356
10.1083/JCB.111.5.1971
P407
P433
P577
1990-11-01T00:00:00Z