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ProteomicsMethionine Alkylation as an Approach to Quantify Methionine Oxidation Using Mass Spectrometry
Post-translational oxidation of methionine residues can destabilize proteins or modify their functions. Although levels of methionine oxidation can provide important information regarding the structural integrity and regulation of proteins, their quantitation is often challenging as analytical proce...
ORGANISM(S): Escherichia coli 
2024-02-08 | PXD045497 | Pride
Methionine oxidation  methionine alkylation  proteomics Mass spectrometry (ms) 
ProteomicsSystematic Evaluation of Protein Reduction and Alkylation reveals Massive Unspecific Side Effects by Iodine-containing Reagents
In this study, we systematically evaluated reduction and alkylation of proteins using three reducing agents (DTT, TCEP, and BME) in combination with four alkylation agents (IAA, IAC, AA, and CAA). We tested these conditions using strong anion exchange (SAX) fractionated in-solution digests and in-ge...
ORGANISM(S): Homo sapiens (Human) 
2017-05-30 | PXD005183 | Pride
Alkylation Proteomics Reduction 
ProteomicsCysteine alkylating methods in shotgun proteomics and their possible effects on methionine residues
Neatly every proteomic protocol has a Cysteine reduction and alkylation step in it preceding the trypsin digestion. It needs to be done in order to remove the s-s bonds and prevent proteins from folding, thus, provide better access for trypsin. Among various reagents used for alkylation, iodoacetami...
ORGANISM(S): Homo sapiens (Human) 
2020-10-28 | PXD013973 | Pride
Cysteine Proteomics Alkylation Methionine 
ProteomicsCysteine alkylating methods in shotgun proteomics and their possible effects on methionine residues
Neatly every proteomic protocol has a Cysteine reduction and alkylation step in it preceding the trypsin digestion. It needs to be done in order to remove the s-s bonds and prevent proteins from folding, thus, provide better access for trypsin. Among various reagents used for alkylation, iodoacetami...
ORGANISM(S): Homo sapiens (Human) 
2024-02-14 | PXD015889 | Pride
Cysteine Proteomics Alkylation Methionine Reduction 
UnknownBioorthogonal Metalloporphyrin-Catalyzed Selective Methionine Alkylation in the Lanthipeptide Nisin.
Not available
S-EPMC6680192 | biostudies-literature
UnknownReversible stapling of unprotected peptides via chemoselective methionine bis-alkylation/dealkylation.
Not available
S-EPMC5931191 | biostudies-literature
ProteomicsDifferential alkylation of PHLPP2
To determine the accessibility of cysteines in purified PHLPP2, we assessed their reactivity with iodoacetamide under native conditions. After denaturing with urea and reducing potential disulfide bridges with TCEP, the remaining free cysteines were modified with methyl methanethiosulfonate. This 2-...
ORGANISM(S): Homo sapiens (Human) 
2025-03-13 | PXD052551 | Pride
Differential alkylation Free thiols 
ProteomicsThe impact of commonly used alkylating agents on artefactual peptide modification
Iodoacetamide is by far the most commonly used agent for alkylation of cysteine during sample preparation for proteomics. An alternative, 2-chloroacetamide, has been recently suggested to reduce the alkylation of residues other than cysteine, such as the N-terminus, Asp, Glu, Lys, Ser, Thr and Tyr....
ORGANISM(S): Rattus norvegicus (Rat) 
2017-08-16 | PXD007071 | Pride
Post-translational modification Cysteine alkylation Artefact N-terminal alkylation Alkylation 
ProteomicsQuantitative analysis of in vivo methionine oxidation of the human proteome
A novel stable isotope labelling strategy was developed to quantify methionine oxidation in an unstressed human proteome. Cell extracts were oxidized with 18O labelled hydrogen peroxide following cell lysis in order to convert all unoxidized methionine residues to an oxidized version with a heavy l...
ORGANISM(S): Homo sapiens (Human) 
2019-12-09 | PXD014629 | Pride
Methionine oxidation Unstressed proteome Human cell line 
UnknownAlkylation of rabbit muscle creatine kinase surface methionine residues inhibits enzyme activity in vitro.
Not available
S-EPMC8448711 | biostudies-literature
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