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

BcNoxD, a putative ER protein, is a new component of the NADPH oxidase complex in Botrytis cinerea.

Molecular microbiology - 1 Mar 2015

Siegmund Ulrike, Marschall Robert, Tudzynski Paul

Abstract excerpt

NADPH oxidases (Nox) are major enzymatic producer of reactive oxygen species (ROS). In fungi these multi-enzyme complexes are involved in sexual differentiation and pathogenicity. However, in contrast to mammalian systems, the composition and recruitment of the fungal Nox complexes are unresolved. Here we introduce a new Nox component, the membrane protein NoxD in the grey mold fungus Botrytis cinerea. It has...

Read the complete abstract on PubMed

Topics

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

Share to Botrytis
Share to Endoplasmic Reticulum
Share to Gene Expression Regulation, Fungal

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hyphae

Share to Multienzyme Complexes

Share to NADPH Oxidases

Share to Reactive Oxygen Species

Share to Spores, Fungal

Source

Identifiers

PMID: 25402961
DOI: 10.1111/mmi.12869

Genes

CAT

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

BcNoxD, a putative ER protein, is a new component of the NADPH oxidase complex in Botrytis cinerea.PMID 25402961Read ↗

Comparative Proteomics Reveals the Potential Targets of BcNoxR, a Putative Regulatory Subunit of NADPH Oxidase of Botrytis cinerea.Semantic proximity Read ↗

Identification of NoxD/Pro41 as the homologue of the p22phox NADPH oxidase subunit in fungi.Semantic proximity Read ↗

NADPH oxidases are involved in differentiation and pathogenicity in Botrytis cinerea.Semantic proximity Read ↗

Conservation of fungal and animal nicotinamide adenine dinucleotide phosphate oxidase complexes.Semantic proximity Read ↗

Functions and regulation of the Nox family in the filamentous fungus Podospora anserina: a new role in cellulose degradation.Semantic proximity Read ↗

Yno1p/Aim14p, a NADPH-oxidase ortholog, controls extramitochondrial reactive oxygen species generation, apoptosis, and actin cable formation in yeast.Semantic proximity Read ↗

New insights into the roles of NADPH oxidases in sexual development and ascospore germination in Sordaria macrospora.Semantic proximity Read ↗

Molecular evolution of the reactive oxygen-generating NADPH oxidase (Nox/Duox) family of enzymesSemantic proximity Read ↗

A secreted Botrytis cinerea stage-specific effector promotes virulence by targeting the plant ROS-generating machinerySemantic proximity Read ↗

Aquaporin8 regulates cellular development and reactive oxygen species production, a critical component of virulence in Botrytis cinerea.Semantic proximity Read ↗

Multifunctional regulation of NADPH oxidase in growth, microsclerotia formation and virulence in Metarhizium rileyiSemantic proximity Read ↗

Nox Enzymes and New Thinking on Reactive Oxygen: A Double-Edged Sword RevisitedSemantic proximity Read ↗

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