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ProteomicsProteomic characterization of ubiquitin carboxyl-terminal hydrolase 19 deficient cells reveals a role for USP19 in secretion of lysosomal proteins
Ubiquitin carboxyl-terminal hydrolase 19 (USP19) is a unique deubiquitinase (DUB), characterized by multiple variants generated by alternative splicing. Several variants bear a C-terminal transmembrane domain that anchors them to the endoplasmic reticulum (ER). Other than regulating protein stabilit...
ORGANISM(S): Homo sapiens (Human) 
2025-05-07 | PXD055064 | Pride
Lysosome Cathepsins. Ubiquitin carboxyl-terminal hydrolase 19  proteomics  unconventional secretion  secretome  legumain 
ProteomicsProteomic characterization of ubiquitin carboxyl-terminal hydrolase 19 deficient cells reveals a role for USP19 in secretion of lysosomal proteins
Ubiquitin carboxyl-terminal hydrolase 19 (USP19) is a unique deubiquitinase (DUB), characterized by multiple variants generated by alternative splicing. Several variants bear a C-terminal transmembrane domain that anchors them to the endoplasmic reticulum (ER). Other than regulating protein stabilit...
ORGANISM(S): Homo sapiens (Human) 
2025-05-07 | PXD055081 | Pride
Lysosome Cathepsins. Ubiquitin carboxyl-terminal hydrolase 19  proteomics  unconventional secretion  secretome  legumain 
ProteomicsProteomic characterization of ubiquitin carboxyl-terminal hydrolase 19 deficient cells reveals a role for USP19 in secretion of lysosomal proteins
Ubiquitin carboxyl-terminal hydrolase 19 (USP19) is a unique deubiquitinase (DUB), characterized by multiple variants generated by alternative splicing. Several variants bear a C-terminal transmembrane domain that anchors them to the endoplasmic reticulum (ER). Other than regulating protein stabilit...
ORGANISM(S): Homo sapiens (Human) 
2025-05-07 | PXD055118 | Pride
Lysosome Cathepsins. Ubiquitin carboxyl-terminal hydrolase 19  proteomics  unconventional secretion  secretome  legumain 
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
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 
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 
UnknownClinical Features, Cardiovascular Risk Profile, and Therapeutic Trajectories of Patients with Type 2 Diabetes Candidate for Oral Semaglutide Therapy in the Italian Specialist Care.
Not available
S-EPMC10597935 | biostudies-literature
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