MassIVE MSV000095249

Partial Public PXD053644

Phenotypic screening against P. falciparum under physiologically relevant nutrients levels reveals novel chemical diversity and highlights the importance of the PSAC channel for parasite survival.

Description

Microenvironment mapping was used to identify the binding targets of two small molecules in Plasmodium Falciparum cells. In the method, small molecule - photocatalyst conjugates sensitize biotinylation of proteins binding the small molecules, which were reduced, alkylated with iodoacetamide, and immunoprecipitated using streptavidin beads. Labeling was subject to offcompete using a large excess of the free small molecule. On-bead tryptic digestion yielded peptides, which were subjected to DDA-PASEF MS measurement using a timsTOF Pro 2. CLAG3 was significantly enriched by labeling by both molecules. [doi:10.25345/C51J97K65] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Proteomics, microenvironment mapping, target identification, TIMSTOF

Contact

Principal Investigators:
(in alphabetical order)
Jacob Geri, Weill Cornell Medicine, United States
Submitting User: jacobgeri
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Experimental Design
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Identification Results
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Quantification Results
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Originally identified proteins that were automatically remapped by MassIVE to proteins in the SwissProt human reference database.

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Number of distinct peptide sequences (including modified variants or peptidoforms) reported across all analyses (original submission and reanalyses) associated with this dataset.

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Total number of peptide-spectrum matches (i.e. spectrum identifications) reported across all analyses (original submission and reanalyses) associated with this dataset.

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Number of distinct proteins quantified across all analyses (original submission and reanalyses) associated with this dataset.

Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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Number of distinct proteins found to be differentially abundant in at least one comparison across all analyses (original submission and reanalyses) associated with this dataset.

A protein is differentially abundant if its change in abundance across conditions is found to be statistically significant with an adjusted p-value <= 0.05 and lists no issues associated with statistical tests for differential abundance.

Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

"N/A" means no results of this type were submitted.
This dataset may not contain all raw spectra data as originally deposited in PRIDE. It has been imported to MassIVE for reanalysis purposes, so its spectra data here may consist solely of processed peak lists suitable for reanalysis with most software.