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ProteomicsClassical virulence factors do not define Cryptococcus pathogenic diversity
Pathogenic determinants in the Cryptococcus genus have been extensively studied, often using standard laboratory isolates. Here, we analyzed the virulence of ten Cryptococcus isolates from diverse sources, species, and genotypes. These isolates exhibited marked differences in their ability to coloni...
ORGANISM(S): Cryptococcus gattii VGII R265 Cryptococcus neoformans var. neoformans JEC21 
2025-10-20 | PXD065863 | Pride
Diversity Virulence Pathogenic Cryptococcus 
ProteomicsOuter membrane proteome of Leptospira; revealing the bottom of iceberg
Leptospira, the causative agent of leptospirosis is known to have several proteases with potential to degrade extracellular matrix. However, a multipronged approach to identify, classify, characterize and elucidate their role has not been attempted. In this study, we carried out in-depth proteomic a...
ORGANISM(S): Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130 
2020-09-01 | PXD016204 | Pride
Pathogenic high resolution proteomics Protease Pathogenesis Outer membrane Leptospira 
ProteomicsProteogenomic analysis of Mycobacterium smegmatis using high resolution mass spectrometry
Biochemical evidence is vital for accurate genome annotation. The integration of experimental data collected at the proteome level using high resolution mass spectrometry allows for improvements in genome annotation by providing evidence for novel gene models, while validating or modifying others. ...
ORGANISM(S): Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) 
2016-03-31 | PXD003500 | Pride
Mass spectrometry Genome annotation Mycobacterium smegmatis Proteogenomics Proteomics 
ProteomicsF1Fo-ATP synthase subunit determines lethal infection in pathogenic fungi
Fungal infections, especially for candidiasis and aspergillosis, claim an unacceptably high fatality. However, the determining mechanism that promote fungal lethal infections are still elusive. The energy ATP necessary for fungal cell growth and function is synthesized mainly through oxidative phosp...
ORGANISM(S): Candida albicans (Yeast) 
2021-09-16 | PXD024729 | Pride
subunit lethal infection pathogenic fungi 
UnknownHigh resolution proteomics of Aedes aegypti salivary glands infected with either dengue, Zika or chikungunya viruses identify new virus specific and broad antiviral factors.
Not available
S-EPMC8654903 | biostudies-literature
ProteomicsProteomic approach and expression analysis revealed the differential expression of leptospiral proteases capable of ECM degradation
Leptospira, the causative agent of leptospirosis is known to have several proteases with potential to degrade extracellular matrix. However, a multipronged approach to identify, classify, characterize and elucidate their role has not been attempted. In this study, we carried out in-depth proteomic a...
ORGANISM(S): Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130 
2018-04-18 | PXD009050 | Pride
High resolution proteomics Protease Pathogenesis Leptospira Metalloprotease 
UnknownProteogenomic analysis of pathogenic yeast Cryptococcus neoformans using high resolution mass spectrometry.
Not available
S-EPMC3915034 | biostudies-literature
UnknownUniversal Identification of Pathogenic Viruses by Liquid Chromatography Coupled with Tandem Mass Spectrometry Proteotyping.
Not available
S-EPMC11795680 | biostudies-literature
ProteomicsProfiling of Bacillus thuringiensis biopesticides: A high-resolution LC-MS/MS approach for subspecies identification and protein quantification
The widespread use of Bacillus thuringiensis (Bt)- based biopesticides in organic farming presents challenges for food diagnostics due to the genetic similarity between Bt and the pathogenic Bacillus cereus as well as the lack of data on the insecticidal protein concentrations in treated food sample...
ORGANISM(S): Bacillus Thuringiensis Serovar Kurstaki Bacillus Thuringiensis Bacillus Thuringiensis Serovar Aizawai Bacillus Thuringiensis Serovar Israelensis 
2026-08-27 | PXD071216 | panorama
ProteomicsThe acetylome analysis of lysine acetylation in the plant pathogenic bacterium Brenneria nigrifluens
Protein lysine acetylation, a dynamic and reversible posttranslational modification, plays a crucial role in several cellular processes including cell cycle regulation, metabolic pathways, enzymatic activities and protein interactions. Brenneria nigrifluens is the pathogen of shallow bark canker of ...
ORGANISM(S): Brenneria nigrifluens Bacteria 
2019-09-30 | PXD014046 | Pride
Brenneria nigrifluens Lc-msms Plant pathogen 
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