Sort   by:  
 Page size 
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 
UnknownPhosphatidylserine transport by Ups2-Mdm35 in respiration-active mitochondria.
Not available
S-EPMC4932372 | biostudies-literature
UnknownMICOS and phospholipid transfer by Ups2-Mdm35 organize membrane lipid synthesis in mitochondria.
Not available
S-EPMC4896057 | biostudies-literature
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 
ProteomicsUPS2 Orbitrap data from Dicker, Lin and Ivanov (PMID: 20823122)
These raw data were first introduced in "Increased Power for the Analysis of Label-free LC-MS/MS Proteomics Data by Combining Spectral Counts and Peptide Peak Attributes" by Lee Dicker, Xihong Lin, and Alexander R. Ivanov (PubMed ID 20823122) (doi 10.1074/mcp.M110.002774). They represent the Sigma ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2014-01-10 | MSV000078520 | MassIVE
ProteomicsAbsolute quantification of cellular levels of photosynthesis-related proteins in Synechocystis sp. PCC 6803
We quantified proteins in the model cyanobacterium Synechocystis sp. PCC 6803 given the general importance of cyanobacteria for global photosynthesis, for synthetic biology and biotechnology research, and their ancestral relationship to the chloroplasts of plants. Four mass spectrometry methods wer...
ORGANISM(S): Synechocystis sp. PCC 6803 substr. GT-I 
2023-01-04 | PXD035632 | Pride
Assembly factor Photosystem Electron transport Mass spectrometry Photosynthesis Synechocystis Cyanobacteria Chlorophyll 
ProteomicsAbsolute quantification of proteins and histone modifications in Drosophila embryos reveals stoichiometric relationships in chromatin regulation
Gene transcription in eukaryotes is regulated through dynamic interactions of a variety of different proteins with DNA in the context of chromatin. Here, we used mass spectrometry for absolute quantification of the nuclear proteome during two stages of Drosophila embryogenesis. Before proteomics ana...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2023-02-01 | PXD015214 | Pride
Absolute proteome quantification/ histone modification quantification Prc2 H3k27 methylation Drosophila 
ProteomicsCritical assessment of proteome-wide label-free absolute abundance estimation strategies
There is a great interest in reliable ways to obtain absolute protein abundances at a proteome-wide scale. To this end, label-free LC-MS/MS quantification methods have been proposed where all identified proteins are assigned an estimated abundance. Several variants of this quantification approach ha...
ORGANISM(S): Mycoplasma pneumoniae Homo sapiens (Human) Drosophila melanogaster (Fruit fly) Leptospira interrogans 
2013-11-15 | PXD000331 | Pride
Ups2 
ProteomicsComparison of DIA and TMT based protein quantification in complex background
Label free quantification (LFQ) and isobaric labelling quantification (ILQ) are among the most popular protein quantification workflows in discovery proteomics. Here, we compared the TMT 10-plex workflow to label free single shot data-independent acquisition (DIA) method on a controlled sample set. ...
ORGANISM(S): Mus musculus (Mouse) 
2019-01-24 | PXD011691 | Pride
Tmt Orbitrap fusion lumos Dia 
ProteomicsS. cerevisiae DDA orbitrap-based benchmark datasets. C4PR_LIV
In this study, label free peptide intensities from a well quantitatively characterised yeast cell lysate were acquired on two orbitrap mass spectrometers (LTQ-Velos and Q Exactive HF). Additionally, samples containing Universal Proteomics Standard and the Proteomics Dynamic range Standard (http://ww...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2017-08-09 | PXD003472 | Pride
Peptide ionization Hydrophobicity Benchmark dataset Coelution Peptide detectability 
Sort   by:  
 Page size