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ProteomicsValidation of a novel shotgun proteomic workflow for the discovery of protein-protein interactions: focus on ZNF521
The study of protein-protein interactions is increasingly relying on mass spectrometry (MS). The classical approach of separating immunoprecipitated proteins by SDS-PAGE followed by in-gel digestion is long and labour-intensive. Besides, it is difficult to integrate it with most quantitative MS-base...
ORGANISM(S): Homo sapiens (Human) 
2015-04-07 | PXD001609 | Pride
Ap-ms  interactomics  18o labelling  znf521  znf423  spt16  spt5  nurd core complex  proteomics  mass spectrometry  shotgun proteomics 
UnknownPreparation of 18O-labelled azaspiracids for accurate quantitation using liquid chromatography-mass spectrometry.
Not available
S-EPMC10556123 | biostudies-literature
ProteomicsThe Quantitative Changes in the Yeast Hsp70 and Hsp90 Interactomes upon DNA Damage
The molecular chaperones Hsp70 and Hsp90 participate in many important cellular processes, including how cells respond to DNA damage. In this study, we applied quantitative affinity-purification mass spectrometry (AP-MS) proteomics to understand the protein network through which Hsp70 and Hsp90 exe...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2014-12-08 | PXD001284 | Pride
Saccharomyces cerevisiae 18o quantitation Ltq orbitrap xl Lc-ms/ms 
UnknownQuantitation of changes in protein phosphorylation: a simple method based on stable isotope labeling and mass spectrometry.
Not available
S-EPMC298695 | biostudies-literature
Proteomicsc-Abl Dependent Tyrosine Phosphorylation of theCo-chaperone Aha1 Regulates Interaction with Hsp90
The ability of Heat Shock Protein 90 (Hsp90) to hydrolyze ATP is essential for its chaperone function. The co-chaperone Aha1 stimulates Hsp90 ATPase activity tailoring the chaperone function to specific “client” proteins. The intracellular signaling mechanisms directly regulating Aha1 association wi...
ORGANISM(S): Homo sapiens (Human) 
2015-08-06 | PXD001737 | Pride
Molecular chaperone Q-exactive C-abl 18o labeling Aha1 Co-chaperone Heat shock protein 90 Quantative proteomics 
ProteomicsQuiXoT+ project: General Statistical framework for quantitative proteomics by stable isotope labeling
Protein identification was carried out by searching against a joint Human + Yeast Swissprot database (Uniprot release 57.3 May 2009, 26885 entries), in order to increase statistical power of peptide identification, which was supplemented with porcine trypsin, and using SEQUEST algorithm (Bioworks 3....
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-05-11 | PXD000325 | Pride
Yeast Stable isotope labeling Statistical analysis Quantitative proteomics 
UnknownEstablishing <sup>18</sup>O-Labeled Inositol Phosphates for Quantitative Capillary Electrophoresis-Mass Spectrometry: Fragmentation Pathways and Comparison with <sup>13</sup>C-Labeled Analogs.
Not available
S-EPMC12631729 | biostudies-literature
Unknown18O proteomics reveal increased human apolipoprotein CIII in Hispanic HIV-1+ women with HAART that use cocaine.
Not available
S-EPMC4977997 | biostudies-literature
ProteomicsMps1 Phosphorylation of the Molecular Chaperone Hsp90 Regulates Mitotic Checkpoint
SUMMARY Mps1 protein kinase is required for accurate chromosome segregation during the mitotic checkpoint. The molecular chaperone Heat Shock Protein 90 (Hsp90) has been linked to Mps1 activity, however the molecular mechanismsunderlying this regulatory process remain elusive. We report that Mps1 d...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2016-01-27 | PXD001969 | Pride
Mitotic checkpoint Molecular chaperones Heat shock protein 90 Mps1 Phosphatase Kinase Phosphorylation Cdc14 
UnknownSpatial mapping of protein abundances in the mouse brain by voxelation integrated with high-throughput liquid chromatography-mass spectrometry.
Not available
S-EPMC1800924 | biostudies-literature
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