Dolenc I - Search Results

1

Crystal structure of Stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases.

Jenko S, Dolenc I, Guncar G, Dobersek A, Podobnik M, Turk D. Jenko S, et al. Among authors: dolenc i. J Mol Biol. 2003 Feb 21;326(3):875-85. doi: 10.1016/s0022-2836(02)01432-8. J Mol Biol. 2003. PMID: 12581647

2

Individual recombinant thyroglobulin type-1 domains are substrates for lysosomal cysteine proteinases.

Pungercic G, Dolenc I, Dolinar M, Bevec T, Jenko S, Kolaric S, Turk V. Pungercic G, et al. Among authors: dolenc i. Biol Chem. 2002 Nov;383(11):1809-12. doi: 10.1515/BC.2002.202. Biol Chem. 2002. PMID: 12530546

3

Human cathepsin X/Z is a biologically active homodimer.

Dolenc I, Štefe I, Turk D, Taler-Verčič A, Turk B, Turk V, Stoka V. Dolenc I, et al. Biochim Biophys Acta Proteins Proteom. 2021 Feb;1869(2):140567. doi: 10.1016/j.bbapap.2020.140567. Epub 2020 Nov 20. Biochim Biophys Acta Proteins Proteom. 2021. PMID: 33227497

4

The complete amino acid sequence of bovine cathepsin S and a partial sequence of bovine cathepsin L.

Ritonja A, Colić A, Dolenc I, Ogrinc T, Podobnik M, Turk V. Ritonja A, et al. Among authors: dolenc i. FEBS Lett. 1991 Jun 3;283(2):329-31. doi: 10.1016/0014-5793(91)80620-i. FEBS Lett. 1991. PMID: 2044774 Free article.

5

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: dolenc i. 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

6

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: dolenc i. Biochemistry. 1994 Dec 13;33(49):14800-6. doi: 10.1021/bi00253a019. Biochemistry. 1994. PMID: 7993907

7

Bovine cathepsins S and L: isolation and amino acid sequences.

Dolenc I, Ritonja A, Colić A, Podobnik M, Ogrinc T, Turk V. Dolenc I, et al. Biol Chem Hoppe Seyler. 1992 Jul;373(7):407-12. doi: 10.1515/bchm3.1992.373.2.407. Biol Chem Hoppe Seyler. 1992. PMID: 1515067

8

N-terminally truncated forms of human cathepsin F accumulate in aggresome-like inclusions.

Jerič B, Dolenc I, Mihelič M, Klarić M, Zavašnik-Bergant T, Gunčar G, Turk B, Turk V, Stoka V. Jerič B, et al. Among authors: dolenc i. Biochim Biophys Acta. 2013 Oct;1833(10):2254-66. doi: 10.1016/j.bbamcr.2013.05.007. Epub 2013 May 14. Biochim Biophys Acta. 2013. PMID: 23684953 Free article.

9

Inhibition of papain-like cysteine proteases and legumain by caspase-specific inhibitors: when reaction mechanism is more important than specificity.

Rozman-Pungercar J, Kopitar-Jerala N, Bogyo M, Turk D, Vasiljeva O, Stefe I, Vandenabeele P, Brömme D, Puizdar V, Fonović M, Trstenjak-Prebanda M, Dolenc I, Turk V, Turk B. Rozman-Pungercar J, et al. Among authors: dolenc i. Cell Death Differ. 2003 Aug;10(8):881-8. doi: 10.1038/sj.cdd.4401247. Cell Death Differ. 2003. PMID: 12867995

10

Cathepsin L is capable of truncating cystatin C of 11 N-terminal amino acids.

Popovic T, Cimerman N, Dolenc I, Ritonja A, Brzin J. Popovic T, et al. Among authors: dolenc i. FEBS Lett. 1999 Jul 16;455(1-2):92-6. doi: 10.1016/s0014-5793(99)00824-8. FEBS Lett. 1999. PMID: 10428479 Free article.

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