Load-induced enhancement of Dynein force production by LIS1-NudE in vivo and in vitro - Wikidata - thesis-toulmin - TriplyDB

Load-induced enhancement of Dynein force production by LIS1-NudE in vivo and in vitro

Load-induced enhancement of Dynein force production by LIS1-NudE in vivo and in vitro

http://www.wikidata.org/entity/Q27334950

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Local synthesis of dynein cofactors matches retrograde transport to acutely changing demands Single Molecule Investigation of Kinesin-1 Motility Using Engineered Microtubule Defects.Regulation of dynein-dynactin-driven vesicular transport.Lipid droplet functions beyond energy storage.Differential effects of the dynein-regulatory factor Lissencephaly-1 on processive dynein-dynactin motility.Dynein: Let's not get stuck!Lissencephaly-1 is a context-dependent regulator of the human dynein complex.Combinatorial regulation of the balance between dynein microtubule end accumulation and initiation of directed motility.Lis1 Has Two Opposing Modes of Regulating Cytoplasmic Dynein.Heterogeneity in kinesin function.Nuclear movement in fungi.Mechanical coupling of microtubule-dependent motor teams during peroxisome transport in Drosophila S2 cells.A posttranslational modification of the mitotic kinesin Eg5 that enhances its mechanochemical coupling and alters its mitotic function.Effect of fuel concentration and force on collective transport by a team of dynein motors.

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Load-induced enhancement of Dynein force production by LIS1-NudE in vivo and in vitro

http://www.wikidata.org/entity/Q27334950

description

2016 nî lūn-bûn

@nan

2016 թուականին հրատարակուած գիտական յօդուած

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2016 թվականին հրատարակված գիտական հոդված

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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name

Load-induced enhancement of Dynein force production by LIS1-NudE in vivo and in vitro

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Load-induced enhancement of Dynein force production by LIS1-NudE in vivo and in vitro

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Load-induced enhancement of Dynein force production by LIS1-NudE in vivo and in vitro

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type

label

Load-induced enhancement of Dynein force production by LIS1-NudE in vivo and in vitro

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Load-induced enhancement of Dynein force production by LIS1-NudE in vivo and in vitro

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Load-induced enhancement of Dynein force production by LIS1-NudE in vivo and in vitro

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Load-induced enhancement of Dynein force production by LIS1-NudE in vivo and in vitro

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Load-induced enhancement of Dynein force production by LIS1-NudE in vivo and in vitro

@en

Load-induced enhancement of Dynein force production by LIS1-NudE in vivo and in vitro

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Nature Communications

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Load-induced enhancement of Dynein force production by LIS1-NudE in vivo and in vitro

@en

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Babu J N Reddy

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

Caitlin L Wynne

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

Dail Chapman

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

Michelle Mattson

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

Omid Vadpey

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

Richard B Vallee

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

Steven P Gross

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

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A role for the lissencephaly gene LIS1 in mitosis and cytoplasmic dynein function

Cooperative cargo transport by several molecular motors.

Lis1 acts as a "clutch" between the ATPase and microtubule-binding domains of the dynein motor.

Dynactin increases the processivity of the cytoplasmic dynein motor

BICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment to cellular structures.

Dual subcellular roles for LIS1 and dynein in radial neuronal migration in live brain tissue

Dynamic and regulated association of caveolin with lipid bodies: modulation of lipid body motility and function by a dominant negative mutant

Mitotic spindle regulation by Nde1 controls cerebral cortical size

Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution

The N-terminal coiled-coil of Ndel1 is a regulated scaffold that recruits LIS1 to dynein.

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12259

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scholarly article

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4135056

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10.1038/NCOMMS12259

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7

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2016-08-04T00:00:00Z

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1038348295

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27489054

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4976208

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