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

Novel role of cytoplasmic dynein motor in maintenance of the nuclear number in conidia through organized conidiation in Aspergillus oryzae.

Biochemical and biophysical research communications - 8 Aug 2003

Maruyama Jun-ichi, Nakajima Harushi, Kitamoto Katsuhiko

Abstract excerpt

Cytoplasmic dynein is a minus-end-directed, microtubule-dependent motor protein complex. DhcA, cytoplasmic dynein heavy chain in Aspergillus oryzae, contained four P-loops involved in ATP binding which were conserved as in cytoplasmic dynein heavy chains of other organisms. The amino acid sequence of A. oryzae DhcA was similar to cytoplasmic dynein heavy chains from other organisms except for the N-terminus of...

Read the complete abstract on PubMed

Topics

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

Share to Aspergillus oryzae
Share to Cell Nucleus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cloning, Molecular

Share to Dyneins

Share to Molecular Motor Proteins

Share to Mutation

Source

Identifiers

PMID: 12878196
DOI: 10.1016/s0006-291x(03)01267-1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Novel role of cytoplasmic dynein motor in maintenance of the nuclear number in conidia through organized conidiation in Aspergillus oryzae.PMID 12878196Read ↗

Role of fungal dynein in hyphal growth, microtubule organization, spindle pole body motility and nuclear migration.Semantic proximity Read ↗

Dynein light intermediate chain in Aspergillus nidulans is essential for the interaction between heavy and intermediate chains.Semantic proximity Read ↗

Characterization and localization of the cytoplasmic dynein heavy chain in Aspergillus nidulans.Semantic proximity Read ↗

A split motor domain in a cytoplasmic dynein.Semantic proximity Read ↗

Cytoplasmic dynein and actin-related protein Arp1 are required for normal nuclear distribution in filamentous fungi.Semantic proximity Read ↗

Deletion of the dynein heavy-chain gene DYN1 leads to aberrant nuclear positioning and defective hyphal development in Candida albicans.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 ↗

The "8-kD" cytoplasmic dynein light chain is required for nuclear migration and for dynein heavy chain localization in Aspergillus nidulans.Semantic proximity Read ↗

Calcium signaling is involved in dynein-dependent microtubule organization.Semantic proximity Read ↗

Genetic evidence for a microtubule-destabilizing effect of conventional kinesin and analysis of its consequences for the control of nuclear distribution in Aspergillus nidulans.Semantic proximity Read ↗

Role of Unc104/KIF1-related motor proteins in mitochondrial transport in Neurospora crassa.Semantic proximity Read ↗

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