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Lysosomal cysteine proteases: more than scavengers.
Turk B, Turk D, Turk V. Turk B, et al. Among authors: turk d, turk v. Biochim Biophys Acta. 2000 Mar 7;1477(1-2):98-111. doi: 10.1016/s0167-4838(99)00263-0. Biochim Biophys Acta. 2000. PMID: 10708852 Review.
Isolation and characterization of bovine stefin B.
Turk B, Krizaj I, Turk V. Turk B, et al. Among authors: turk v. Biol Chem Hoppe Seyler. 1992 Jul;373(7):441-6. doi: 10.1515/bchm3.1992.373.2.441. Biol Chem Hoppe Seyler. 1992. PMID: 1515072
The most interesting feature of bovine stefin B is the replacement of the highly conserved QVVAG region in stefins with the QLVAG sequence without interfering its inhibitory properties....
The most interesting feature of bovine stefin B is the replacement of the highly conserved QVVAG region in stefins with the QLVAG seq …
Characterization and structure of pineapple stem inhibitor of cysteine proteinases.
Lenarcic B, Ritonja A, Turk B, Dolenc I, Turk V. Lenarcic B, et al. Among authors: turk b, turk v. Biol Chem Hoppe Seyler. 1992 Jul;373(7):459-64. doi: 10.1515/bchm3.1992.373.2.459. Biol Chem Hoppe Seyler. 1992. PMID: 1515075
Regulation of the activity of lysosomal cysteine proteinases by pH-induced inactivation and/or endogenous protein inhibitors, cystatins.
Turk B, Bieth JG, Björk I, Dolenc I, Turk D, Cimerman N, Kos J, Colic A, Stoka V, Turk V. Turk B, et al. Among authors: turk d, turk v. Biol Chem Hoppe Seyler. 1995 Apr;376(4):225-30. doi: 10.1515/bchm3.1995.376.4.225. Biol Chem Hoppe Seyler. 1995. PMID: 7626231
From log kinac vs pH plots, 3.0 and 1.7 protons were calculated to be desorbed for pH-induced inactivation of cathepsins L and B. Cathepsin B was thus substantially more stable than cathepsin L (approximately 15-fold at pH 7.0 and 37 degrees C). Cathepsin B w …
From log kinac vs pH plots, 3.0 and 1.7 protons were calculated to be desorbed for pH-induced inactivation of cathepsins L and B. Cat …
Oligomeric structure and substrate induced inhibition of human cathepsin C.
Dolenc I, Turk B, Pungercic G, Ritonja A, Turk V. Dolenc I, et al. Among authors: turk b, turk v. J Biol Chem. 1995 Sep 15;270(37):21626-31. doi: 10.1074/jbc.270.37.21626. J Biol Chem. 1995. PMID: 7665576
Kinetics of the pH-induced inactivation of human cathepsin L.
Turk B, Dolenc I, Turk V, Bieth JG. Turk B, et al. Among authors: turk v. Biochemistry. 1993 Jan 12;32(1):375-80. doi: 10.1021/bi00052a046. Biochemistry. 1993. PMID: 7678196
The rate of inhibition of cathepsin L by stefin B or chicken cystatin at pH 7.4 was much faster than the rate of spontaneous inactivation of the enzyme. The stefin B-cathepsin L complex incubated at pH 7.4 released active enzyme at pH 5.5, suggesting that the cystei …
The rate of inhibition of cathepsin L by stefin B or chicken cystatin at pH 7.4 was much faster than the rate of spontaneous inactiva …
Identification of bovine stefin A, a novel protein inhibitor of cysteine proteinases.
Turk B, Ritonja A, Björk I, Stoka V, Dolenc I, Turk V. Turk B, et al. Among authors: turk v. FEBS Lett. 1995 Feb 27;360(2):101-5. doi: 10.1016/0014-5793(95)00060-m. FEBS Lett. 1995. PMID: 7875311
For the first time, three different stefins, A, B and C, have been isolated from a single species. The complete amino acid sequence of bovine stefin A was determined. ...In contrast, the binding to cathepsin B was much slower (kass = 1.4 x 10(5) M-1.s-1), but still …
For the first time, three different stefins, A, B and C, have been isolated from a single species. The complete amino acid sequence o …
Human cathepsin B is a metastable enzyme stabilized by specific ionic interactions associated with the active site.
Turk B, Dolenc I, Zerovnik E, Turk D, Gubensek F, Turk V. Turk B, et al. Among authors: turk d, turk v. Biochemistry. 1994 Dec 13;33(49):14800-6. doi: 10.1021/bi00253a019. Biochemistry. 1994. PMID: 7993907
Both the pH-induced inactivation and the pH-induced unfolding of cathepsin B were found to be first-order processes, exponentially increasing with increasing pH of the solution. ...Cathepsin B was also found to be destabilized both by increasing ionic strength and o …
Both the pH-induced inactivation and the pH-induced unfolding of cathepsin B were found to be first-order processes, exponentially in …
Stefin B, the major low molecular weight inhibitor in ovarian carcinoma.
Kastelic L, Turk B, Kopitar-Jerala N, Stolfa A, Rainer S, Turk V, Lah TT. Kastelic L, et al. Among authors: turk b, turk v. Cancer Lett. 1994 Jul 15;82(1):81-8. doi: 10.1016/0304-3835(94)90149-x. Cancer Lett. 1994. PMID: 8033073
Ovarian carcinoma contain high levels of Stefin B and about twentyfold less Stefin A compared to normal epithelial tissue. Stefin B was isolated and characterized. ...As these properties are similar to Stefin B from human and bovine origin, as well as to Stef …
Ovarian carcinoma contain high levels of Stefin B and about twentyfold less Stefin A compared to normal epithelial tissue. Stefin …
Kinetics of inhibition of bovine cathepsin S by bovine stefin B.
Turk B, Colić A, Stoka V, Turk V. Turk B, et al. Among authors: turk v. FEBS Lett. 1994 Feb 14;339(1-2):155-9. doi: 10.1016/0014-5793(94)80405-2. FEBS Lett. 1994. PMID: 8313966
The kinetics of the complex formation between bovine cathepsin S and bovine stefin B was studied by conventional and stopped-flow techniques. ...
The kinetics of the complex formation between bovine cathepsin S and bovine stefin B was studied by conventional and stopped-flow tec …
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