Identification of Ncd tail domain-binding sites on the tubulin dimer.
about
Probing interactions between CLIP-170, EB1, and microtubules.Microtubule-associated protein-like binding of the kinesin-1 tail to microtubules.Kinesin's light chains inhibit the head- and microtubule-binding activity of its tail.Importin alpha/beta and Ran-GTP regulate XCTK2 microtubule binding through a bipartite nuclear localization signal.Developmentally Regulated GTP binding protein 1 (DRG1) controls microtubule dynamics.The C-terminal tails of heterotrimeric kinesin-2 motor subunits directly bind to α-tubulin1: Possible implications for cilia-specific tubulin entry.Kinesin-14 is Important for Chromosome Segregation During Mitosis and Meiosis in the Ciliate Tetrahymena thermophila.
P2860
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P2860
Identification of Ncd tail domain-binding sites on the tubulin dimer.
description
2003 nî lūn-bûn
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2003年の論文
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2003年学术文章
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2003年学术文章
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2003年学术文章
@zh-cn
2003年学术文章
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2003年学术文章
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2003年学术文章
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2003年學術文章
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2003年學術文章
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name
Identification of Ncd tail domain-binding sites on the tubulin dimer.
@en
Identification of Ncd tail domain-binding sites on the tubulin dimer.
@nl
type
label
Identification of Ncd tail domain-binding sites on the tubulin dimer.
@en
Identification of Ncd tail domain-binding sites on the tubulin dimer.
@nl
prefLabel
Identification of Ncd tail domain-binding sites on the tubulin dimer.
@en
Identification of Ncd tail domain-binding sites on the tubulin dimer.
@nl
P1476
Identification of Ncd tail domain-binding sites on the tubulin dimer.
@en
P2093
P304
P356
10.1016/S0006-291X(03)00827-1
P407
P577
2003-06-01T00:00:00Z