I. Dolenc

V. Turk, I. Dolenc, D. Gabrijelčič, 1992, European journal of clinical chemistry and clinical biochemistry : journal of the Forum of European Clinical Chemistry Societies.

Cathepsin D inactivates cysteine proteinase inhibitors, cystatins.

J. Kos, B. Lenarčič, V. Turk, 1988, Biochemical and biophysical research communications.

Tumor Necrosis Factor‐α Induced Apoptosis in U937 Cells Promotes Cathepsin D‐Independent Stefin B Degradation

V. Turk, I. Dolenc, B. Turk, 2017, Journal of cellular biochemistry.

Individual Recombinant Thyroglobulin Type-1 Domains Are Substrates for Lysosomal Cysteine Proteinases

V. Turk, I. Dolenc, Saša Jenko, 2002, Biological chemistry.

Human recombinant pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic processing.

V. Turk, I. Dolenc, B. Turk, 2001, Biochemistry.

Cathepsin C and plasma glutamate carboxypeptidase secreted from Fischer rat thyroid cells liberate thyroxin from the N-terminus of thyroglobulin.

V. Turk, I. Dolenc, B. Turk, 2012, Biochimie.

Characterization and structure of pineapple stem inhibitor of cysteine proteinases.

B. Lenarčič, V. Turk, I. Dolenc, 1992, Biological chemistry Hoppe-Seyler.

Oligomeric Structure and Substrate Induced Inhibition of Human Cathepsin C (*)

V. Turk, I. Dolenc, B. Turk, 1995, The Journal of Biological Chemistry.

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.

D. Turk, G. Guncar, I. Dolenc, 2003, Journal of molecular biology.

Human cathepsin X/Z is a biologically active homodimer.

D. Turk, V. Turk, I. Štefe, 2020, Biochimica et biophysica acta. Proteins and proteomics.

Aspartic cathepsin D degrades the cytosolic cysteine cathepsin inhibitor stefin B in the cells.

V. Turk, I. Dolenc, T. Železnik, 2015, Biochemical and biophysical research communications.

Bovine stefin C, a new member of the stefin family.

V. Turk, I. Dolenc, B. Turk, 1993, Journal of Biological Chemistry.

Decelerated degradation of short peptides by the 20S proteasome

W Baumeister, W. Baumeister, I. Dolenc, 1998, FEBS letters.

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

V. Turk, I. Dolenc, A. Colic, 1991, FEBS letters.

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

V. Turk, G. Guncar, I. Dolenc, 2013, Biochimica et biophysica acta.

Human cathepsin B is a metastable enzyme stabilized by specific ionic interactions associated with the active site.

D. Turk, V. Turk, I. Dolenc, 1994, Biochemistry.

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

V. Turk, I. Dolenc, A. Colic, 1992, Biological chemistry Hoppe-Seyler.

Biochemical characterization and structural modeling of human cathepsin E variant 2 in comparison to the wild-type protein

A. Sali, U. Pieper, N. Eswar, 2012, Biological chemistry.

Subunit topology of the Rhodococcus proteasome

W Baumeister, W. Baumeister, I. Dolenc, 1997, FEBS letters.

Feedback Regulation of Cathepsin C by the Propeptide Dipeptides of Granzymes A and B.

I. Dolenc, J. Božič, 2019, Acta chimica Slovenica.

Menadione‐induced apoptosis in U937 cells involves Bid cleavage and stefin B degradation

I. Dolenc, V. Stoka, J. Božič, 2019, Journal of cellular biochemistry.

Interaction of human cathepsin C with chicken cystatin

J. Kos, V. Turk, I. Dolenc, 1996, FEBS letters.

Pig leukocyte cysteine proteinase inhibitor (PLCPI), a new member of the stefin family

B. Lenarčič, V. Turk, B. Strukelj, 1993, FEBS letters.

The fluorogenic peptide substrate for cathepsin S

V. Turk, I. Dolenc, A. C̆olić, 1993 .