Walking on two heads: the many talents of kinesin (Q34286401)

1 August 2017

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title

Walking on two heads: the many talents of kinesin (English)

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1 August 2017

G Woehlke

1

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PubMed ID

11413489

1 August 2017

M Schliwa

series ordinal

2

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1 August 2017

1 October 2000

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Nature Reviews Molecular Cell Biology

1 August 2017

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1 August 2017

1

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1 August 2017

1

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1 August 2017

50-58

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https://scigraph.springernature.com/pub.10.1038/35036069

1 August 2017

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Nucleotide specificities of anterograde and retrograde organelle transport in Reticulomyxa are indistinguishable

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Direct observation of kinesin stepping by optical trapping interferometry

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Movement of microtubules by single kinesin molecules

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One-headed kinesin derivatives move by a nonprocessive, low-duty ratio mechanism unlike that of two-headed kinesin

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Processivity of the motor protein kinesin requires two heads

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Failure of a single-headed kinesin to track parallel to microtubule protofilaments

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Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis

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Interacting head mechanism of microtubule-kinesin ATPase

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Alternating site mechanism of the kinesin ATPase.

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A structural change in the kinesin motor protein that drives motility

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Moving a microtubule may require two heads: a kinetic investigation of monomeric Ncd

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Mechanism of the single-headed processivity: diffusional anchoring between the K-loop of kinesin and the C terminus of tubulin.

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Processive movement of single 22S dynein molecules occurs only at low ATP concentrations

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Inner-arm dynein c of Chlamydomonas flagella is a single-headed processive motor

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Microtubules and microtubule motors: mechanisms of regulation.

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Kinesin light chains are essential for axonal transport in Drosophila

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Immunochemical analysis of kinesin light chain function

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Kinesin interactions with membrane bounded organelles in vivo and in vitro

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Light chain-dependent regulation of Kinesin's interaction with microtubules

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Phosphorylation of neuronal kinesin heavy and light chains in vivo

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A specific light chain of kinesin associates with mitochondria in cultured cells

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The molecular structure of adrenal medulla kinesin

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Formation of the compact confomer of kinesin requires a COOH-terminal heavy chain domain and inhibits microtubule-stimulated ATPase activity

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Kinesin's tail domain is an inhibitory regulator of the motor domain.

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Single-molecule analysis of kinesin motility reveals regulation by the cargo-binding tail domain

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Cargo binding and regulatory sites in the tail of fungal conventional kinesin

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Kinesin takes one 8-nm step for each ATP that it hydrolyzes.

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Kinesin's IAK tail domain inhibits initial microtubule-stimulated ADP release.

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7 January 2021

Functional anatomy of the kinesin molecule in vivo

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Bead movement by single kinesin molecules studied with optical tweezers

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Coupling of kinesin steps to ATP hydrolysis.

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Kinesin hydrolyses one ATP per 8-nm step

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Pathway of processive ATP hydrolysis by kinesin.

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7 January 2021

Force and velocity measured for single molecules of RNA polymerase.

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Basic mechanisms of transcript elongation and its regulation

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F1-ATPase: a rotary motor made of a single molecule

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The turn of the screw: the bacterial flagellar motor

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Torque-generating units of the flagellar motor of Escherichia coli have a high duty ratio

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7 January 2021

Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes

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7 January 2021

The Arp2/3 complex is essential for the actin-based motility of Listeria monocytogenes.

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7 January 2021

Actin-based motility of vaccinia virus mimics receptor tyrosine kinase signalling.

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7 January 2021

The case for a common ancestor: kinesin and myosin motor proteins and G proteins

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7 January 2021

Molecular motors: structural adaptations to cellular functions

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7 January 2021

The crystal structure of dimeric kinesin and implications for microtubule-dependent motility

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7 January 2021

Identifiers

DOI

10.1038/35036069

1 reference

PubMed ID

11413489

Dimensions Publication ID

1 August 2017

0 references

1 reference

PubMed ID

11413489