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UnknownIn-Depth Characterization of Apoptosis N-Terminome Reveals a Link Between Caspase-3 Cleavage and Posttranslational N-Terminal Acetylation.
Not available
S-EPMC10362333 | biostudies-literature
UnknownImpact of posttranslational modifications on atomistic structure of fibrinogen.
Not available
S-EPMC6988951 | biostudies-literature
UnknownPosttranslational modifications of proopiomelanocortin in vertebrates and their biological significance.
Not available
S-EPMC3797980 | biostudies-literature
TranscriptomicsSite-specific methylation of Notch1 controls the amplitude and duration of the Notch1 response
Physiologically, Notch signal transduction plays a pivotal role in differentiation; pathologically, Notch signaling contributes to the development of cancer. Transcriptional activation of Notch target genes involves cleavage of the Notch receptor in response to ligand binding, production of the Notc...
ORGANISM(S): Mus musculus 
2015-03-26 | E-GEOD-62528 | biostudies-arrayexpress
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 (ncbitaxon:9606) 
2017-03-29 | MSV000080741 | MassIVE
UnknownFurin-Mediated Cleavage of Zona Pellucida Proteins Is Essential for Oocyte Development.
Not available
S-EPMC12701285 | biostudies-literature
UnknownNonenzymatic Posttranslational Modifications and Peptide Cleavages Observed in Peptide Epimers.
Not available
S-EPMC10524105 | biostudies-literature
ProteomicsChemoproteomic identification of a phosphohistidine acceptor: Insights into posttranslational regulation of glycolysis
Histidine phosphorylation is an underexplored form of protein phosphorylation. Despite the widespread existence of phosphohistidine (pHis) sites, particularly in bacteria, their phosphorylation regulation and physiological functions remain poorly understood. In this study, we developed a chemoproteo...
ORGANISM(S): Escherichia coli 
2025-05-07 | PXD053006 | Pride
Cell lysate E.coli Qexactive Lc-ms/ms 
ProteomicsChemoproteomic identification of a phosphohistidine acceptor: Insights into posttranslational regulation of glycolysis
Histidine phosphorylation is an underexplored form of protein phosphorylation. Despite the widespread existence of phosphohistidine (pHis) sites, particularly in bacteria, their phosphorylation regulation and physiological functions remain poorly understood. In this study, we developed a chemoproteo...
ORGANISM(S): Escherichia coli 
2025-05-07 | PXD056526 | Pride
Cell lysate E.coli Qexactive Lc-ms/ms 
UnknownThe complexity of the IGF1 gene splicing, posttranslational modification and bioactivity.
Not available
S-EPMC4022784 | biostudies-literature
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