Microtubule depolymerization promotes particle and chromosome movement in vitro. - Wikidata - awgldk - TriplyDB

Microtubule depolymerization promotes particle and chromosome movement in vitro.

Microtubule depolymerization promotes particle and chromosome movement in vitro.

http://www.wikidata.org/entity/Q30966793

about

CLASP1, astrin and Kif2b form a molecular switch that regulates kinetochore-microtubule dynamics to promote mitotic progression and fidelity Mitotic centromere-associated kinesin is important for anaphase chromosome segregation Opposing motor activities are required for the organization of the mammalian mitotic spindle pole Motile kinetochores and polar ejection forces dictate chromosome position on the vertebrate mitotic spindle Directional instability of kinetochore motility during chromosome congression and segregation in mitotic newt lung cells: a push-pull mechanism The kinesin-13 proteins Kif2a, Kif2b, and Kif2c/MCAK have distinct roles during mitosis in human cells.Review series: The functions and consequences of force at kinetochores Reconstituting the kinetochore–microtubule interface: what, why, and how The kinetochore-bound Ska1 complex tracks depolymerizing microtubules and binds to curved protofilaments.The kinesin-related proteins, Kip2p and Kip3p, function differently in nuclear migration in yeast.The yeast dynactin complex is involved in partitioning the mitotic spindle between mother and daughter cells during anaphase B.Novel roles for saccharomyces cerevisiae mitotic spindle motors.A Brief History of Research on Mitotic Mechanisms Chromosome congression is promoted by CENP-Q- and CENP-E-dependent pathways.Identification and partial characterization of mitotic centromere-associated kinesin, a kinesin-related protein that associates with centromeres during mitosis Force production by depolymerizing microtubules: a theoretical study Differential expression of a phosphoepitope at the kinetochores of moving chromosomes Direct physical study of kinetochore-microtubule interactions by reconstitution and interrogation with an optical force clamp.In search of an optimal ring to couple microtubule depolymerization to processive chromosome motions.Different assemblies of the DAM1 complex follow shortening microtubules by distinct mechanisms.The Dam1 ring binds microtubules strongly enough to be a processive as well as energy-efficient coupler for chromosome motion.Fast microtubule dynamics in meiotic spindles measured by single molecule imaging: evidence that the spindle environment does not stabilize microtubules.Tubulin depolymerization may be an ancient biological motor.Deformations within moving kinetochores reveal different sites of active and passive force generation.A spindle checkpoint functions during mitosis in the early Caenorhabditis elegans embryo Force production by disassembling microtubules.Microtubule motors in spindle and chromosome motility.Contrasting models for kinetochore microtubule attachment in mammalian cells The life and miracles of kinetochores.Force production by depolymerizing microtubules: load-velocity curves and run-pause statistics.Centromeres of human chromosomes.Simulating the role of microtubules in depolymerization-driven transport: a Monte Carlo approach.Force generation by microtubule assembly/disassembly in mitosis and related movements.A driving and coupling "Pac-Man" mechanism for chromosome poleward translocation in anaphase A.Mitosis futures: the past is prologue.Biophysics of mitosis The free energy for hydrolysis of a microtubule-bound nucleotide triphosphate is near zero: all of the free energy for hydrolysis is stored in the microtubule lattice.Antibodies to the kinesin motor domain and CENP-E inhibit microtubule depolymerization-dependent motion of chromosomes in vitro Chromokinesin: a DNA-binding, kinesin-like nuclear protein Membrane/microtubule tip attachment complexes (TACs) allow the assembly dynamics of plus ends to push and pull membranes into tubulovesicular networks in interphase Xenopus egg extracts.

P2860

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P2860

Microtubule depolymerization promotes particle and chromosome movement in vitro.

http://www.wikidata.org/entity/Q30966793

description

1991 nî lūn-bûn

@nan

1991 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

1991 թվականի մարտին հրատարակված գիտական հոդված

@hy

1991年の論文

@ja

1991年論文

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1991年論文

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1991年論文

@zh-hk

1991年論文

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1991年論文

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1991年论文

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name

Microtubule depolymerization promotes particle and chromosome movement in vitro.

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Microtubule depolymerization promotes particle and chromosome movement in vitro.

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type

label

Microtubule depolymerization promotes particle and chromosome movement in vitro.

@ast

Microtubule depolymerization promotes particle and chromosome movement in vitro.

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prefLabel

Microtubule depolymerization promotes particle and chromosome movement in vitro.

@ast

Microtubule depolymerization promotes particle and chromosome movement in vitro.

@en

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Journal of Cell Biology

P1476

Microtubule depolymerization promotes particle and chromosome movement in vitro.

@en

P2093

J R McIntosh

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

M Coue

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

V A Lombillo

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P2860

Spindle microtubules: thermodynamics of in vivo assembly and role in chromosome movement.

Pressure-induced depolymerization of spindle microtubules. I. Changes in birefringence and spindle length.

Temperature dependence of anaphase chromosome velocity and microtubule depolymerization

Measurements of the force produced by the mitotic spindle in anaphase.

Properties of the kinetochore in vitro. I. Microtubule nucleation and tubulin binding.

Oscillatory movements of monooriented chromosomes and their position relative to the spindle pole result from the ejection properties of the aster and half-spindle

On the mechanism of anaphase A: evidence that ATP is needed for microtubule disassembly and not generation of polewards force

Dynamic instability of individual microtubules analyzed by video light microscopy: rate constants and transition frequencies.

Characterization of the microtubule-activated ATPase of brain cytoplasmic dynein (MAP 1C)

The role of kinesin and other soluble factors in organelle movement along microtubules.

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1165-1175

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scholarly article

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10.1083/JCB.112.6.1165

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6

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112

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1991-03-01T00:00:00Z

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1999468

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2288901

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