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ProteomicsSynthetic (Phospho)Peptide Library
The submitted dataset contains raw files from 96 synthetic peptide libraries, using either HCD or ETD as fragmentation technique. The synthesized 96 tryptic peptide libraries containing >100,000 unmodified peptides plus their corresponding >100,000 phosphorylated counterparts with precisely known s...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-04-14 | MSV000091718 | MassIVE
ProteomicsNovel antibody-peptide binding assay indicates presence of immunoglobulins against EGFR phospho-site S1166 in high-grade glioma.
The project’s aim was to develop and test the applicability of a method to determine the presence of serum immunoglobulins against specific autoantibodies. The method combined immunoglobulin G enrichment (using Melon Gel), molecular weight filtration, and targeted mass spectrometry and the feasibili...
ORGANISM(S): Bos taurus (Bovine) Homo sapiens (Human) 
2022-06-09 | PXD032844 | Pride
Glioblastoma Melon gel Peptide antigen Autoantibodies Immunoglobulin g 
ProteomicsSynthetic (Phospho)Peptide Library
The submitted dataset contains raw files from 96 synthetic peptide libraries, using either HCD or ETD as fragmentation technique. The synthesized 96 tryptic peptide libraries containing >100,000 unmodified peptides plus their corresponding >100,000 phosphorylated counterparts with precisely known s...
ORGANISM(S): Homo sapiens (Human) 
2013-05-05 | PXD000138 | Pride
Synthetic library Hcd Etd 
TranscriptomicsMOTS-c: A Novel Peptide Encoded by a Short Mitochondrial Open Reading Frame Regulates Metabolic Homeostasis
Mitochondria are known to be functional organelles, but their role as a signaling unit is increasingly being appreciated. The recent identification of a short open reading frame (sORF) in the mitochondrial DNA (mtDNA) that encodes a signaling peptide, humanin, suggests the possible existence of addi...
ORGANISM(S): Homo sapiens 
2015-03-07 | E-GEOD-65068 | biostudies-arrayexpress
ProteomicsEnhanced Access to the Human Phosphoproteome with Genetically Encoded Phosphothreonine
Protein phosphorylation is a ubiquitous post-translational modification that governs signaling cascades and protein-protein interactions. Orthogonal translation systems repurpose evolutionarily divergent aminoacyl-tRNA synthetase and tRNA pairs for the co-translational insertion of a modified amino ...
ORGANISM(S): Homo sapiens (Human) 
2022-11-11 | PXD037724 | Pride
Synthetic biology Phosphorylation Phosphoprotein Peptide library 
ProteomicsChemical phosphoproteomic approaches reveal substrate specificity of phosphoprotein phosphatases-1 and -2
The phosphatases PP1 and PP2A are responsible for the majority of dephosphorylation reactions on phosphoserine (pSer) and –threonine (pThr), and are involved in basically all cellular processes and many related diseases. They are thought to have no appreciable intrinsic substrate specificity, but ...
ORGANISM(S): Homo sapiens (Human) 
2020-07-14 | PXD013775 | Pride
Phospho peptide library Pp2a Pp1 
UnknownNovel Antibody-Peptide Binding Assay Indicates Presence of Immunoglobulins against EGFR Phospho-Site S1166 in High-Grade Glioma.
Not available
S-EPMC9100080 | biostudies-literature
ProteomicsSpatial-proteomics reveals phospho-signaling dynamics at subcellular resolution
Dynamic change in subcellular localization of signaling proteins is a general concept that eukaryotic cells evolved for responding and elicit a coordinated response to stimuli. Mass spectrometry (MS)-based proteomics in combination with subcellular fractionation can provide comprehensive maps of spa...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2021-11-18 | PXD023690 | Pride
Dia Spatio-temporal dynamics Proteomics Phosphoproteomics 
ProteomicsYeast Phospho QTL (resubmission)
Rachel Brem's QTL yeast strain collection (BY4716 x S288C cross) profiled by full lysate and phospho-enrichment proteomic analysis
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-05-10 | PXD010893 | Pride
Dia Swath Qtl Phosphoproteomics Quantitative trait loci Yeast 
TranscriptomicsiCLIP Analysis of WT, phospho-defective, and phospho-mimicking mutants of mouse Nucleolin in iKras PDAC cells
This experiment aimed to identify Nucleolin (Ncl) binding sites on a transcriptome-wide scale, by performing iCLIP in mouse iKras PDAC cells (Ying et al., 2012) transiently transfected with a mammalian expression construct encoding a wild-type (WT) myc-Ncl, a phospho-defective mutant in which S28, S...
ORGANISM(S): Mus musculus 
2023-03-01 | E-MTAB-12481 | biostudies-arrayexpress
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