Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

ORNL Filamentous Fungal Lipidomics

ABSTRACT: Investigation of the lipidomes of filamentous fungi

INSTRUMENT(S): LTQ Orbitrap Velos Pro

ORGANISM(S): Aspergillus Fumigatus (ncbitaxon:746128)

SUBMITTER: Dr. Robert Hettich

PROVIDER: MSV000096650 | MassIVE | Thu Dec 12 11:54:00 GMT 2024

REPOSITORIES: MassIVE

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

GNPS - ORNL Filamentous Fungal Lipidomics

Project description:Investigation of the lipidomes of filamentous fungi

2024-12-12 | MSV000096650 | GNPS

Identification of fungal secreted proteins

Project description:The project aims to identify proteins secreted by filamentous fungi.

2020-07-19 | PXD020432 |

fungal sp.

Project description:Comapartive genomics of ambrosia fungi

| PRJNA1084195 | ENA

A broadly conserved fungal alcohol oxidase (AOX) facilitates fungal invasion of plants

Project description:Alcohol oxidases are ecologically important enzymes which facilitate a number of plant-fungal interactions. Within Ascomycota they are primarily associated with methylotrophy, as a peroxisomal alcohol oxidase (AOX) catalyzing the conversion of methanol to formaldehyde in methylotrophic yeast. In this study we demonstrate that AOX orthologs are phylogenetically conserved proteins which are common in the genomes of non-methylotrophic, plant-associating fungi. Additionally, AOX orthologs are highly expressed during infection in a range of diverse pathosystems. To study the role of AOX in plant colonization, AOX knockout mutants were generated in the broad host range pathogen Sclerotinia sclerotiorum. Disease assays in soybean showed that these mutants had a significant virulence defect as evidenced by markedly reduced stem lesions and mortality rates. Chemical genomics suggest that SsAOX may function as an aromatic alcohol oxidase, and growth assays demonstrate that ΔSsAOX is incapable of properly utilizing plant extract as a nutrient source. Profiling of known aromatic alcohols point towards the monolignol coniferyl alcohol (CoA) as a possible substrate for SsAOX. As CoA and other monolignols are ubiquitous among land plants, the presence of highly conserved AOX orthologs throughout Ascomycota imply that this is a broadly conserved protein used by ascomycete fungi during plant colonization.

2022-12-02 | GSE212269 | GEO

Transcription profiling of Physcomitrella patens response to fungal exudates

Project description:Physcomitrella patens gametophores were treated with exudates from the arbuscular mycorrhiza fungi (AMF) Rhizophagus irregularis (formerly known as Glomus intraradices) and Gigaspora margerita for one hour and 24 hours.

2014-11-10 | E-MTAB-3081 | biostudies-arrayexpress

fungal sp.

Project description:VMGC: fungi cultured from human vagina

| PRJNA1100704 | ENA

Melanization of fungal necromass drives the upregulation of multiple chitinase, protease, and laccase genes when being degraded by Trichoderma reesei

Project description:Fungal necromass in soil represents the stable carbon pools. While fungi are known to decompose fungal necromass, how fungi decomopose melanin, remains poorly understood. Recently, Trichoderma species was found to be one of the most commonly associated fungi in soil, we have used a relevant fungal species, Trichoderma reesei, to characterized Genes involved in the decomposition of melanized and non-melanized necromass from Hyaloscypha bicolor.

2024-05-01 | GSE263516 | GEO

Presence of fungal infection in brains of patients with Parkinsons disease (PD)

Project description:Isolation of fungi in infected neural tissues in patients with Parkinson's disease. Here we used next generation sequencing of Internal Transcribed Spacer (ITS) regions, by PCR amplicons (NGS ITS amplicon analysis).

| EGAS00001003644 | EGA

Structural characterisation of the fungal Pmt4 homodimer - native MS and lipidomics

Project description:Protein O-mannosyltransferases (PMTs) are conserved endoplasmic reticulum membrane embedded enzymes responsible for the transfer of mannose from dolichol phosphate-mannose (Dol-P-Man) to serine/threonine-rich protein substrates or unfolded proteins. PMTs from three subfamilies form obligate dimers with different substrate specificities, and require the concerted action of their transmembrane domains (TMDs) and a luminal MIR domain for catalysis. Here, we present structures, native mass spectrometry and structure-based mutagenesis of the Chaetomium thermophilum and Saccharomyces cerevisiae Pmt4 homodimers. The core fold of the TMDs and MIR domain is conserved with the Pmt1-Pmt2 heterodimer, indicating a shared catalytic mechanism. Distinct to Pmt4, the MIR domain interacts in cis with the TMDs of the same subunit and has a beta-hairpin insertion required for O-mannosylation of substrates. We further identify a cytosolic binding site for substrate Dol33 P-Man within the Pmt4 TMDs, which is conserved amongst PMTs and important for in vivo activity. Thus, we provide a framework to understand the substrate specificity and regulation of the Pmt4 homodimer.

2025-11-19 | PXD061837 | Pride

Arbuscular mycorrhizal fungal communities

Project description:Dispersal of arbuscular mycorrhizal fungi

| PRJNA783165 | ENA