1. Crystal structures of aprotinin and its complex with sucrose octasulfate reveal multiple modes of interactions with implications for heparin binding. Yang, In Seok, Kim, Tae Gyun, Park, Bum Seok, Cho, Ki Joon, Lee, Ji-Hye, Park, Yiho, Kim, Kyung Hyun. Biochemical and Biophysical Research Communications 397 (2010) 429-435.
2. Garrett, Charles M, Garrett, Reginald H. Biochemistry. Boston:Brooks/Cole, Cengage Learning, 2010. Textbook.
3. Crystal structure of textilin-1, a Kunitz-type serine protease inhibitor from the venom of the Australian common brown snake (Pseudonaja textilis). Millers, Emma-Karin I., Trabi, Manuela, Masci, Paul P., Lavin, Martin F., Jersey, John de, and Guddat, Luke W. FEBS Journal 276 (2009) 3163-3175.
4. A Highly Destabilizing Mutation, G37A, of the Bovine Pancreatic Trypsin Inhibitor Retains the Average Native Conformation but Greatly Increases Local Flexibility. Battiste, John L., Li, Renhao, and Woodward, Clare. Biochemistry. 41 (2002) 2237-2245.
5. Holm L, Rosenström P (2010) Dali server: conservation mapping in 3D. Nucl. Acids Res. 38, W545-549.
6. Protein Self-Association in Solution: The Bovine Pancreatic Trypsin Inhibitor Decamer. Gottschalk, Michael, Venu, Kandadai, Halle, Bertil. Biophysical Journal. 84 (2003) 3941-3958.
7. The Bovine Basic Pancreatic Trypsin Inhibitor (Kunitz Inhibitor): A Milestone Protein. Ascenzi, Paolo, Bocedi, Alessio, Bolognesi, Martino, Spallarossa, Andrea, Coletta, Massimo, De Cristofaro, Raimondo, Menegatti, Enea. Current Protein and Peptide Science. 4 (2003) 231-251.
8. Biochemistry and Applications of Aprotinin, the Kallikrein Inhibitor from Bovine Organs. Fritz, H., Wunder, G. Arzneimittel Forschung. 33 (1983) 479-494.