Stu2p binds tubulin and undergoes an open-to-closed conformational change.
about
Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1Structural analysis of Bub3 interactions in the mitotic spindle checkpointLessons from in vitro reconstitution analyses of plant microtubule-associated proteinsThe fission yeast XMAP215 homolog Dis1p is involved in microtubule bundle organizationAlp7/TACC-Alp14/TOG generates long-lived, fast-growing MTs by an unconventional mechanism.A TOG: -tubulin Complex Structure Reveals Conformation-Based Mechanisms for a Microtubule PolymeraseThe XMAP215 family drives microtubule polymerization using a structurally diverse TOG arrayA tethered delivery mechanism explains the catalytic action of a microtubule polymeraseRoles for the conserved spc105p/kre28p complex in kinetochore-microtubule binding and the spindle assembly checkpoint.Regulation of microtubule dynamics by Bim1 and Bik1, the budding yeast members of the EB1 and CLIP-170 families of plus-end tracking proteins.Discrete states of a protein interaction network govern interphase and mitotic microtubule dynamicsAspergillus nidulans Dis1/XMAP215 protein AlpA localizes to spindle pole bodies and microtubule plus ends and contributes to growth directionality.XMAP215 is a processive microtubule polymerase.Structural mutants of the spindle pole body cause distinct alteration of cytoplasmic microtubules and nuclear dynamics in multinucleated hyphae.Fission yeast Alp14 is a dose-dependent plus end-tracking microtubule polymeraseOne-step purification of assembly-competent tubulin from diverse eukaryotic sources.A fluorescent reporter for mapping cellular protein-protein interactions in time and space.The structured core of human β tubulin confers isotype-specific polymerization properties.Detection of alpha-rod protein repeats using a neural network and application to huntingtin.A TOGL domain specifically targets yeast CLASP to kinetochores to stabilize kinetochore microtubules.Stu2, the budding yeast XMAP215/Dis1 homolog, promotes assembly of yeast microtubules by increasing growth rate and decreasing catastrophe frequencyThe contribution of αβ-tubulin curvature to microtubule dynamics.XMAP215 polymerase activity is built by combining multiple tubulin-binding TOG domains and a basic lattice-binding region.CLASP promotes microtubule rescue by recruiting tubulin dimers to the microtubule.The Chlamydia effector chlamydial outer protein N (CopN) sequesters tubulin and prevents microtubule assembly.Drosophila melanogaster mini spindles TOG3 utilizes unique structural elements to promote domain stability and maintain a TOG1- and TOG2-like tubulin-binding surfaceThe cyclin-dependent kinase Cdc28p regulates multiple aspects of Kar9p function in yeast.Katanin Severing and Binding Microtubules Are Inhibited by Tubulin Carboxy TailsMutations in Human Tubulin Proximal to the Kinesin-Binding Site Alter Dynamic Instability at Microtubule Plus- and Minus-Ends.XMAP215: a tip tracker that really moves.The composition, functions, and regulation of the budding yeast kinetochoreCentriole inheritanceGated entry into the ciliary compartment.Regulation of microtubule dynamics by TOG-domain proteins XMAP215/Dis1 and CLASP.Kinetochores generate microtubules with distal plus ends: their roles and limited lifetime in mitosisAn unconventional interaction between Dis1/TOG and Mal3/EB1 in fission yeast promotes the fidelity of chromosome segregation.Kinetochore-dependent microtubule rescue ensures their efficient and sustained interactions in early mitosis.Spc24 and Stu2 promote spindle integrity when DNA replication is stalled.A TOG Protein Confers Tension Sensitivity to Kinetochore-Microtubule Attachments.Assembling the protein architecture of the budding yeast kinetochore-microtubule attachment using FRET.
P2860
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P2860
Stu2p binds tubulin and undergoes an open-to-closed conformational change.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Stu2p binds tubulin and undergoes an open-to-closed conformational change.
@ast
Stu2p binds tubulin and undergoes an open-to-closed conformational change.
@en
type
label
Stu2p binds tubulin and undergoes an open-to-closed conformational change.
@ast
Stu2p binds tubulin and undergoes an open-to-closed conformational change.
@en
prefLabel
Stu2p binds tubulin and undergoes an open-to-closed conformational change.
@ast
Stu2p binds tubulin and undergoes an open-to-closed conformational change.
@en
P2093
P2860
P356
P1476
Stu2p binds tubulin and undergoes an open-to-closed conformational change.
@en
P2093
Anthony Hyman
Jawdat Al-Bassam
Mark van Breugel
Stephen C Harrison
P2860
P304
P356
10.1083/JCB.200511010
P407
P577
2006-03-01T00:00:00Z