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Ectodomain shedding is a proteolytic process that regulates level and function of membrane proteins. By quantitative protein terminomics consisting of N- and C-terminal peptide enrichment, TMT-labeling and mass spectrometry, we quantified protein termini in the cultured media across 10 human cell li...
ORGANISM(S): Homo Sapiens (human) 
Targeting cardiomyocyte ADAM10 ectodomain shedding promotes survival early after myocardial infarction
Proteolytic ectodomain shedding of membrane proteins is a fundamental mechanism to control the communication between cells and their environment. A key protease for membrane protein shedding is ADAM17, which requires a non-proteolytic subunit, either inactive Rhomboid 1 (iRhom1) or iRhom2 for its ac...
ORGANISM(S): Mus musculus (Mouse) 
2021-10-07 | PXD028096 | Pride
Myocardial infarction (MI) contributes to cardiac mortality and morbidity. After myocardial infarction the innate immune response is pivotal in clearing of tissue debris as well as scar formation, but exaggerated cytokine and chemokine secretion with subsequent leukocyte infiltration also leads to f...
ORGANISM(S): Mus musculus 
2022-11-10 | GSE217268 | GEO
Heparan sulfate modifications of betaglycan promote TIMP3-dependent ectodomain shedding to fine-tune TGF-β signaling.
Betaglycan/type III TGF-β receptor (TGFBR3) is an established co-receptor for the TGF-β superfamily with direct binding demonstrated for TGF-β 1-3 and inhibin A. Betaglycan can be membrane-bound or have its ectodomain cleaved/ shed to produce soluble-betaglycan that has been demonstrated to sequeste...
ORGANISM(S): Homo sapiens 
2024-02-21 | GSE237403 | GEO
The adhesion molecule CD99 is essential for transendothelial migration (TEM) of leukocytes. Here we demonstrate by biochemical and cellular assays that CD99 undergoes ectodomain shedding by the metalloprotease meprin ? and subsequent intramembrane proteolysis by ?-secretase. The cleavage site in CD9...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080746 | MassIVE
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