Processive cytoskeletal motors studied with single-molecule fluorescence techniques. - Test2 - elhamkhani - TriplyDB

Processive cytoskeletal motors studied with single-molecule fluorescence techniques.

Processive cytoskeletal motors studied with single-molecule fluorescence techniques.

http://www.wikidata.org/entity/Q38216570

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Collective dynamics of processive cytoskeletal motors Biophysical methods for the characterization of PTEN/lipid bilayer interactions Energy utilization in fluctuating biological energy converters Super-resolution imaging for monitoring cytoskeleton dynamics.Assessing heterogeneity in oligomeric AAA+ machines.Analyzing kinesin motor domain translocation in cultured hippocampal neurons.Breaking the Concentration Barrier for Single-Molecule Fluorescence Measurements.Measurement of Force-Dependent Release Rates of Cytoskeletal Motors.Combining Structure-Function and Single-Molecule Studies on Cytoplasmic Dynein.Use of Single Molecule Fluorescence Polarization Microscopy to Study Protein Conformation and Dynamics of Kinesin-Microtubule Complexes.

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P2860

Processive cytoskeletal motors studied with single-molecule fluorescence techniques.

http://www.wikidata.org/entity/Q38216570

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article científic

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article scientifique

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articol științific

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articolo scientifico

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artigo científico

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artigo científico

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artikel ilmiah

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artikull shkencor

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artículo científico

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Processive cytoskeletal motors studied with single-molecule fluorescence techniques.

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type

label

Processive cytoskeletal motors studied with single-molecule fluorescence techniques.

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Processive cytoskeletal motors studied with single-molecule fluorescence techniques.

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J.FEBSLET.2014.05.040

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Processive cytoskeletal motors studied with single-molecule fluorescence techniques

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Ahmet Yildiz

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P2860

Myosin VI is a processive motor with a large step size

Single-molecule analysis of dynein processivity and stepping behavior

An oxygen scavenging system for improvement of dye stability in single-molecule fluorescence experiments

The Structure of the Kinesin-1 Motor-Tail Complex Reveals the Mechanism of Autoinhibition

She1-mediated inhibition of dynein motility along astral microtubules promotes polarized spindle movements

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

Subnanometre single-molecule localization, registration and distance measurements

Myosin V: regulation by calcium, calmodulin, and the tail domain

Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization

Precise nanometer localization analysis for individual fluorescent probes

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3520-3525

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scholarly article

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10.1016/J.FEBSLET.2014.05.040

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Vladislav Belyy

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262780486

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