Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

An extended microtubule-binding structure within the dynein motor domain.

Nature - 11 Dec 1997

Gee M A, Heuser J E, Vallee R B

Abstract excerpt

Flagellar dynein was discovered over 30 years ago as the first motor protein capable of generating force along microtubules. A cytoplasmic form of dynein has also been identified which is involved in mitosis and a wide range of other intracellular movements. Rapid progress has been made on understanding the mechanism of force production by kinesins and myosins. In contrast, progress in understanding the dyneins...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding Sites
Share to Cloning, Molecular
Share to COS Cells

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Dyneins

Share to Microtubules

Share to Mutation

Share to Recombinant Proteins

Source

Identifiers

PMID: 9403697
DOI: 10.1038/37663

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

An extended microtubule-binding structure within the dynein motor domain.PMID 9403697Read ↗

Interaction mapping of a dynein heavy chain. Identification of dimerization and intermediate-chain binding domains.Semantic proximity Read ↗

Cryo-EM Reveals the Mechanochemical Cycle of Reactive Full-length Human Dynein-1Semantic proximity Read ↗

Trypanosome doublet microtubule structures reveal flagellum assembly and motility mechanismsSemantic proximity Read ↗

Backbone and side-chain ¹H, ¹⁵N, and ¹³C resonance assignments of the microtubule-binding domain of yeast cytoplasmic dynein in the high and low-affinity states.Semantic proximity Read ↗

Motor proteins 1: kinesins.Semantic proximity Read ↗

The myosin superfamily at a glanceSemantic proximity Read ↗

Kinesin motors as molecular machines.Semantic proximity Read ↗

Modular aspects of kinesin force generation machinery.Semantic proximity Read ↗

Overexpression of cytoplasmic dynein's globular head causes a collapse of the interphase microtubule network in Dictyostelium.Semantic proximity Read ↗

A force-sensitive mutation reveals a non-canonical role for dynein in anaphase progression.Semantic proximity Read ↗

Regulatory ATPase sites of cytoplasmic dynein affect processivity and force generation.Semantic proximity Read ↗

Structural basis for two-way communication between dynein and microtubules.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.