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...
Príomhchruthaitheoirí: | Fowkes, MM, Lim, NH |
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Rannpháirtithe: | Apte, SS |
Formáid: | Book section |
Teanga: | English |
Foilsithe / Cruthaithe: |
Humana Press
2019
|
Míreanna comhchosúla
Míreanna comhchosúla
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Screening for selective ADAMTS-5 substrates to monitor proteinase activity
de réir: Fowkes, MM
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Development of selective ADAMTS-5 peptide substrates to monitor proteinase activity
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Functional differences of the catalytic and non-catalytic domains in human ADAMTS-4 and ADAMTS-5 in aggrecanolytic activity.
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Proteolytic activities of human ADAMTS-5: comparative studies with ADAMTS-4.
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Reactive-site mutants of N-TIMP-3 that selectively inhibit ADAMTS-4 and ADAMTS-5: biological and structural implications.
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Foilsithe / Cruthaithe: (2010)