Energy-filtered electron microscopy reveals that talin is a highly flexible protein composed of a series of globular domains.
about
Layilin, a novel talin-binding transmembrane protein homologous with C-type lectins, is localized in membrane rufflesStructural basis for amplifying vinculin activation by talinActivation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundleCentral Region of Talin Has a Unique Fold That Binds Vinculin and ActinRecreation of the terminal events in physiological integrin activation.Talin contains three similar vinculin-binding sites predicted to form an amphipathic helixDisruption of the talin gene arrests mouse development at the gastrulation stage.Talins and kindlins: partners in integrin-mediated adhesion.Studies on the morphology and spreading of human endothelial cells define key inter- and intramolecular interactions for talin1.A fluorescence cell biology approach to map the second integrin-binding site of talin to a 130-amino acid sequence within the rod domain.Podosome organization drives osteoclast-mediated bone resorption.The talin dimer structure orientation is mechanically regulated.New insights into vinculin function and regulation.Simple high-cell density fed-batch technique for high-level recombinant protein production with Pichia pastoris: Application to intracellular production of Hepatitis B surface antigenStructural studies on full-length talin1 reveal a compact auto-inhibited dimer: implications for talin activation.Structural and biophysical properties of the integrin-associated cytoskeletal protein talin.Mechanisms of talin-dependent integrin signaling and crosstalkTalin concentrates to the midbody region during mammalian cell cytokinesis.Disruption of the talin gene compromises focal adhesion assembly in undifferentiated but not differentiated embryonic stem cellsFurther characterization of the interaction between the cytoskeletal proteins talin and vinculin.The activity of the vinculin binding sites in talin is influenced by the stability of the helical bundles that make up the talin rod.Talin-null cells of Dictyostelium are strongly defective in adhesion to particle and substrate surfaces and slightly impaired in cytokinesis.Phosphatidylinositol phosphate kinase type 1gamma and beta1-integrin cytoplasmic domain bind to the same region in the talin FERM domain.
P2860
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P2860
Energy-filtered electron microscopy reveals that talin is a highly flexible protein composed of a series of globular domains.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
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1997年学术文章
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1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
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1997年學術文章
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1997年學術文章
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name
Energy-filtered electron micro ...... a series of globular domains.
@en
Energy-filtered electron micro ...... a series of globular domains.
@nl
type
label
Energy-filtered electron micro ...... a series of globular domains.
@en
Energy-filtered electron micro ...... a series of globular domains.
@nl
prefLabel
Energy-filtered electron micro ...... a series of globular domains.
@en
Energy-filtered electron micro ...... a series of globular domains.
@nl
P2093
P2860
P1433
P1476
Energy-filtered electron micro ...... a series of globular domains.
@en
P2093
B M Jockusch
H Lünsdorf
P2860
P304
P356
10.1111/J.1432-1033.1997.0430A.X
P407
P577
1997-01-01T00:00:00Z