Dataset Information
Active 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.
Ontology highlight
ABSTRACT:
INSTRUMENT(S): QSTAR XL, QSTAR Pulsar
ORGANISM(S): Homo Sapiens (human)
SUBMITTER: 
Ulrich ECKHARD
LAB HEAD: Prof. Christopher Mark Overall
PROVIDER: PXD002265 | Pride | 2015-09-29
REPOSITORIES: Pride
Publications
Active site specificity profiling of the matrix metalloproteinase family: Proteomic identification of 4300 cleavage sites by nine MMPs explored with structural and synthetic peptide cleavage analyses.
Matrix biology : journal of the International Society for Matrix Biology 20150925
Secreted and membrane tethered matrix metalloproteinases (MMPs) are key homeostatic proteases regulating the extracellular signaling and structural matrix environment of cells and tissues. For drug targeting of proteases, selectivity for individual molecules is highly desired and can be met by high yield active site specificity profiling. Using the high throughput Proteomic Identification of protease Cleavage Sites (PICS) method to simultaneously profile both the prime and non-prime sides of the ...[more]
