V. Turk

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

STRUCTURAL AND DENATURATION STUDIES OF CATHEPSIN D AND THE EXISTENCE OF ITS POSSIBLE PRECURSOR

V. Turk, V. Puizdar, F. Gubensek, 1981 .

Stem bromelain: Amino acid sequence and implications for weak binding of cystatin

N. Rawlings, A. Barrett, V. Turk, 1989, FEBS letters.

Cathepsin D inactivates cysteine proteinase inhibitors, cystatins.

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

Structure-based development of pyridoxal propionate derivatives as specific inhibitors of cathepsin K in vitro and in vivo.

D. Turk, V. Turk, N. Katunuma, 2000, Biochemical and biophysical research communications.

The major cysteine proteinase of Trypanosoma cruzi: a valid target for chemotherapy of Chagas disease.

V. Turk, V. Stoka, J. José Cazzulo, 2001, Current pharmaceutical design.

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.

Novel aspartyl proteinase associated to fat body histolysis during Ceratitis capitata early metamorphosis.

V. Turk, V. Puizdar, V. Stoka, 2004, Archives of insect biochemistry and physiology.

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

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

Amino-acid sequence of ammodytoxin B partially reveals the location of the site of toxicity of ammodytoxins.

V. Turk, W. Machleidt, F. Gubensek, 1986, Biological chemistry Hoppe-Seyler.

Inhibitory p41 isoform of invariant chain and its potential target enzymes cathepsins L and H in distinct populations of macrophages in human lymph nodes

J. Kos, A. Schweiger, R. Golouh, 2004, Immunology.

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.

4 Human Cysteine Proteinases and Their Inhibitors, Stefins and Cystatins

W. Bode, V. Turk, 1994 .

Lysosomal cysteine proteases: facts and opportunities

D. Turk, V. Turk, B. Turk, 2001, The EMBO journal.

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.

MAGUKs, scaffolding proteins at cell junctions, are substrates of different proteases during apoptosis

D. Bredt, P. Vandenabeele, L. Banks, 2011, Cell Death and Disease.

Critical Review The p41 Fragment Story

V. Turk, 1999 .

Cathepsin D: rapid isolation by affinity chromatography on haemoglobin-agarose resin.

V. Turk, R. Smith, R. Smith, 1974, European journal of biochemistry.

Amino acid sequences of the human kidney cathepsins H and L

V. Turk, W. Machleidt, T. Popović, 1988, FEBS letters.

Chicken egg white cystatin as a ligand for affinity chromatography

J. Kos, V. Turk, A. Maksimenko, 1986 .

Interactions between a viral protease and cystatins.

B. Lenarčič, V. Turk, T. Towatari, 1988, Biological chemistry Hoppe-Seyler.

Proteases New Perspectives

V. Turk, 1999, MCBU Molecular and Cell Biology Updates.

Human plasma kininogens are identical with alpha-cysteine proteinase inhibitors. Evidence from immunological, enzymological and sequence data.

V. Turk, F. Lottspeich, J. Kellermann, 1985, FEBS letters.

INHIBITION OF TRYPSIN AND CHYMOTRYPSIN BY INHIBITORS FROM VIPERA AMMODYTES VENOM

V. Turk, F. Gubensek, A. Ritonja, 1981 .

Participation of cathepsin L on bone resorption

B. Lenarčič, V. Turk, N. Katunuma, 1993, FEBS letters.

Detection of cathepsin L-like proteinase and cathepsin D in gingival fluid.

V. Turk, U. Skalerič, T. Lah, 1986, Journal of periodontal research.

Apoptotic Pathways: Involvement of Lysosomal Proteases

V. Turk, J. Rozman-Pungercar, B. Turk, 2002, Biological chemistry.

Human immunodeficiency virus has an aspartic-type protease that can be inhibited by pepstatin A.

V. Turk, V Turk, S Seelmeier, 1988, Proceedings of the National Academy of Sciences of the United States of America.

Inhibitory effect of carnosolic acid on HIV-1 protease in cell-free assays

V. Turk, B. Strukelj, M. Renko, 1993 .

cystatins: protein inhibitors of cysteine proteinases

W. Bode, V. Turk, Wolfram Bode, 2001 .

Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function.

D. Turk, V. Turk, G. Guncar, 1998, Structure.

Effects of proteinase inhibitors on digestive proteinases and growth of the red flour beetle, Tribolium castaneum (Herbst) (Coleoptera: Tenebrionidae).

