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ProteomicsProteolytic processing of CD99
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
UnknownEnhanced potency of the metalloprotease inhibitor TAPI-2 by multivalent display.
Not available
S-EPMC4043442 | biostudies-literature
ProteomicsA Landscape of Ectodomain Shedding by Quantitative Protein Terminomics
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) 
2021-03-05 | PXD021378 | JPOST Repository
ProteomicsCleavage preference of metalloprotease EA1
The cleavage preference of the thermophilic metalloprotease from Geobacillus sp. EA1 was characterised using mass spectrometry, confirming its similarity to thermolysin in preferring P1’ hydrophobic amino acids. While EA1 showed similar efficiencies for cleavage of short peptides with one of six hyd...
ORGANISM(S): Escherichia coli Geobacillus sp. EFT1 Bacillus thermoproteolyticus 
2025-11-25 | PXD064530 | Pride
Protease cleavage assay Thermolysin Itraq 
UnknownMetalloprotease inhibitor TIMP proteins control FGF-2 bioavailability and regulate skeletal growth.
Not available
S-EPMC6719459 | biostudies-literature
UnknownNMR structure of emfourin, a novel protein metalloprotease inhibitor: Insights into the mechanism of action.
Not available
S-EPMC10124921 | biostudies-literature
UnknownHelical ultrastructure of the metalloprotease meprin α in complex with a small molecule inhibitor.
Not available
S-EPMC9581967 | biostudies-literature
UnknownCrystal structure of Mycobacterium tuberculosis zinc-dependent metalloprotease-1 (Zmp1), a metalloprotease involved in pathogenicity.
Not available
S-EPMC3173161 | biostudies-literature
UnknownStructure of gentlyase, the neutral metalloprotease of Paenibacillus polymyxa.
Not available
S-EPMC3532130 | biostudies-literature
UnknownThe metalloprotease inhibitor TIMP-3 regulates amyloid precursor protein and apolipoprotein E receptor proteolysis.
Not available
S-EPMC6672812 | biostudies-literature
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