Protein Structure Insights into the Bilayer Interactions of the Saposin-Like Domain of Solanum tuberosum Aspartic Protease
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Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-017-16734-2.pdf
Reference96 articles.
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2. Ramalho-Santos, M. et al. Identification and proteolytic processing of procardosin A. European Journal of Biochemistry 255, 133–138, https://doi.org/10.1046/j.1432-1327.1998.2550133.x (1998).
3. Kervinen, J. et al. Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting. EMBO Journal 18, 3947–3955 (1999).
4. Egas, C. et al. The saposin-like domain of the plant aspartic proteinase precursor is a potent inducer of vesicle leakage. Journal of Biological Chemistry 275, 38190–38196, https://doi.org/10.1074/jbc.M006093200 (2000).
5. Frazão, C. et al. Crystal structure of cardosin A, a glycosylated and Arg-Gly-Asp-containing aspartic proteinase from the flowers of Cynara cardunculus L.Crystal structure of cardosin A, a glycosylated and Arg-Gly-Asp-containing aspartic proteinase from the flowers of Cynara cardunculus L. Journal of Biological Chemistry 274, 27694–27701 (1999).
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