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MT1-MMP Binds Membranes by Opposite Tips of Its β Propeller to Position It for Pericellular Proteolysis
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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 [55]
The 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 [55]
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Cited by
Sorted by citations
Wang, M., Alabi, A., Gu, H.-M., Gill, G., Zhang, Z., Jarad, S., Xia, X.-D., Shen, Y., Wang, G.-Q., & Zhang, D.-W. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.917238 · Cited by 13
Metadata
- Authors
- Marcink, T. C., Simoncic, J. A., An, B., Knapinska, A. M., Fulcher, Y. G., Akkaladevi, N., Fields, G. B., & Van Doren, S. R.
- ORCID
- Van Doren, Steven R.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2019-02
- Volume
- 27
- Issue
- 2
- Pages
- 281-292.e6
- ISSN
- 0969-2126
- PMC
- PMC6365218
- Cited by
- 24
- References
- 0
- Language
- en
- Licence
- Funders
- University of Missouri
- National Institutes of Health (S10 RR022341, R01 CA098799, R01 GM60048)
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