Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Exploring the effect of citronellol on Candida albicans using proteomics appraoch

ABSTRACT: To explore the proteome profiles of Candida albicans exposed to citronellol. We used label-free proteomics approach.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Candida Albicans (yeast)

SUBMITTER: Sucheewin Krobthong

LAB HEAD: Sucheewin Krobthong

PROVIDER: PXD030379 | Pride | 2022-05-04

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	yeast.mzData	Other
	yeast.mzML	Mzml
	yeast.mzid.gz	Mzid

Items per page:

1 - 3 of 3

Similar Datasets

Atmospheric and Room Temperature Plasma (ARTP) Mutagenesis Improved the Anti-MRSA Activity of Brevibacillus sp. SPR20

Project description:Brevibacillus sp. SPR20 produced potentially antibacterial substances against MRSA. The synthe-sis of these substances is controlled by their biosynthetic gene clusters. Several mutagenesis methods are used to overcome the restriction of gene regulations when genetic information is ab-sent. Atmospheric and room temperature plasma (ARTP) is a powerful technique to make random mutagenesis for microbial strain improvement. This study utilized an argon-based ARTP to conduct the mutations on SPR20. The positive mutants of 40% occurred. The M27 mutant exhib-ited an increase in anti-MRSA activity when compared to the wild-type, by which the MIC values were 250500 and 500 g/mL, respectively. M27 had genetic stability because it exhibited con-stant activity throughout 15 generations. This mutant had similar morphology and antibiotic susceptibility to the wild-type. Comparative proteomic analysis identified some specific proteins that were upregulated in M27. These proteins were involved in the metabolism of amino acids, cell structure and movement, and catalytic enzymes. These might result in the enhancement of the anti-MRSA activity of the ARTP-treated SPR20 mutant. This study supports the ARTP technology to increase the production of valuable antibacterial agents.

2023-08-31 | PXD043954 | Pride

Utilizing of quantitative proteomics to identify species-specific protein therapeutic target for treatment of leishmaniasis.

Project description:Identification of common Leishmania antigen proteins is important for practical purposes ranging from diagnostic to the development of a vaccine for the prevention of leishmaniasis. Moreover, we need to establish the potential drug targets that interrupt the replication and transmission of the pathogen to promote drug discovery. Therefore, the objective of this work was to provide the public proteome database which would be useful for the establishment of novel protein antigenicity for therapeutic purposes. This information would introduce the alternative protein targets for Leishmaniasis, allowing the development of therapeutic strategies for the disease.

2022-05-20 | PXD026304 | Pride

Serum proteomics analysis of CCA

Project description:Differential plasma proteomes of the patients with Opisthorchiasis viverrini and cholangiocarcinoma identifies polymeric immunoglobulin receptor as potential biomarker

2023-03-10 | PXD028152 | Pride

LC-MSMS of media agar from co-cultivation of Auricularia cornea and Pseudonocardia mangrovi

Project description:The co-cultivation investigation showed that A. cornea TBRC 12900 co-cultivated with P. mangrovi TBRC-BCC 42794 showed a high level of A. cornea mycelial growth. Proteomics analysis was employed to reveal predicted biological activities involved in the mutualistic relationship between the two strains during mycelial growth.

2022-10-27 | PXD035814 | Pride

TMT-10plex-based phosphoproteomics of bioactive compounds in A549 cells

Project description:We conducted a comprehensive screening of bioactive compounds sourced from natural products, specifically targeting those capable of inducing apoptosis while inhibiting tyrosine kinase activity. Our investigation encompassed a diverse range of compounds, including pure compounds, compound mixtures, and peptides, all evaluated within the A549 cell line. To delve into the underlying molecular mechanisms, we employed phosphoproteomics analysis, which enabled us to comprehensively assess the impact of these bioactive compounds on cellular pathways. Through labeling digested proteins with distinct isobaric tags, we meticulously examined the cellular response to each compound. In our experimental design, we included two established chemical drugs, Afatinib and Osimertinib, serving as positive controls. These drugs, both kinase inhibitors utilized in cancer treatment, operate via distinct mechanisms and target different kinases. By comparing the effects of our test compounds with these controls, we aimed to elucidate their potential therapeutic relevance and mechanisms of action. Among the compounds examined were extracts from Phallus indusiatus and Fomes rimosus (Berk.) Cooke, as well as specific compounds like Chamuangone, Cannabigerol (CBG), Cannabidiol (CBD), and NP1-cyclic peptide