K. Ohtsubo, B. Lenarčič, V. Turk, 2003, Comparative biochemistry and physiology. Toxicology & pharmacology : CBP.

The primary structure of inhibitor of cysteine proteinases from potato

V. Turk, R. Jerala, I. Križaj, 1993, FEBS letters.

Lysosomal cysteine proteases: more than scavengers.

D. Turk, V. Turk, B. Turk, 2000, Biochimica et biophysica acta.

Lysosomal cathepsins and their regulation in aging and neurodegeneration

V. Turk, B. Turk, V. Stoka, 2016, Ageing Research Reviews.

Amyloid fibril formation by human stefin B: influence of the initial pH-induced intermediate state.

J. Waltho, V. Turk, E. Žerovnik, 2001, Biochemical Society transactions.

Variations in MHC Class II Antigen Processing and Presentation in Health and Disease.

E. Unanue, J. Neefjes, V. Turk, 2016, Annual review of immunology.

Characterization and structure of pineapple stem inhibitor of cysteine proteinases.

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

Differences in the effects of TFE on the folding pathways of human stefins A and B

J. Waltho, V. Turk, R. Jerala, 1999, Proteins.

On the mechanism of human stefin B folding: I. Comparison to homologous stefin A. Influence of pH and trifluoroethanol on the fast and slow folding phases

J. Waltho, V. Turk, R. Jerala, 1998, Proteins.

Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases

D Lamba, D. Turk, V. Turk, 2001, The EMBO journal.

Cystatins: biochemical and structural properties, and medical relevance.

D. Turk, V. Turk, V. Stoka, 2008, Frontiers in bioscience : a journal and virtual library.

Equistatin, a New Inhibitor of Cysteine Proteinases fromActinia equina, Is Structurally Related to Thyroglobulin Type-1 Domain*

B. Lenarčič, V. Turk, B. Strukelj, 1997, The Journal of Biological Chemistry.

Fractionation of Vipera ammodytes venom and seasonal variation of its composition.

V. Turk, F. Gubensek, D. Lebez, 1974, Toxicon : official journal of the International Society on Toxinology.

Inactivation of human cystatin C and kininogen by human cathepsin D

Isleifur Olafsson, I. Olafsson, B. Lenarčič, 1991, FEBS letters.

Metacaspases of Trypanosoma cruzi: possible candidates for programmed cell death mediators.

D. Sánchez, Fernán Agüero, V. Turk, 2006, Molecular and biochemical parasitology.

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

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

The refined 2.15 A X‐ray crystal structure of human liver cathepsin B: the structural basis for its specificity.

Robert Huber, Richard A. Engh, Djordje Musil, 1991, The EMBO journal.

The amino acid sequence of a novel inhibitor of cathepsin D from potato

A. Barrett, V. Turk, B. Strukelj, 1990, FEBS letters.

Lysosomal Protease Pathways to Apoptosis

L. Ellerby, John Calvin Reed, H. Freeze, 2001, The Journal of Biological Chemistry.

Cysteine Cathepsins Trigger Caspase-dependent Cell Death through Cleavage of Bid and Antiapoptotic Bcl-2 Homologues*

G. Salvesen, V. Turk, B. Turk, 2008, Journal of Biological Chemistry.

The refined 2.4 A X‐ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction.

R. Huber, W. Bode, B. Lenarčič, 1990, The EMBO journal.

Human Leucocyte Urokinase Inhibitor - Purification, Characterization and Comparative Studies Against Different Plasminogen Activators

V. Turk, B. Rozman, J. Babnik, 1985, Thrombosis and Haemostasis.

Lysosomes and lysosomal cathepsins in cell death.

V. Turk, B. Turk, V. Stoka, 2012, Biochimica et biophysica acta.

Ferri-liposomes as an MRI-visible drug-delivery system for targeting tumours and their microenvironment.

Christoph Peters, Matthew Bogyo, Olga Vasiljeva, 2011, Nature nanotechnology.

Non-invasive in vivo imaging of tumour-associated cathepsin B by a highly selective inhibitory DARPin

O. Vasiljeva, D. Turk, M. Grütter, 2017, Theranostics.

Expression and activity profiling of selected cysteine cathepsins and matrix metalloproteinases in synovial fluids from patients with rheumatoid arthritis and osteoarthritis

V. Turk, B. Turk, B. Rozman, 2010, Biological chemistry.

Autocatalytic processing of recombinant human procathepsin B is a bimolecular process

V. Turk, B. Turk, J. Stojan, 1999, FEBS letters.

Crystal structure of the wild-type human procathepsin B at 2.5 A resolution reveals the native active site of a papain-like cysteine protease zymogen.

