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UnknownEvaluation of Sample Preparation Strategies for Human Milk and Plasma Proteomics.
Not available
S-EPMC8618985 | biostudies-literature
ProteomicsDifferentially abundant proteins between non-blood fed female and male Aedes aegypti proteome via LC-ESI-MS/MS using label-free protein quantification
Proteins from female and male Aedes aegypti were extracted and analyzed on high-resolution LC ESI MS MS. Proteomic data were analyzed using PeaksX+ search algorithm against Uniprot Mosquito released 2020_01 from Swissprot and TrEMBL databases with a fixed modification on Carbamidomethylation.
ORGANISM(S): Aedes Aegypti (ncbitaxon:7159) 
MSV000086179 | MassIVE
ProteomicsPitfalls and Solutions in Mass Spectrometry-based Identification of Protein Glycation
Protein glycation is a type of post-translational modification (PTM) involving complex non-enzymatic reactions of reducing sugars or reactive dicarbonyls with proteins, generating a heterogeneous group of advanced glycation end-products (AGEs) such as carboxymethyllysine (CML). In bottom-up proteomi...
ORGANISM(S): Homo sapiens (Human) Escherichia coli 
2023-01-24 | PXD032235 | Pride
Cam Post-translational modification Human Iaa N-isopropylcarbamidoethylation Nipam Cm Cml Cell line Q-exactive N-isopropylacrylamide Hela 2-iodoacetamide Orbitrap Carboxymethylation Escherichia coli E. coli Ptm Kidney Protein glycation Hek293 Carboxymethyllysine Lc-ms/ms Age Nipcae Carbamidomethylation Advanced glycation end-product 
ProteomicsChaFRADIC: A novel SCX-based approach for N-terminal Enrichment
Step 1: Cell lysis of yeast sphaeroblast (Saccharomyces cerevisiae) and carbamidomethylation. Step 2: Isotopic labeling with dimethylation (light + medium). Step 3: Proteolytic digestion with trypsin (ArgC specificity because of blocked lysines by dimethylation). Step 4: Enrichment via ChaFRADIC...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2013-08-09 | PXD000292 | Pride
Chafradic Yeast Protease Peptidase Icp55 Cofradic N-terminal Degradomics 
ProteomicsMethylated trypsin - Enhanced trypsin on a budget: Stabilization, purification and high-temperature application of inexpensive commercial trypsin for proteomics applications
HCP analysis of the various trypsins was performed using the X! Tandem search engine (Alanine) (http://www.thegpm.org). All data was searched against the downloaded UniProt Sus scrofa proteome (40.706 sequences, March 10, 2019) and the most recent cRAP list (http://www.thegpm.org). Data were search ...
ORGANISM(S): Sus scrofa domesticus (domestic pig) 
2019-06-06 | PXD013458 | Pride
Methylation Trypsin Hcp 
ProteomicsExtending the coverage of Lys-C/trypsin-based bottom-up proteomics using cysteine S-aminoethylation
In this study, S-aminoethylation of Cys (AE-Cys) was carried out with 2-bromoethylamine to form pseudo-Lys, which was then digested with Lys-C or trypsin to improve proteome coverage in bottom-up proteomics. A model study with bovine serum albumin showed that the C-terminal side of Cys was successfu...
ORGANISM(S): Homo Sapiens (human) Bos Taurus 
2023-09-27 | PXD045433 | JPOST Repository
ProteomicsCopper-responsive proteome changes in human kidney proximal tubule epithelial cells
Copper is essential for cellular function but potentially toxic in excess. While copper's influence on cytoskeletal dynamics remains unclear, loss of mechanical integrity is a hallmark of kidney disease. Here we investigated how copper availability modulates mechanical properties and cytoskeletal ar...
ORGANISM(S): Homo sapiens (Human) 
2026-07-21 | PXD072220 | Pride
Proteomics Cytoskeleton Mechanotransduction Actin Kidney Copper Oxidative stress Hk-2 
MetabolomicsGNPS - Sticky organisms create underwater biological adhesives driven by interactions between EGF- and GlcNAc- containing polysaccharides.
This data includes the ESI-LC-MS/MS data from the paper below; Sticky organisms create underwater biological adhesives driven by interactions between EGF- and GlcNAc- containing polysaccharides.
ORGANISM(S): Barbatia Virescens (ncbitaxon:6559) 
2024-10-28 | MSV000096230 | GNPS
ProteomicsProteomic profile of Cephalosporin-Resistant Neisseria gonorrhoeae Isolates by low pH nano-HPLC-MS/MS
The experiment was performed using three N. gonorrhoeae clinical isolates and N. gonorrhoeae strain ATCC 49226 was used as a reference strain. Tandem mass spectra were processed by PEAKS Studio version 8.5 (Bioinformatics Solutions Inc., Waterloo, Canada). PEAKS DB was set up to search the database ...
ORGANISM(S): Neisseria gonorrhoeae 
2019-10-22 | PXD015296 | Pride
Low ph nano-hplc-ms/ms  cephalosporin-resistant neisseria gonorrhoeae 
ProteomicsA model considering the different forms of a protein to accurately describe protein degradation in human cells
Searching parameter: 10 ppm precursor mass tolerance; 0.025 Da product ion mass tolerance; fully digested with trypsin; up to two missed cleavages; Variable modifications: oxidation of methionine (M+15.9949); heavy lysine (K+8.0142); heavy arginine (R+6.0201); Fixed modifications: carbamidomethylati...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-10-20 | MSV000086337 | MassIVE
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