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

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

Molecular biology of the cell - 1 Jun 1996

Koonce M P, Samsó M

Abstract excerpt

Cytoplasmic dynein is a minus-end directed microtubule-based motor. Using a molecular genetic approach, we have begun to dissect structure-function relationships of dynein in the cellular slime mold Dictyostelium. Expression of a carboxy-terminal 380-kDa fragment of the heavy chain produces a protein that approximates the size and shape of the globular, mechanochemical head of dynein. This polypeptide cosediments...

Read the complete abstract on PubMed

Topics

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

Share to Cytoplasm
Share to Cytoskeleton
Share to Dictyostelium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Microscopy, Electron

Share to Microtubules

Share to Molecular Structure

Share to Phenotype

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 8816999
DOI: 10.1091/mbc.7.6.935
PMCID: PMC275944

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Overexpression of cytoplasmic dynein's globular head causes a collapse of the interphase microtubule network in Dictyostelium.PMID 8816999Read ↗

Dynein motor regulation stabilizes interphase microtubule arrays and determines centrosome position.Semantic proximity Read ↗

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

Dynein intermediate chain mediated dynein-dynactin interaction is required for interphase microtubule organization and centrosome replication and separation in Dictyostelium.Semantic proximity Read ↗

In vitro microtubule-based organelle transport in wild-type Dictyostelium and cells overexpressing a truncated dynein heavy chain.Semantic proximity Read ↗

An extended microtubule-binding structure within the dynein motor domain.Semantic proximity Read ↗

Regulated offloading of cytoplasmic dynein from microtubule plus ends to the cortex.Semantic proximity Read ↗

Molecular genetic truncation analysis of filament assembly and phosphorylation domains of Dictyostelium myosin heavy chain.Semantic proximity Read ↗

Structure and function of the cytoskeleton of a Dictyostelium myosin-defective mutant.Semantic proximity Read ↗

Dynein is regulated by the stability of its microtubule track.Semantic proximity Read ↗

Analyses of dynein heavy chain mutations reveal complex interactions between dynein motor domains and cellular dynein functions.Semantic proximity Read ↗

Identification of a novel site in the tail of dynein heavy chain important for dynein function in vivo.Semantic proximity Read ↗

Dynein pulls microtubules without rotating its stalk.Semantic proximity Read ↗

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