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Q34114956-37D3BA35-0147-4F02-A2D3-C49A8EEBE0F2
Q34114956-37D3BA35-0147-4F02-A2D3-C49A8EEBE0F2
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Statement
http://www.wikidata.org/entity/statement/Q34114956-37D3BA35-0147-4F02-A2D3-C49A8EEBE0F2
ADAMTS4 cleaves at the aggrecanase site (Glu373-Ala374) and secondarily at the matrix metalloproteinase site (Asn341-Phe342) in the aggrecan interglobular domain.
P2860
Q34114956-37D3BA35-0147-4F02-A2D3-C49A8EEBE0F2
BestRank
Statement
http://www.wikidata.org/entity/statement/Q34114956-37D3BA35-0147-4F02-A2D3-C49A8EEBE0F2
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wasDerivedFrom
a1d186e99a6317d81f3d1b9f53e0b6d49f266d8d
P2860
Analysis of aggrecan in human knee cartilage and synovial fluid indicates that aggrecanase (ADAMTS) activity is responsible for the catabolic turnover and loss of whole aggrecan whereas other protease activity is required for C-terminal processing i