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ProteomicsLys-C/Arg-C, a New Enzyme Combination for Next-Generation Proteomics
Today, the most widely used bottom-up proteomics studies necessitate a proteolysis step prior to MS analysis. Trypsin is often the best protease in choice due to its high specificity and MS-favored proteolytic products. Trypsin has been challenged for its low cleavage efficiency at Lys-X bonds, and ...
ORGANISM(S): Homo sapiens (Human) 
2018-07-24 | PXD009797 | Pride
Lys-c / arg-c / trypsin / dia / mass spectrometry 
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
UnknownSynergistic Arg-C Ultra and Lys-C Digestion for Quantitative Proteomics.
Not available
S-EPMC12338676 | biostudies-literature
ProteomicsReversible Lysine Derivatization Enables High Specificity of Arg-C Digestion Using Trypsin
Bottom-up proteomics approach has become an important strategy in diverse areas of biological research, and the enzymatic digestion is essential for this technology. Endopeptidase Arg-C catalyzing the hydrolytic cleavage of peptide bonds C-terminal to arginine could be an important protease in botto...
ORGANISM(S): Homo sapiens (Human) Escherichia coli 
2018-01-04 | PXD007994 | Pride
Proteomics Arg-c Trypsin Lys-c Citraconylation Lc-ms/ms 
UnknownEffects of C-Terminal Lys-Arg Residue of AapA1 Protein on Toxicity and Structural Mechanism.
Not available
S-EPMC10537873 | biostudies-literature
UnknownRole of the C-terminal lysine residues of streptococcal surface enolase in Glu- and Lys-plasminogen-binding activities of group A streptococci.
Not available
S-EPMC343989 | biostudies-literature
ProteomicsProteome-wide identification of SUMO2 modification sites
Posttranslational modification with small ubiquitin-like modifiers (SUMOs) alters the function of proteins involved in diverse cellular processes. SUMOs are conjugated to lysine residues in target proteins by SUMO-specific enzymes. Although proteomic studies have identified hundreds of sumoylated su...
ORGANISM(S): Homo sapiens (Human) 
2014-10-15 | PXD001281 | Pride
Heat-shock Sumo modification sites Hek293 
UnknownStructures and oxygen affinities of crystalline human hemoglobin C (β6 Glu->Lys) in the R and R2 quaternary structures.
Not available
S-EPMC3190907 | biostudies-literature
ProteomicsSample preparation for proteomics
Urea-containing buffer solutions are generally used in proteomic studies to aid protein denaturation and solubilisation during cell and tissue lysis. It is well-known, however, that urea can lead to the carbamylation of peptides and proteins and; subsequently, incomplete digestion of proteins. In...
ORGANISM(S): Rattus rattus (Black rat) Homo sapiens (Human) 
2018-06-06 | PXD009426 | Pride
Lys-c/trypsin Urea Lc-ms/ms 
TranscriptomicsCancer SLC3A2-mediated lysine uptake restricts T cell immunity against hepatocellular carcinoma
Our research demonstrates that in hepatocellular carcinoma (HCC), tumor cells outcompete T cells for lysine (Lys) by overexpressing the SLC3A2 transporter, thereby reducing Lys availability within the tumor microenvironment. This lysine deprivation results in decreased STAT3 levels in T cells, inhib...
ORGANISM(S): Homo sapiens Mus musculus 
2024-12-23 | GSE284633 | GEO
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