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

Proliferation of intrahyphal hyphae caused by disruption of csmA, which encodes a class V chitin synthase with a myosin motor-like domain in Aspergillus nidulans.

Journal of bacteriology - 1 Jun 1999

Horiuchi H, Fujiwara M, Yamashita S, Ohta A, Takagi M

Abstract excerpt

We have found that the Aspergillus nidulans csmA gene encodes a novel protein which consists of an N-terminal myosin motor-like domain and a C-terminal chitin synthase domain (M. Fujiwara, H. Horiuchi, A. Ohta, and M. Takagi, Biochem. Biophys. Res. Commun. 236:75-78, 1997). To clarify the roles of csmA in fungal morphogenesis, we constructed csmA null mutants. The growth rate of the mutant colonies was almost the...

Read the complete abstract on PubMed

Topics

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

Share to Aspergillus niger
Share to Chitin Synthase

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

Share to Genotype

Share to Microscopy, Electron, Scanning

Share to Myosins

Share to Plasmids

Share to Restriction Mapping

Source

Open in PubMed Open full text

Identifiers

PMID: 10368147
DOI: 10.1128/JB.181.12.3721-3729.1999
PMCID: PMC93850

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

Proliferation of intrahyphal hyphae caused by disruption of csmA, which encodes a class V chitin synthase with a myosin motor-like domain in Aspergillus nidulans.PMID 10368147Read ↗

Aspergillus nidulans class V and VI chitin synthases CsmA and CsmB, each with a myosin motor-like domain, perform compensatory functions that are essential for hyphal tip growth.Semantic proximity Read ↗

Myosin motor-like domain of the class VI chitin synthase CsmB is essential to its functions in Aspergillus nidulans.Semantic proximity Read ↗

CsmA, a class V chitin synthase with a myosin motor-like domain, is localized through direct interaction with the actin cytoskeleton in Aspergillus nidulans.Semantic proximity Read ↗

Chitin synthases with a myosin motor-like domain control the resistance of Aspergillus fumigatus to echinocandins.Semantic proximity Read ↗

Different functions of the class I and class II chitin synthase genes, chsC and chsA, are revealed by repression of chsB expression in Aspergillus nidulans.Semantic proximity Read ↗

Transportation of Aspergillus nidulans Class III and V Chitin Synthases to the Hyphal Tips Depends on Conventional Kinesin.Semantic proximity Read ↗

Class III chitin synthase ChsB of Aspergillus nidulans localizes at the sites of polarized cell wall synthesis and is required for conidial development.Semantic proximity Read ↗

MpkA-Dependent and -independent cell wall integrity signaling in Aspergillus nidulans.Semantic proximity Read ↗

Functional differentiation of chitin synthases in Yarrowia lipolytica.Semantic proximity Read ↗

Evidence that the Aspergillus nidulans class I and class II chitin synthase genes, chsC and chsA, share critical roles in hyphal wall integrity and conidiophore development.Semantic proximity Read ↗

The Aspergillus nidulans pkcA gene is involved in polarized growth, morphogenesis and maintenance of cell wall integrity.Semantic proximity Read ↗

The myosin motor domain of fungal chitin synthase V is dispensable for vesicle motility but required for virulence of the maize pathogen Ustilago maydis.Semantic proximity Read ↗

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