Crossref Cited-by Linking logo

Collect. Czech. Chem. Commun. 1976, 41, 489-497
https://doi.org/10.1135/cccc19760489

Isolation and some properties of cathepsin D inhibitor from potatoes

H. Keilová and V. Tomášek

Crossref Cited-by Linking

  • Osmani Zhila, Sabet Mohammad Sadegh, Nakahara Kenji S.: Aspartic protease inhibitor enhances resistance to potato virus Y and A in transgenic potato plants. BMC Plant Biol 2022, 22. <https://doi.org/10.1186/s12870-022-03596-8>
  • Cai Xixi, Xie Xiaoli, Fu Nanyan, Wang Shaoyun: Physico-Chemical and Antifungal Properties of a Trypsin Inhibitor from the Roots of Pseudostellaria heterophylla. Molecules 2018, 23, 2388. <https://doi.org/10.3390/molecules23092388>
  • Rehman Shazia, Aziz Ejaz, Akhtar Wasim, Ilyas Muhammad, Mahmood Tariq: Structural and functional characteristics of plant proteinase inhibitor-II (PI-II) family. Biotechnol Lett 2017, 39, 647. <https://doi.org/10.1007/s10529-017-2298-1>
  • Guerra Yasel, Valiente Pedro A., Pons Tirso, Berry Colin, Rudiño-Piñera Enrique: Structures of a bi-functional Kunitz-type STI family inhibitor of serine and aspartic proteases: Could the aspartic protease inhibition have evolved from a canonical serine protease-binding loop?. Journal of Structural Biology 2016, 195, 259. <https://doi.org/10.1016/j.jsb.2016.06.014>
  • Guo Jingxu, Erskine Peter T., Coker Alun R., Wood Steve P., Cooper Jonathan B.: Structure of a Kunitz-type potato cathepsin D inhibitor. Journal of Structural Biology 2015, 192, 554. <https://doi.org/10.1016/j.jsb.2015.10.020>
  • Guerra Yasel, Valiente Pedro A., Berry Colin, Pons Tirso: Predicting functional residues of the Solanum lycopersicum aspartic protease inhibitor (SLAPI) by combining sequence and structural analysis with molecular docking. J Mol Model 2012, 18, 2673. <https://doi.org/10.1007/s00894-011-1290-2>
  • Vathipadiekal Vinod, Umasankar Perunthottathu K., Patole Milind S., Rao Mala: Molecular cloning, over expression, and activity studies of a peptidic HIV-1 protease inhibitor: Designed synthetic gene to functional recombinant peptide. Peptides 2010, 31, 16. <https://doi.org/10.1016/j.peptides.2009.09.034>
  • Kulkarni Aarohi, Rao Mala: Differential elicitation of an aspartic protease inhibitor: Regulation of endogenous protease and initial events in germination in seeds of Vigna radiata. Peptides 2009, 30, 2118. <https://doi.org/10.1016/j.peptides.2009.08.024>
  • Lisón Purificación, Rodrigo Ismael, Conejero Vicente: A Novel Function for the Cathepsin D Inhibitor in Tomato. Plant Physiology 2006, 142, 1329. <https://doi.org/10.1104/pp.106.086587>
  • Mosolov V. V., Valueva T. A.: Proteinase inhibitors and their function in plants: A review. Appl Biochem Microbiol 2005, 41, 227. <https://doi.org/10.1007/s10438-005-0040-6>
  • Haq Soghra Khatun, Atif Shaikh Muhammad, Khan Rizwan Hasan: Biochemical characterization, stability studies and N-terminal sequence of a bi-functional inhibitor from Phaseolus aureus Roxb. (Mung bean). Biochimie 2005, 87, 1127. <https://doi.org/10.1016/j.biochi.2005.05.007>
  • Cater Simon A., Lees Wendy E., Hill Jeffrey, Brzin Joze, Kay John, Phylip Lowri H.: Aspartic proteinase inhibitors from tomato and potato are more potent against yeast proteinase A than cathepsin D. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 2002, 1596, 76. <https://doi.org/10.1016/S0167-4838(02)00206-6>
  • Wilhite Stephen E, Elden Thomas C, Brzin Joze, Smigocki Ann C: Inhibition of cysteine and aspartyl proteinases in the alfalfa weevil midgut with biochemical and plant-derived proteinase inhibitors. Insect Biochemistry and Molecular Biology 2000, 30, 1181. <https://doi.org/10.1016/S0965-1748(00)00095-3>
  • Herbers Karin, Prat Salom�, Willmitzer Lothar: Cloning and characterization of a cathepsin D inhibitor gene from Solanum tuberosum L. Plant Mol Biol 1994, 26, 73. <https://doi.org/10.1007/BF00039521>
  • Maganja Darja Barlič, Štrukelj Borut, Pungerčar Jože, Gubenšek Franc, Turk Vito, Kregar Igor: Isolation and sequence analysis of the genomic DNA fragment encoding an aspartic proteinase inhibitor homologue from potato (Solanum tuberosum L.). Plant Mol Biol 1992, 20, 311. <https://doi.org/10.1007/BF00014499>
  • Baudyš Miroslav, Ghosh Minakshi, Harlos Karl, Mareš Michael, Fusek Martin, Kostka Vladimír, Blake Colin C.F.: Crystallization and preliminary crystallographic study of cathepsin D inhibitor from potatoes. Journal of Molecular Biology 1991, 218, 21. <https://doi.org/10.1016/0022-2836(91)90869-8>
  • Ritonja Anka, Križaj Igor, Meško Pika, Kopitar Majda, Lučovnik Peter, Štrukelj Borut, Pungerčar Jože, Buttle David J., Barrett Alan J., Turk Vito: The amino acid sequence of a novel inhibitor of cathepsin D from potato. FEBS Letters 1990, 267, 13. <https://doi.org/10.1016/0014-5793(90)80275-N>
  • Mareš M., Meloun B., Pavlík M., Kostka V., Baudyš M.: Primary structure of cathepsin D inhibitor from potatoes and its structure relationship to soybean trypsin inhibitor family. FEBS Letters 1989, 251, 94. <https://doi.org/10.1016/0014-5793(89)81435-8>
  • Sicard P. J., Mialonier G., Smagghe M., Galen F. X., Corvol P., Devaux C., Ménard J.: Large Scale Preparation of Pure Hog Kidney Renin. Preparative Biochemistry 1978, 8, 19. <https://doi.org/10.1080/00327487808068216>