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Regulation of membrane-type-1 matrix metalloproteinase activity by its cytoplasmic domain.
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Deletion of the cytoplasmic tail did not affect the trafficking of MT1-MMP to the plasma membrane nor its ability to activate proMMP2, but the mutant proteins displayed a different distribution pattern on the cell surface and an impaired ability to mediate cell invasion compared to the wild-type protein.
“Deletion of the cytoplasmic tail did not affect the trafficking of MT1-MMP to the plasma membrane nor its ability to activate proMMP2, but the mutant proteins displayed a different distribution pattern on the cell surface and an impaired ability to mediate cell invasion compared to the wild-type protein (59, 60).”
From Identification of amino acid residues in the MT-loop of MT1-MMP critical for its ability to cleave low-density lipoprotein receptor (2022) · cites this paper as [59]
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Metadata
- Authors
- Lehti, K., Valtanen, H., Wickström, S., Lohi, J., & Keski-Oja, J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-05
- Volume
- 275
- Issue
- 20
- Pages
- 15006-15013
- ISSN
- 0021-9258
- Cited by
- 144
- References
- 0
- Language
- en
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