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ProteomicsYeast TRAPPIII complex cross-linking mass spectrometry
A comprehensive analysis of the structure and function of the yeast TRAPPIII complex
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-06-02 | PXD025172 | Pride
Trapp Cross-linking mass spectrometry 
ProteomicsProteome-wide Cross-linking mass spectrometry
Proteome-wide Cross-linking mass spectrometry on human k562 cell lysate
ORGANISM(S): Homo sapiens (Human) 
2020-01-09 | PXD013928 | Pride
Human 
ProteomicsProteome-wide cross-linking mass spectrometry of human K562 cells
Proteome-wide cross-linking mass spectrometry was performed on human K562 cell lysates. MS2-MS3 fragmentation strategy was used to aquire the XL-MS data. The raw files in this dataset are a subset of PXD013928.
ORGANISM(S): Homo sapiens (Human) 
2020-07-01 | PXD018771 | Pride
Human Protein-protein Cross-linking mass spectrometry Proteome-wide Interaction 
ProteomicsA comprehensive SARS-CoV-2-human protein-protein interactome network that can identify pathobiology and host-targeting therapies for COVID-19
Physical interactions between viral and host proteins are responsible for almost all aspects of the viral life cycle and the host’s immune response. Studying viral-host protein-protein interactions is thus crucial for identifying strategies for treatment and prevention of viral infection. Here, we u...
ORGANISM(S): Homo sapiens (Human) Severe acute respiratory syndrome coronavirus 2 
2023-03-11 | PXD035805 | Pride
Y2h Sars-cov-2 Tmt Human Ip-ms Virus pathobiology 
TranscriptomicsDivergence of Transcription Factor Binding Sites in Related Yeast Species
A fundamental problem in biology is the molecular basis for divergence among related organisms. We have investigated the level of divergence of transcription factor binding sites for two key factors that regulate developmental processes in the budding yeasts. The genomic binding locations for the St...
ORGANISM(S): Saccharomyces mikatae 
2007-09-06 | E-GEOD-5421 | biostudies-arrayexpress
ProteomicsMaximizing Confidence and Sensitivity in Phosphoproteomics reveals novel targets of DNA damage signling Kinases
Proteome-wide analysis of phosphorylation events is a challenging, yet essential, task for the comprehensive and unbiased investigation of kinase action. Here we developed a phosphoproteomic approach in which quantitation consistency among reversed isotopically labeled samples is used as a central f...
ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932) 
2020-01-24 | MSV000084839 | MassIVE
ProteomicsMaximizing Confidence and Sensitivity in quantitative Phosphoproteomics - Targets of Tel1 kinase
Proteome-wide analysis of phosphorylation events is a challenging, yet essential, task for the comprehensive and unbiased investigation of kinase action. Here we developed a phosphoproteomic approach in which quantitation consistency among reversed isotopically labeled samples is used as a central f...
ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932) 
2020-01-30 | MSV000084871 | MassIVE
ProteomicsMaximizing Confidence and Sensitivity in quantitative Phosphoproteomics
Proteome-wide analysis of phosphorylation events is a challenging, yet essential, task for the comprehensive and unbiased investigation of kinase action. Here we developed a phosphoproteomic approach in which quantitation consistency among reversed isotopically labeled samples is used as a central f...
ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932) 
2020-01-29 | MSV000084852 | MassIVE
ProteomicsMaximizing Confidence and Sensitivity in quantitative Phosphoproteomics - Targets of Mec1 kinase
Proteome-wide analysis of phosphorylation events is a challenging, yet essential, task for the comprehensive and unbiased investigation of kinase action. Here we developed a phosphoproteomic approach in which quantitation consistency among reversed isotopically labeled samples is used as a central f...
ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932) 
2020-01-30 | MSV000084875 | MassIVE
UnknownBMI matters: understanding the link between weight and severe psoriasis.
Not available
S-EPMC11961747 | biostudies-literature
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