D. Turk, V. Turk, M. Podobnik, 1997, Journal of molecular biology.

Crystal structures of human procathepsin B at 3.2 and 3.3 Å resolution reveal an interaction motif between a papain‐like cysteine protease and its propeptide

D. Turk, V. Turk, M. Dolinar, 1996, FEBS letters.

Crystal structure of cathepsin B inhibited with CA030 at 2.0-A resolution: A basis for the design of specific epoxysuccinyl inhibitors.

R. Huber, D. Turk, W. Bode, 1995, Biochemistry.

The 2.0 A X‐ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases.

W. Bode, R. Huber, J. Kos, 1988, The EMBO journal.

Stefin B deficiency reduces tumor growth via sensitization of tumor cells to oxidative stress in a breast cancer model

O. Vasiljeva, A. Krüger, C. Peters, 2014, Oncogene.

Methodologic Problems Encountered in the Assay of Proteinases in Lewis Lung Carcinoma, a Mouse Metastasizing Tumor

A. Baici, V. Turk, G. Sava, 1982, Tumori.

Biochemical and biological characteristics of leucocyte proteinase inhibitors.

M. Korbelik, V. Turk, S. Svetina, 1982, Advances in experimental medicine and biology.

Antimetastatic effects and tumor proteinase inhibition by spleen intracellular inhibitors of neutral proteinases.

V. Turk, G. Sava, J. Brzin, 1981, European journal of cancer & clinical oncology.

INTRACELLULAR NEUTRAL PROTEINASES AND INHIBITORS

V. Turk, J. Brzin, J. Babnik, 1981 .

Biochemical and biological properties of leukocyte intracellular inhibitors of proteinases.

V. Turk, T. Giraldi, M. Kopitar, 1979, Advances in experimental medicine and biology.

Inhibition studies of an intracellular inhibitor on thiol proteinases.

V. Turk, J. Brzin, I. Kregar, 1978, FEBS letters.

Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors.

D. Turk, V. Turk, B. Turk, 1997, Biological chemistry.

Diversity and evolution of the thyroglobulin type-1 domain superfamily.

Marko Novinec, B. Lenarčič, V. Turk, 2006, Molecular biology and evolution.

Intracellular aggregation of human stefin B: confocal and electron microscopy study

V. Turk, N. Kopitar-Jerala, R. Layfield, 2010, Biology of the cell.

In vitro study of stability and amyloid‐fibril formation of two mutants of human stefin B (cystatin B) occurring in patients with EPM1

V. Turk, E. Žerovnik, Sabina Rabzelj, 2005, Protein Science.

Amyloid Fibril Formation by Human Stefin B in vitro: Immunogold Labelling and Comparison to Stefin A

V. Turk, K. Goldie, N. Kopitar-Jerala, 2002, Biological chemistry.

Cysteine proteinases and inhibitors in inflammation: their role in periodontal disease.

V. Turk, U. Skalerič, T. Lah, 1993, Journal of periodontology.

Cloning a synthetic gene for human stefin B and its expression in E. coli

B. Lenarčič, V. Turk, R. Jerala, 1988, FEBS letters.

A Thiol Dependent Acid Protease

V. Turk, I. Kregar, D. Lebez, 1977 .

High‐molecular‐weight kininogen binds two molecules of cysteine proteinases with different rate constants

V. Turk, B. Turk, V. Stoka, 1996, FEBS letters.

Intracellular Protein Catabolism II

A. Barrett, J. Woessner, V. Turk, 1977, Springer US.

The expression of lysosomal proteinases and their inhibitors in breast cancer: Possible relationship to prognosis of the disease

A. Blejec, J. Kos, R. Golouh, 2008, Pathology & Oncology Research.

Crystal structure of MHC class II‐associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S

D. Turk, V. Turk, G. Guncar, 1999, The EMBO journal.

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.

