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Inhibition of matrix metalloproteinase 14 (MMP-14)-mediated cancer cell migration.
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The HPX domain contributes to the interaction of MT1-MMP with its substrates, such as CD44 and collagen.
“The HPX domain contributes to the interaction of MT1-MMP with its substrates, such as CD44 and collagen (54–57).”
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 [57]
The section on PEX-domain motifs reports that a blade I mutant failed to coprecipitate with CD44, supporting a role for the domain in the MMP-14–CD44 interaction. The Discussion also describes CD44 cleavage by MMP-14. Our copy does not establish that the PEX domain contributes to interaction with collagen; searches for collagen binding and substrate interaction did not find such a passage. No page number was available in the indexed copy. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThe HPX domain is required for MT1-MMP binding to CD44 and collagen.
“The HPX domain is required for MT1-MMP binding to CD44 and collagen.”
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 [57]
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New functions for the matrix metalloproteinases in cancer progression
Egeblad, M., & Werb, Z. (2002) · Nature Reviews Cancer · doi:10.1038/nrc745 · Cited by 6,108
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Metadata
- Authors
- Zarrabi, K., Dufour, A., Li, J., Kuscu, C., Pulkoski-Gross, A., Zhi, J., Hu, Y., Sampson, N. S., Zucker, S., & Cao, J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2011-09
- Volume
- 286
- Issue
- 38
- Pages
- 33167-33177
- ISSN
- 0021-9258
- Cited by
- 188
- References
- 1
- Language
- en
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