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ProteomicsActive Site Specificity Profiling of the Matrix Metalloproteinase Family: Proteomic Identification of 4,300 Cleavage Sites by MMPs 1, 2, 3, 7, 8, 9, 12, 13, and 14.
Background: The active site of matrix metalloproteinases (MMPs) is highly conserved, complicating the rational design of specific substrates and inhibitors for individual family members. Results: Active site specificity profiles of 9 MMPs were determined using high throughput Proteomic Identificatio...
ORGANISM(S): Homo sapiens (Human) 
2015-09-29 | PXD002265 | Pride
Ecm Pics Mmps Mass spectrometry Specificity profiling Webpics 
ProteomicsFactor Xa PICS with chymotryptic peptide library
Factor Xa PICS with chymotryptic peptide library
ORGANISM(S): Homo sapiens (Human) 
2011-10-14 | PRD000421 | Pride
ProteomicsEarly response of C2C12 myotubes to a sub-cytotoxic dose of hemorrhagic metalloproteinase HF3 from Bothrops jararaca venom
Manifestations of local tissue damage, such as hemorrhage and myonecrosis, are among the most dramatic effects of envenomation by viperid snakes. Snake venom metalloproteinases (SVMPs) of the P-III class are main players of the hemorrhagic effect due to their activities in promoting blood vessel dis...
ORGANISM(S): Mus musculus (Mouse) 
2019-02-25 | PXD011274 | Pride
C2c12 myotubes  hf3  snake venom metalloproteinase  peptidomics  proteomics 
ProteomicsA systemic view of active site specificity profiling of the snake venom metalloprotease HF3 using Proteomic Identification of Cleavage Sites and N-terminomics TAILS
Snake venom metalloproteinases play important roles in the pathological effects of Viperidae venoms including severe local tissue damage, hemorrhage and coagulopathy. Hemorrhagic Factor 3 (HF3), a metalloproteinase isolated from Bothrops jararaca venom, induces severe local hemorrhage. Previous prot...
ORGANISM(S): Mus musculus (Mouse) 
2019-07-29 | PXD009201 | Pride
N-terminome Snake venom metalloprotease Snake venom Hf3 Tails Degradomics 
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