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UnknownDeciphering the human platelet sheddome.
Not available
S-EPMC3037762 | biostudies-literature
ProteomicsDevelopment of a proteomic workflow for the identification of heparan sulfate proteoglycan-binding substrates of ADAM17. Evaluation of heparin effects on sample preparation by FASP.
Ectodomain shedding, which is the proteolytic release of transmembrane proteins from the cell surface, is crucial for cell-to-cell communication and other biological processes. The metalloproteinase ADAM17 mediates ectodomain shedding of over 50 transmembrane proteins ranging from cytokines and grow...
ORGANISM(S): Mus musculus (Mouse) 
2025-07-23 | PXD054987 | Pride
Sheddome Adam17 Ectodomain shedding Disintegrin metalloproteinases Secretome 
ProteomicsDevelopment of a proteomic workflow for the identification of heparan sulfate proteoglycan-binding substrates of ADAM17 - Evaluation of heparin effects on sample preparation PreOmics
Ectodomain shedding, which is the proteolytic release of transmembrane proteins from the cell surface, is crucial for cell-to-cell communication and other biological processes. The metalloproteinase ADAM17 mediates ectodomain shedding of over 50 transmembrane proteins ranging from cytokines and grow...
ORGANISM(S): Mus musculus (Mouse) 
2025-05-07 | PXD055002 | Pride
Sheddome Adam17 Ectodomain shedding Heparin Disintegrin metalloproteinases Secretome 
UnknownShed CNTNAP2 ectodomain is detectable in CSF and regulates Ca2+ homeostasis and network synchrony via PMCA2/ATP2B2.
Not available
S-EPMC8857041 | biostudies-literature
ProteomicsFalse positive glycopeptide identification through in-FAIMS glycan fragmentation.
Glycosylation is an important post-translational modification characterized by extensive heterogeneity. While mass spectrometry (MS) is the premier technique to characterize glycoproteins, the study of intact glycopeptides presents challenges often not observed in the study of unmodified species. Hi...
ORGANISM(S): Homo sapiens (Human) 
2023-09-11 | PXD041217 | Pride
Glycoproteomics Mucinomics faims Mucin-domain glycoproteomics Enrichment. Ion mobility separation 
UnknownDevelopment of a Proteomic Workflow for the Identification of Heparan Sulphate Proteoglycan-Binding Substrates of ADAM17.
Not available
S-EPMC11648071 | biostudies-literature
UnknownProteolysis of Gingival Keratinocyte Cell Surface Proteins by Gingipains Secreted From Porphyromonas gingivalis - Proteomic Insights Into Mechanisms Behind Tissue Damage in the Diseased Gingiva.
Not available
S-EPMC7198712 | biostudies-literature
Proteomicsmembrane substrates of gingipains
Porphyromonas gingivalis secretes cysteine proteases named gingipains which can cleave an array of proteins and importantly contribute to the development of periodontitis. In this study we focused on gingipain-exerted proteolysis at the cell surface of human gingival epithelial cells (telomerase imm...
ORGANISM(S): Homo sapiens (Human) 
2020-04-28 | PXD015679 | Pride
Protease Shedding Gingipain Anoikis Proteolysis 
UnknowniRhom2 regulates ectodomain shedding and surface expression of the major histocompatibility complex (MHC) class I.
Not available
S-EPMC10991058 | biostudies-literature
ProteomicsDevelopment of a proteomic workflow for the identification of heparan sulfate proteoglycan-binding substrates of ADAM17
Ectodomain shedding, which is the proteolytic release of transmembrane proteins from the cell surface, is crucial for cell-to-cell communication and other biological processes. The metalloproteinase ADAM17 mediates ectodomain shedding of over 50 transmembrane proteins ranging from cytokines and grow...
ORGANISM(S): Mus musculus (Mouse) 
2024-10-15 | PXD055223 | Pride
Adam17 Ectodomain shedding Mouse Hepsec Secretome Metalloproteases 
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