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ProteomicsEasy, robust, and reproducible online acid cleavage of proteins in mobile phase for fast quantitative LC-MS bottom-up proteomics – application for ricin detection
The data were recorded during the development, optimization, and characterization of a method for fast online acid cleavage of proteins directly in the mobile phase.
ORGANISM(S): Ricinus communis Homo sapiens (Human) 
2023-10-24 | PXD041124 | Pride
Bottom-up proteomics  lc-ms  online protein cleavage  acid hydrolysis  aspartic acid  ricin  artifacts 
ProteomicsOnline-2D nanoLC-MS for crude serum proteome profiling: assessing sample preparation impact on proteome composition
Although current LC-MS technology permits scientists to efficiently screen clinical samples in translational research, e.g. steroids, biogenic amines and even plasma or serum proteomes, in a daily routine, maintaining the balance between throughput and analytical depth is still a limiting factor. A ...
ORGANISM(S): Homo sapiens (Human) 
2021-07-09 | PXD024893 | Pride
Peptide fractionation Blood Nanolc-ms 1d nanolc-ms Proteome profiling Crude serum High-resolution accurate mass-spectrometry Online-2d nanolc-ms 
ProteomicsIdentification C3 cleavage sites by alpha-Thrombin
Identification C3 cleavage sites by alpha-Thrombin. Goal of the experiment is the validation of predicted cleavage sites by HTPS
ORGANISM(S): Homo sapiens (Human) 
2021-02-04 | PXD022971 | Pride
Htps Cleavages identification 
UnknownEasy, Robust, and Repeatable Online Acid Cleavage of Proteins in Mobile Phase for Fast Quantitative LC-MS Bottom-Up Protein Analysis─Application for Ricin Detection.
Not available
S-EPMC10448442 | biostudies-literature
ProteomicsActive Site Specificity Profiling of the Matrix Metalloproteinase Family: Proteomic Identification of 4,300 Cleavage Sites by MMPs 1, 2, 3, 7, 8, 9, 12, 13, and 14.
Background: The active site of matrix metalloproteinases (MMPs) is highly conserved, complicating the rational design of specific substrates and inhibitors for individual family members. Results: Active site specificity profiles of 9 MMPs were determined using high throughput Proteomic Identificatio...
ORGANISM(S): Homo sapiens (Human) 
2015-09-29 | PXD002265 | Pride
Ecm Pics Mmps Mass spectrometry Specificity profiling Webpics 
ProteomicsHydrogen deuterium exchange epitope mapping of glycosylated epitopes enabled by online immobilized glycosidase
Numerous mAbs are known to recognize N-glycosylated epitopes or to bind in close proximity to an N-glycan site, however, glycosylated protein sites are typically obscured from HDX detection as a result of the inherent heterogeneity of glycans. To overcome this limitation, we covalently immobilized ...
ORGANISM(S): Homo sapiens (Human) 
2024-05-24 | PXD041204 | Pride
Lc/ms-ms Hdx 
UnknownA novel secretion and online-cleavage strategy for production of cecropin A in Escherichia coli.
Not available
S-EPMC5544755 | biostudies-literature
TranscriptomicsCharacterisation of the AGO2 binding sites in HeLa cell line using eiCLIP
Here we investigate the RNA-binding protein AGO2 in HeLa by using a combination of AGO2 enhanced individual nucleotide resolution UV crosslinking and immunoprecipitation (eiCLIP). We find that 5’ capped RNAs derived from 3’UTRs likely originate from AGO2-mediated cleavage, and most often occur at lo...
ORGANISM(S): Homo sapiens 
2024-09-19 | E-MTAB-12945 | biostudies-arrayexpress
ProteomicsA lysine residue at the C-terminus of MHC class I ligands correlates with low C-terminal proteasomal cleavage probability
The majority of peptides presented by MHC class I results from proteasomal protein turnover. The specialized immunoproteasome, which is induced during inflammation, plays a major role in antigenic peptide generation. However, other cellular proteases can, either alone or together with the proteasome...
ORGANISM(S): Homo sapiens (Human) 
2023-10-24 | PXD044235 | Pride
Immunopeptidomics  proteasome-independent  non-canonical mhc class i ligands  hla-a*03:01  hla-a*11:01  hla-a*30:01  proteasomal cleavage probability  peptide origin  peptide processing 
ProteomicsSymbiont proteome data of whiteflies
To examined the effect of the antibiotic treatment on protein expression of symbionts in the whitefly. Proteome analysis showed that 23 Hamiltonella proteins were down-regulated in Hamiltonella-cured (–HBt) compared to Hamiltonella-infected (+HBt) whiteflies (Dataset S1A,B), this data including all ...
ORGANISM(S): Rickettsia sp. MEAM1 (Bemisia tabaci) 
2023-02-14 | PXD038323 | Pride
Symbiont  proteome  whiteflies 
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