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Mechanism of Folding and Activation of Subtilisin Kexin Isozyme-1 (SKI-1)/Site-1 Protease (S1P)
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The prodomain of S1P is crucial for its folding, autoprocessing and proteolysis of substrates including SREBP2.
“Contrasting to those in other proprotein convertases that function as an inhibitor, the prodomain of S1P is crucial for its folding, autoprocessing and proteolysis of substrates including SREBP2 (da Palma et al., 2014; da Palma et al., 2016).”
From POST1/C12ORF49 regulates the SREBP pathway by promoting site-1 protease maturation (2021) · cites this paper as da Palma et al., 2016
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Zhu, X., Ohta, Y., Jordan, F., & Inouye, M. (1989) · Nature · doi:10.1038/339483a0 · Cited by 344
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Cited by
Sorted by citations
POST1/C12ORF49 regulates the SREBP pathway by promoting site-1 protease maturation
Xiao, J., Xiong, Y., Yang, L.-T., Wang, J.-Q., Zhou, Z.-M., Dong, L.-W., Shi, X.-J., Zhao, X., Luo, J., & Song, B.-L. (2021) · Protein & Cell · doi:10.1007/s13238-020-00753-3 · Cited by 49
SPRING is a Dedicated Licensing Factor for SREBP-Specific Activation by S1P
Hendrix, S., Tan, J. M. E., Ndoj, K., Kingma, J., Valiloo, M., Zijlstra, L. F., Ottenhoff, R., Seidah, N. G., Loregger, A., Kober, D. L., et al. (2024) · Molecular and Cellular Biology · doi:10.1080/10985549.2024.2348711 · Cited by 9
Self-citation
Metadata
- Authors
- da Palma, J. R., Cendron, L., Seidah, N. G., Pasquato, A., & Kunz, S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2016-01
- Volume
- 291
- Issue
- 5
- Pages
- 2055-2066
- ISSN
- 0021-9258
- Cited by
- 14
- References
- 1
- Language
- en
- Licence
- Funders
- Swiss National Science Foundation (31003A-135536, 310030_149746)
- Canadian Institutes of Health Research (93792)
- Canada Research Chairs (216684)
- Novartis Stiftung für Medizinisch-Biologische Forschung (14B086)
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