The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family.
By H. E. Wart, Henning BIRKEDAL-HANSENt. 1990
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
- P. E. Van den Steen
- S. Zhong
- G. Opdenakker
- R. Khalil
- T. Klein
- Francis G. Spinale
- O. Zítka
- B. M
Citations in the corpus
- Accurate prediction of protein structures and interactions using a 3-track neural network (2021, positive): “There is a cysteine in an extension following the predicted prodomain barrel; taken together, these data are consistent with experimental data suggesting that the ADAM prodomain inhibits metalloprotease activity using a cysteine switch (26).”
- A Disintegrin and Metalloproteinase (ADAM) and ADAM with Thrombospondin Motifs (ADAMTS) Family in Vascular Biology and Disease (2019, background): “The cysteine switch in the pro-domain should not be confounded with the distinct cysteine-rich domain in the ADAM molecule [17].”
- Matrix metalloproteinases as modulators of inflammation and innate immunity (2004, background): “They are converted to active proteinases by disruption of this interaction (a process known as the CYSTEINE-SWITCH MECHANISM”
- Gelatinase-mediated migration and invasion of cancer cells. (2005, background): “The cysteine residue coordinates with the catalytic zinc ion and blocks the entry of a catalytically essential water molecule to the active site (Van Wart and Birkedal-Hansen, 1990).”
- Regulation of the α‐secretase ADAM10 by its prodomain and proprotein convertases (2001, background): “This mechanism is mediated by a highly conserved cysteine residue in the prodomain, which might coordinate the zink ion located at the active site of the catalytic domain (21, 22).”
- Matrix metalloproteinases. (2010, background): “This interaction, [Zn 2+ -cysteine], keeps the proMMP inactive [74,75].”