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Proteomicsyeast-UPS1 standard LC-MS/MS dataset
Proteomic workflows based on nanoLC-MS/MS data-dependent-acquisition analysis have progressed tremendously in recent years due to the technical improvement of mass spectrometers, and now allow to extensively characterize complex protein mixtures. High-resolution and fast sequencing instruments have ...
ORGANISM(S): Homo sapiens (Human) Saccharomyces cerevisiae (Baker's yeast) 
2015-12-01 | PXD001819 | Pride
Yesat Ups1 Label-free quantification Lc-ms/ms 
ProteomicsArabidopsis thaliana spiked UPS1 standard protein mixtures
This project aims at providing a quantitative dataset from LC-MS/MS injections of a calibrated UPS1 mixture spiked in an Arabidopsis thaliana background.
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) Homo sapiens (Human) 
2022-07-31 | PXD027800 | Pride
Arabidopsis thaliana Ups Hf-x 
UnknownMolecular mechanism of mitochondrial phosphatidate transfer by Ups1.
Not available
S-EPMC7447767 | biostudies-literature
ProteomicsUPS1 and UPS2 TMT Benchmarking Experiment
This experiment is a TMT10plex labelled experiment containing trypsin digested UPS1 and UPS2 human proteins in replicate along with E.Coli lysates. The mass spectra were generated in a single MS2-based experiment, using TMT10plex-labelled samples made up of UPS1, UPS2, and E.Coli lysate. UPS1 (Unive...
ORGANISM(S): Homo sapiens (Human) Escherichia coli 
2026-05-15 | PXD070151 | Pride
Human Ms/ms Ups E.coli 
UnknownStructural basis of intramitochondrial phosphatidic acid transport mediated by Ups1-Mdm35 complex.
Not available
S-EPMC4515121 | biostudies-literature
UnknownStructural and mechanistic insights into phospholipid transfer by Ups1-Mdm35 in mitochondria.
Not available
S-EPMC4532887 | biostudies-literature
UnknownCooperative function of Fmp30, Mdm31, and Mdm32 in Ups1-independent cardiolipin accumulation in the yeast Saccharomyces cerevisiae.
Not available
S-EPMC5703896 | biostudies-literature
ProteomicsStandard dataset of UPS1 spiked into yeast at various concentrations
A standard proteolytic digest of a human protein mixture, prepared at 1.5-fold to 3-fold protein concentration changes, and diluted into a constant background of yeast proteins. Similar to other datasets used for ground truth in quantitative studies, with the exception of being more granular, and mu...
ORGANISM(S): Homo sapiens (Human) Saccharomyces cerevisiae (Baker's yeast) 
2018-09-24 | PXD006447 | Pride
Dilution series Yeast Standard Ups1 
ProteomicsUPS1-yeast standard analysis - Technical Brief Calibration Plot for Proteomics (CP4P): A graphical tool to visually check the assumptions underlying FDR control in quantitative experiments
Label-free quantification of various concentrations of Universal Proteomic Standard (UPS1, Sigma-Aldrich) spiked in yeast extract.
ORGANISM(S): Homo sapiens (Human) Saccharomyces cerevisiae (Baker's yeast) 
2015-11-27 | PXD002370 | Pride
Proteomic standard Label-free Nanolc-ms/ms 
ProteomicsUPS1 and UPS2 proteins diluted in E. coli
This dataset derives from experiments testing quantitation using label-free methods. We used the Sigma-Aldrich UPS1 and UPS2 protein standard sets, containing proteins of 6-83 kD; the UPS1 set includes 49 human proteins at a single molar concentration, while the UPS2 set includes six groups of eight...
ORGANISM(S): Escherichia coli 
2013-12-05 | PXD000602 | Pride
Ups2 Standards E. coli Ups1 
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