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Results: 1-3 |
Results: 3
Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease
Authors: Guncar, G Klemencic, I Turk, B Turk, V Karaoglanovic-Carmona, A Juliano, L Turk, D
Citation: G. Guncar et al., Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease, STRUCT F D, 8(3), 2000, pp. 305-313
Biochemical characterization of human cathepsin X revealed that the enzymeis an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase
Authors: Klemencic, I Carmona, AK Cezari, MHS Juliano, MA Juliano, L Guncar, G Turk, D Krizaj, I Turk, V Turk, B
Citation: I. Klemencic et al., Biochemical characterization of human cathepsin X revealed that the enzymeis an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase, EUR J BIOCH, 267(17), 2000, pp. 5404-5412
Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsinsL and S
Authors: Guncar, G Pungercic, G Klemencic, I Turk, V Turk, D
Citation: G. Guncar et al., Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsinsL and S, EMBO J, 18(4), 1999, pp. 793-803
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