Purification and activity determination of ADAMTS-4 and ADAMTS-5 and their domain deleted mutants
AA disintegrin-like and metalloproteinase with thrombospondin type-1 motifs-4 (ADAMTS-4) and ADAMTS-5 are zinc-dependent metalloproteinases that are involved in the maintenance of cartilage extracellular matrix (ECM) and are currently considered the major aggrecanases in the development of osteoarth...
المؤلفون الرئيسيون: | Fowkes, MM, Lim, NH |
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مؤلفون آخرون: | Apte, SS |
التنسيق: | Book section |
اللغة: | English |
منشور في: |
Humana Press
2019
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مواد مشابهة
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Screening for selective ADAMTS-5 substrates to monitor proteinase activity
حسب: Fowkes, MM
منشور في: (2021) -
Development of selective ADAMTS-5 peptide substrates to monitor proteinase activity
حسب: Fowkes, MM, وآخرون
منشور في: (2023) -
Functional differences of the catalytic and non-catalytic domains in human ADAMTS-4 and ADAMTS-5 in aggrecanolytic activity.
حسب: Fushimi, K, وآخرون
منشور في: (2008) -
Proteolytic activities of human ADAMTS-5: comparative studies with ADAMTS-4.
حسب: Gendron, C, وآخرون
منشور في: (2007) -
Reactive-site mutants of N-TIMP-3 that selectively inhibit ADAMTS-4 and ADAMTS-5: biological and structural implications.
حسب: Lim, N, وآخرون
منشور في: (2010)