Heparan Sulfate Regulates ADAM12 through a Molecular Switch Mechanism

The disintegrin and metalloproteases (ADAMs) are emerging as therapeutic targets in human disease, but specific drug design is hampered by potential redundancy. Unlike other metzincins, ADAM prodomains remain bound to the mature enzyme to regulate activity. Here ADAM12, a protease that promotes tumo...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	The Journal of biological chemistry 2008-11, Vol.283 (46), p.31920-31932
Hauptverfasser:	Sørensen, Hans Peter, Vivès, Romain R., Manetopoulos, Christina, Albrechtsen, Reidar, Lydolph, Magnus C., Jacobsen, Jonas, Couchman, John R., Wewer, Ulla M.
Format:	Artikel
Sprache:	eng
Schlagworte:	ADAM Proteins ADAM Proteins - genetics ADAM Proteins - metabolism ADAM12 Protein Animals Biochemistry Biochemistry, Molecular Biology Catalytic Domain Cell Line Cell Membrane Cell Membrane - metabolism Cricetinae Enzyme Activation Glucuronidase Glucuronidase - metabolism Glycosaminoglycans Glycosaminoglycans - metabolism Heparitin Sulfate Heparitin Sulfate - metabolism Humans Life Sciences Membrane Proteins Membrane Proteins - genetics Membrane Proteins - metabolism Osteoarthritis Osteoarthritis - enzymology Protein Binding Substrate Specificity
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!