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Molecular insights into the multilayered regulation of ADAM17: The role of the extracellular region
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Lysosomal-dependent degradation of ADAM17 has an impact on ADAM17 shedding activity.
“Last, lysosomal-dependent degradation of ADAM17 has an impact on ADAM17 shedding activity (29).”
From ADAM17 mediates ectodomain shedding of the soluble VLDL receptor fragment in the retinal epithelium (2021) · cites this paper as [29]
There are negative regulators that inhibit ADAM17 activities, including the prodomain of ADAM17, β-integrin, and TIMP3.
“There are negative regulators that inhibit the ADAM17 activities, including the prodomain of ADAM17, β-integrin, and TIMP3 (29).”
From ADAM17 mediates ectodomain shedding of the soluble VLDL receptor fragment in the retinal epithelium (2021) · cites this paper as [29]
TIMP3 binds with its N terminus to ADAM17 and sterically blocks the interaction between ADAM17 and its substrates.
“Among them, TIMP3 binds with its N terminus to ADAM17 and sterically blocked the interaction between ADAM17 and its substrates (29).”
From ADAM17 mediates ectodomain shedding of the soluble VLDL receptor fragment in the retinal epithelium (2021) · cites this paper as [29]
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A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells
Black, R. A., Rauch, C. T., Kozlosky, C. J., Peschon, J. J., Slack, J. L., Wolfson, M. F., Castner, B. J., Stocking, K. L., Reddy, P., Srinivasan, S., et al. (1997) · Nature · doi:10.1038/385729a0 · Cited by 3,149
Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C‐shaped scaffold
Takeda, S., Igarashi, T., Mori, H., & Araki, S. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601131 · Cited by 202
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Metadata
- Authors
- Grötzinger, J., Lorenzen, I., & Düsterhöft, S.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2017-11
- Volume
- 1864
- Issue
- 11
- Pages
- 2088-2095
- ISSN
- 0167-4889
- Cited by
- 76
- References
- 2
- Language
- en
- Licence
- Funders
- German Research Foundation (SFB877, DU 1582/1-1, 1710)
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