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

The connection of protein O-mannosyltransferase family to the biocontrol potential of Beauveria bassiana, a fungal entomopathogen.

Glycobiology - 1 Jul 2014

Wang Juan-Juan, Qiu Lei, Chu Zhen-Jian, Ying Sheng-Hua, Feng Ming-Guang

Abstract excerpt

O-Mannosylation dependent on the protein O-mannosyltransferase (Pmt) family is an essential post-translational modification process in eukaryotes, but their connection to the biocontrol potential of a filamentous entomopathogen against arthropod pests is not understood. Here, we characterized the functions of three Pmt orthologues (Pmt1, Pmt2 and Pmt4) in the Pmt family of Beauveria bassiana and found that they...

Read the complete abstract on PubMed

Topics

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

Share to Antifungal Agents
Share to Beauveria
Share to Cell Wall

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

Share to Fungal Proteins

Share to Mannosyltransferases

Share to Oxidants

Share to Spores, Fungal

Source

Identifiers

PMID: 24727441
DOI: 10.1093/glycob/cwu028

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

The connection of protein O-mannosyltransferase family to the biocontrol potential of Beauveria bassiana, a fungal entomopathogen.PMID 24727441Read ↗

The C-terminal MIR-containing region in the Pmt1 O-mannosyltransferase restrains sporulation and is dispensable for virulence in Beauveria bassiana.Semantic proximity Read ↗

The histone acetyltransferase Mst2 sustains the biological control potential of a fungal insect pathogen through transcriptional regulation.Semantic proximity Read ↗

Genetical and O-glycoproteomic analyses reveal the roles of three protein O-mannosyltransferases in phytopathogen Fusarium oxysporum f.sp. cucumerinum.Semantic proximity Read ↗

Global Insight into Lysine Acetylation Events and Their Links to Biological Aspects in Beauveria bassiana, a Fungal Insect Pathogen.Semantic proximity Read ↗

Primary roles of two dehydrogenases in the mannitol metabolism and multi-stress tolerance of entomopathogenic fungus Beauveria bassiana.Semantic proximity Read ↗

Glc8, a regulator of protein phosphatase type 1, mediates oxidation tolerance, asexual development and virulence in Beauveria bassiana, a filamentous entomopathogenic fungus.Semantic proximity Read ↗

The Pmt2p-Mediated Protein O-Mannosylation Is Required for Morphogenesis, Adhesive Properties, Cell Wall Integrity and Full Virulence of Magnaporthe oryzaeSemantic proximity Read ↗

Members of protein O-mannosyltransferase family in Aspergillus fumigatus differentially affect growth, morphogenesis and viability.Semantic proximity Read ↗

A p53-like transcription factor, BbTFO1, contributes to virulence and oxidative and thermal stress tolerances in the insect pathogenic fungus, Beauveria bassiana.Semantic proximity Read ↗

Pleiotropic roles of O-mannosyltransferase MoPmt4 in development and pathogenicity of Magnaporthe oryzaeSemantic proximity Read ↗

Differentiated functions of Ras1 and Ras2 proteins in regulating the germination, growth, conidiation, multi-stress tolerance and virulence of Beauveria bassiana.Semantic proximity Read ↗

Botrytis cinerea protein O-mannosyltransferases play critical roles in morphogenesis, growth, and virulence.Semantic proximity Read ↗

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