2024-03-13 | PXD050555 | Pride

Proteomics analysis of octapeptide from Lingzhi mushroom with anti-tyrosinase and anti-oxidative activity

Project description:Study the effect of novel octapeptide isolated from Lingzhi mushroom on skin melanocyte cell (Mus Musculus) by gel-free based proteomics

2022-08-11 | PXD017234 | Pride

The effect of cannabinoid receptor agonists on triple-negative breast cancer cell line (MDA-MB-231)

Project description:The endocannabinoid system (ECS) provides regulatory functions in several cellular and physiological processes. It has also been found to play a role in control of cancer development. Our group found that breast cancer cells responded to cannabinoid receptor (CB) agonist treatments. This leads the activation of CB receptors in breast cancer, which inhibited their growth. In addition, breast cancer cells also behaved differentially when they were exposed to combinations of both CB1 and CB2 agonists. The underlying mechanism of individual- or co- activation after CB agonist exposure is still unknown. Hence, we studied the impact of CB activation on cancer molecular signature by performing proteomic analysis after triple-negative breast cancer (MDA-MB-231) cells exposed to CB receptor agonists. In this study, ACEA and GW405833 were used as CB1 and CB2 receptor agonists, respectively.

2024-07-27 | PXD040666 | Pride

Proteomics identification for toxicological pathways screening: A partial difference between low concentration ionic and nanoparticulate silver

Project description:LC-MS/MS based proteomics coupled with online bioinformatics platform was under evaluation for the better understanding of toxicological pathways induced by silver nanoparticle (AgNP), and to distinguish the difference of such pathways induced by ionic silver. This approach was appraised using AgNP as a model to develop a platform technology for toxicological screening of nanoparticles (NPs), which is currently incorporated into various consumer products. Proteomic study was conducted by exposing human carcinoma cell line to AgNP or AgNO3 for 48 hours at low cytotoxic concentration (LC10). The comparison of proteins expressed in each treatment group was performed using One-way ANOVA (p < 0.05). Proteins with more than 4-fold differentially-expressed were subjected to functional pathway analysis by STITCH. Principal component analysis (PCA) showed the significant variation of proteins identified in each treatment group. Most identified proteins were functioned in cellular process. SOTA clustering indicated the similarity of protein expression between AgNP and control group. We established the resemblance of proteins in cell cycle pathway affected by both Ag substances. While the difference in toxicological pathways from AgNO3 were involved in cellular organization and regulation of metabolic process of macromolecule, and nucleic acid metabolic process were altered by AgNP. The present study supported the practicability of LC-MS/MS based proteomics coupled with STITCH bioinformatics platform, for the identification of toxicological pathways from ionic and AgNP, which were discovered to be partially different. We appraised this platform technology to be promising and powerful for toxicological screening of other new substances.

2020-08-18 | PXD012793 | Pride

Proteomic profiling of oleamide-mediated polarization in a primary human monocyte-derived tumor-associated macrophages model: a functional analysis

Project description:To investigate the effect of oleamide on tumor-associated macrophages (TAMs) polarization.

2024-08-25 | PXD043461 | Pride

Assay for characterizing adsorption-properties of surfaces (APS)

Project description:Analytes, from sample preparation, until entering an analytical instrument, are prone to adsorb to surfaces, driven by the chemical properties of the surface and the liquids they are dissolved in. This problem can be addressed with internal standards when a single or few known analytes are quantified that are usually not available in omics. However, minimal to no loss of analytes is the aim. Here, we present a novel assay for qualifying and quantifying interactions responsible for adsorption of molecules to surfaces (APS) by using LC-MS/MS-based differential quantitative analysis. To reflect a broad range of chemical interactions with surfaces, a reference mixture of thousands of tryptic peptides, with known compositions was selected, representing a variety of different chemical characteristics. The assay was tested by investigating the adsorption properties of several different vials with different surface chemistries. A significant number of hydrophobic peptides adsorbed to conventional polypropylene vials. In contrast, only few peptides adsorbed to polypropylene vials, assigned as low-protein-binding. The highest number of peptides adsorbed to glass vials driven by electrostatic interactions. In summary, the new assay is suitable to characterize adsorption properties of different surfaces and to approximate the loss of analytes during sample preparation.

2024-08-30 | PXD044268 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data