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ProteomicsiPRG 2012: A Study on Detecting Modified Peptides in a Complex Mixture
This is the data and results associated with the 2012 study organized by the proteome informatics research group of the Association of Biomolecular Resource Facilities, which investigated participants' ability to identify a range of post-translationally modified peptides spiked into a yeast lysate b...
ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932) 
2013-11-19 | MSV000078492 | MassIVE
ProteomicsBDNF BONLAC in HEK cells
In-depth Quantitative Proteomic Analysis of De Novo Protein Synthesis Induced by Brain-derived Neurotrophic Factor
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2014-08-26 | MSV000078831 | MassIVE
ProteomicsA pipeline that integrates the discovery and verification of plasma protein biomarkers reveals candidate markers for cardiovascular disease
Addona TA, Shi X, Keshishian H, Mani DR, Burgess M, Gillette MA, Clauser KR, Shen D, Lewis GD, Farrell LA, Fifer MA, Sabatine MS, Gerszten RE, Carr SA. Nat Biotechnol. 2011, 29(7):635-43. doi: 10.1038/nbt.1899. PMCID:PMC3366591. Discovery, AIMS, and MRM datasets Discovery_Tranche_hash: b/quYtp/Q8fY...
2013-12-19 | MSV000078513 | MassIVE
UnknownExtracellular phosphorylation of a receptor tyrosine kinase controls synaptic localization of NMDA receptors and regulates pathological pain.
Not available
S-EPMC5515392 | biostudies-literature
ProteomicsChanges in the strength of protein-protein interactions portend oncogenic activity and generate actionable targets for cancer
Stresses associated with disease may pathologically remodel the cellular proteins by increasing the interaction strength between chaperome members, and between the chaperome and the proteins it regulates. How these changes in protein-protein interaction strength are executed remains unknown. Our stu...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-05-22 | MSV000085459 | MassIVE
UnknownVLK drives extracellular phosphorylation of EphB2 to govern the EphB2-NMDAR interaction and injury-induced pain.
Not available
S-EPMC10983893 | biostudies-literature
ProteomicsIPRG2015
IPRG-2015 Study -Differential Abundance Analysis in Label-Free Quantitative Proteomics. This study of LC-MS/MS data analysis focuses on data processing and statistical assessment for relative protein-level quantification in label-free proteomics.
ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932) 
2016-06-20 | MSV000079843 | MassIVE
ProteomicsDesign, Implementation and Multisite Evaluation of a System Suitability Protocol for the Quantitative Assessment of Instrument Performance in Liquid Chromatography-Multiple Reaction Monitoring-MS (LC-MRM-MS)
Multiple reaction monitoring (MRM) mass spectrometry coupled with stable isotope dilution (SID) and liquid chromatography (LC) is increasingly used in biological and clinical studies for precise and reproducible quantification of peptides and proteins in complex sample matrices. Robust LC-SID-MRM-MS...
ORGANISM(S): Bos Taurus 
PXD010535 | panorama
UnknownGroup A streptococcal disease in paediatric inpatients: a European perspective.
Not available
S-EPMC9709363 | biostudies-literature
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