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ProteomicsDeamidation drives molecular aging of the SARS-CoV-2 spike receptor-binding motif
The spike is the main protein component of the SARS-CoV-2 virion surface. The spike receptor-binding motif mediates recognition of the hACE2 receptor, a critical infection step, and is the preferential target for spike-neutralizing antibodies. Post-translational modifications of the spike receptor-b...
ORGANISM(S): Severe acute respiratory syndrome coronavirus 2 
2022-02-15 | PXD028071 | Pride
Sars-cov-2 Molecular aging Rbd Deamidation 
ProteomicsDeamidation drives molecular aging of the SARS-CoV-2 spike receptor-binding motif
The spike is the main protein component of the SARS-CoV-2 virion surface. The spike receptor-binding motif mediates recognition of the hACE2 receptor, a critical infection step, and is the preferential target for spike-neutralizing antibodies. Post-translational modifications of the spike receptor-b...
ORGANISM(S): Severe acute respiratory syndrome coronavirus 2 
2022-02-17 | PXD027873 | Pride
Sars-cov-2 Molecular aging Rbd Deamidation 
ProteomicsEvaluation of the Effect of Trypsin Digestion Buffers on Artificial Deamidation
This work comprehensively compared 50 mM of ammonium acetate (pH 6), Tris-HCl (pH 8), ABC and TEAB as in-solution trypsin digestion buffers. Both iTRAQ quantification and label-free results indicate that ammonium acetate (pH 6) is more suitable than other buffers for studying endogenous deamidation ...
ORGANISM(S): Rattus norvegicus (Rat) 
2022-02-28 | PXD001650 | Pride
Rat Kidney Artificial deamidation 
ProteomicsRevisiting the effect of trypsin digestion buffers on artificial deamidation
Deamidation of asparagine and glutamine residues occurs spontaneously, accelerated by adjacent amino acid residues and influenced by pH, temperature, and incubation time. Standard proteolytic digestion induces significant deamidation, which is especially problematic in bottom-up proteomic studies. T...
ORGANISM(S): Mus musculus (Mouse) 
2025-03-11 | PXD054603 | Pride
De-glycopeptides Chemical deamidation De-glycoproteomics 
ProteomicsHuman Brain LC-MS/MS - Dementia-linked amyloidosis is associated with brain protein deamidation as revealed by proteomic profiling of human brain tissues
Brian Protein Deamidation Associated with Amyloidosis Revealed by Soluble and Amyloidal Brian Proteome Profiling
ORGANISM(S): Homo sapiens (Human) 
2016-08-24 | PXD002516 | Pride
Neurodegenerative disease Amyloids Deamidation Brain proteome 
ProteomicsDeamidation sites of G6PD and PHGDH catalyzed by CAD
CAD interacts with and deamidates glucose-6-phosphate dehydrogenase (G6PD) and phosphoglycerate dehydrogenase (PHGDH), which are rate-limiting enzymes of the PPP and SSP, respectively. Here we identified G6PD and PHGDH deamidation sites by mass spectrometry.
ORGANISM(S): Homo sapiens (Human) 
2026-02-03 | PXD052165 | Pride
G6pd Phgdh Cad Deamidation 
ProteomicsCharacterization of protein deamidation by shotgun proteomics
Characterization of glutamine (Gln) deamidation with the current available methods is only feasible for single compounds or simple mixtures. Here we have developed a new method to analyze in depth Gln and asparagine (Asn) deamidation from complex biological samples by shotgun proteomics.
ORGANISM(S): Homo sapiens (Human) 
2018-07-04 | PXD004355 | Pride
Deamidation Brain Ptm Shotgun Dpm Glutamic acid 
UnknownProtein deamidation.
Not available
S-EPMC122761 | biostudies-literature
ProteomicsAberrant expression of transglutaminase 2 in pancreas and thymus of NOD mice underscores the importance of deamidation in neoantigen generation.
Post-translational modifications can lead to a break in immune tolerance in autoimmune diseases such as type 1 diabetes (T1D). Deamidation, the conversion of glutamine to glutamic acid by transglutaminase (TGM) enzymes, is a post-translational modification of interest, with deamidated peptides being...
ORGANISM(S): Mus musculus (Mouse) 
2022-07-21 | PXD034102 | Pride
Type 1 diabetes Post-translational modification Transglutaminase 2 Deamidation 
UnknownDeamidation of human proteins.
Not available
S-EPMC60067 | biostudies-literature
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