Phosphoregulation and depolymerization-driven movement of the Dam1 complex do not require ring formation. - Wikidata - wikimedia - TriplyDB

Phosphoregulation and depolymerization-driven movement of the Dam1 complex do not require ring formation.

Phosphoregulation and depolymerization-driven movement of the Dam1 complex do not require ring formation.

http://www.wikidata.org/entity/Q30491892

about

Kinetochore-microtubule interactions: steps towards bi-orientation Reconstituting the kinetochore–microtubule interface: what, why, and how From equator to pole: splitting chromosomes in mitosis and meiosis The molecular architecture of the Dam1 kinetochore complex is defined by cross-linking based structural modelling.Structure of the Kinesin13-Microtubule Ring Complex The Dam1 complex confers microtubule plus end-tracking activity to the Ndc80 kinetochore complex.Cooperation of the Dam1 and Ndc80 kinetochore complexes enhances microtubule coupling and is regulated by aurora B.In-line separation by capillary electrophoresis prior to analysis by top-down mass spectrometry enables sensitive characterization of protein complexes Production and initial characterization of Dad1p, a component of the Dam1-DASH kinetochore complex Fluorescence applications in molecular neurobiology Direct physical study of kinetochore-microtubule interactions by reconstitution and interrogation with an optical force clamp.The Dam1 ring binds microtubules strongly enough to be a processive as well as energy-efficient coupler for chromosome motion.The Ndc80 kinetochore complex forms load-bearing attachments to dynamic microtubule tips via biased diffusion.Catalysis of the microtubule on-rate is the major parameter regulating the depolymerase activity of MCAK.A non-ring-like form of the Dam1 complex modulates microtubule dynamics in fission yeast Tubulin depolymerization may be an ancient biological motor.A tethering mechanism controls the processivity and kinetochore-microtubule plus-end enrichment of the kinesin-8 Kif18A.The Ndc80 kinetochore complex directly modulates microtubule dynamics.Long tethers provide high-force coupling of the Dam1 ring to shortening microtubules Kinetochore kinesin CENP-E is a processive bi-directional tracker of dynamic microtubule tips.Kinetochores require oligomerization of Dam1 complex to maintain microtubule attachments against tension and promote biorientation.Multisite phosphorylation of the NDC80 complex gradually tunes its microtubule-binding affinity.Data Analysis for Total Internal Reflection Fluorescence Microscopy.Correcting aberrant kinetochore microtubule attachments: an Aurora B-centric view.Catch and release: how do kinetochores hook the right microtubules during mitosis?Regulated targeting of protein phosphatase 1 to the outer kinetochore by KNL1 opposes Aurora B kinase.One-dimensional Brownian motion of charged nanoparticles along microtubules: a model system for weak binding interactions.Finding the middle ground: how kinetochores power chromosome congression.Contrasting models for kinetochore microtubule attachment in mammalian cells The life and miracles of kinetochores.Native capillary isoelectric focusing for the separation of protein complex isoforms and subcomplexes Aurora kinases and protein phosphatase 1 mediate chromosome congression through regulation of CENP-E.The MIS12 complex is a protein interaction hub for outer kinetochore assembly.Cryo-EM studies of microtubule structural intermediates and kinetochore-microtubule interactions.Force is a signal that cells cannot ignore.The Dam1 ring binds to the E-hook of tubulin and diffuses along the microtubule.Sensing centromere tension: Aurora B and the regulation of kinetochore function.Covalent immobilization of microtubules on glass surfaces for molecular motor force measurements and other single-molecule assays.Temperature-sensitive ipl1-2/Aurora B mutation is suppressed by mutations in TOR complex 1 via the Glc7/PP1 phosphatase Phosphoregulation promotes release of kinetochores from dynamic microtubules via multiple mechanisms

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P2860

Phosphoregulation and depolymerization-driven movement of the Dam1 complex do not require ring formation.

http://www.wikidata.org/entity/Q30491892

description

2008 nî lūn-bûn

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2008 թուականի Մարտին հրատարակուած գիտական յօդուած

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2008 թվականի մարտին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Phosphoregulation and depolyme ...... do not require ring formation.

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Phosphoregulation and depolyme ...... do not require ring formation.

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type

label

Phosphoregulation and depolyme ...... do not require ring formation.

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Phosphoregulation and depolyme ...... do not require ring formation.

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prefLabel

Phosphoregulation and depolyme ...... do not require ring formation.

@ast

Phosphoregulation and depolyme ...... do not require ring formation.

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P1433

Nature Cell Biology

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Phosphoregulation and depolyme ...... do not require ring formation.

@en

P2093

Alex Zelter

http://www.w3.org/2001/XMLSchema#string

Beth Graczyk

http://www.w3.org/2001/XMLSchema#string

Charles L Asbury

http://www.w3.org/2001/XMLSchema#string

Daniel R Gestaut

http://www.w3.org/2001/XMLSchema#string

Jeremy Cooper

http://www.w3.org/2001/XMLSchema#string

P2860

The conserved KMN network constitutes the core microtubule-binding site of the kinetochore

Implication of a novel multiprotein Dam1p complex in outer kinetochore function

Mps1 phosphorylation of Dam1 couples kinetochores to microtubule plus ends at metaphase.

Glc7/protein phosphatase 1 regulatory subunits can oppose the Ipl1/aurora protein kinase by redistributing Glc7.

Phospho-regulation of kinetochore-microtubule attachments by the Aurora kinase Ipl1p.

Molecular analysis of kinetochore-microtubule attachment in budding yeast.

The Ipl1-Aurora protein kinase activates the spindle checkpoint by creating unattached kinetochores.

Formation of a dynamic kinetochore- microtubule interface through assembly of the Dam1 ring complex.

The Dam1 kinetochore complex harnesses microtubule dynamics to produce force and movement.

Kinetochore protein interactions and their regulation by the Aurora kinase Ipl1p

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407-414

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scholarly article

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10.1038/NCB1702

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4

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10

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Trisha N. Davis

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2008-03-23T00:00:00Z

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5487134

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1009177814

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18364702

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2782782

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