Kinetics of inhibition of bovine cathepsin S by bovine stefin B

V. Turk, B. Turk, V. Stoka, 1994, FEBS letters.

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

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

Isolation of kininogens using affinity chromatography

V. Turk, W. Machleidt, J. Brzin, 1986 .

Selective cleavage of glycyl bonds by papaya proteinase IV

L. Pearl, A. Barrett, V. Turk, 1990, FEBS letters.

Recombinant Anti-Stefin A Fab Fragment: Sequence Analysis of the Variable Region and Expression in Escherichia coli

V. Turk, N. Kopitar-Jerala, F. Gubenek, 2000, Biological chemistry.

Cruzipain, the major cysteine proteinase from the protozoan parasite Trypanosoma cruzi.

V. Turk, V. Stoka, J. Cazzulo, 1997, Biological chemistry.

Increased expression and altered subcellular distribution of cathepsin B in microglia induce cognitive impairment through oxidative stress and inflammatory response in mice

H. Nakanishi, C. Peters, H. Qing, 2018, Aging cell.

Blocking autophagy to prevent parasite differentiation: A possible new strategy for fighting parasitic infections?

V. Turk, B. Turk, J. Cazzulo, 2008, Autophagy.

Lysosomes as “Suicide Bags” in Cell Death: Myth or Reality?*

V. Turk, B. Turk, 2009, The Journal of Biological Chemistry.

Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease.

D. Turk, L. Juliano, V. Turk, 2000, Structure.

A procathepsin D specific monoclonal antibody that recognizes procathepsin D but not cathepsin D.

V. Turk, N. Kopitar-Jerala, 2000, Immunology letters.

Emerging roles of cysteine cathepsins in disease and their potential as drug targets.

O. Vasiljeva, C. Peters, T. Reinheckel, 2007, Current pharmaceutical design.

pH-induced Conformational Transitions of the Propeptide of Human Cathepsin L

V. Turk, R. Jerala, E. Žerovnik, 1998, The Journal of Biological Chemistry.

Lysosomal proteases cathepsins D, B, H, L and their inhibitors stefins A and B in head and neck cancer.

J. Kos, B. Lenarčič, V. Turk, 1995, Biological chemistry Hoppe-Seyler.

Size and morphology of toxic oligomers of amyloidogenic proteins: a case study of human stefin B

D. Turk, V. Turk, G. Anderluh, 2008, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis.

Interaction between Oligomers of Stefin B and Amyloid-β in Vitro and in Cells*

V. Turk, V. Hodnik, G. Anderluh, 2009, The Journal of Biological Chemistry.

Purification and some properties of the cathepsin from the small intestinal mucosa of pig.

V. Turk, I. Kregar, D. Lebez, 1967, Enzymologia.

The effect of intracellular proteinases on transformation of human lymphocytes.

M. Korbelik, V. Turk, P. Schauer, 1986, Advances in experimental medicine and biology.

Rapid affinity chromatographic method for the isolation of human cathepsin H.

V. Turk, T. Popović, J. Brzin, 1993, Journal of chromatography.

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.

Papaya proteinase IV amino acid sequence

N. Rawlings, A. Barrett, V. Turk, 1989, 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.

22 – Structure and Chemistry of Lysozyme: pH-Rate Profile, Calorimetric Studies, and Computations on Exposure to Solvent*

V. Turk, A. Shrake, J. A. Rupley, 1974 .

Collagenolytic cathepsins of rabbit spleen: a kinetic analysis of collagen degradation and inhibition by chicken cystatin.

R. Maciewicz, J. Kos, V. Turk, 1987, Collagen and related research.

Determination of Cathepsins B and H in Sera and Synovial Fluids of Patients with Different Joint Diseases

V. Turk, B. Rozman, D. Gabrijelčič, 1990, Journal of clinical chemistry and clinical biochemistry. Zeitschrift fur klinische Chemie und klinische Biochemie.

Phylogenomic analysis of the cystatin superfamily in eukaryotes and prokaryotes

V. Turk, D. Kordis, 2009, BMC Evolutionary Biology.

Cystatins and stefins in ascites fluid from ovarian carcinoma.

V. Turk, T. Lah, L. Kastelic, 1992, Cancer letters.

A new purification procedure of human kidney cathepsin H, its properties and kinetic data.

J. Kos, B. Lenarčič, V. Turk, 1988, Biological chemistry Hoppe-Seyler.

Human cathepsin B and cysteine proteinase inhibitors (CPIs) in inflammatory and metabolic joint diseases.

B. Lenarčič, V. Turk, B. Rozman, 1988, Biological chemistry Hoppe-Seyler.

The mammalian cysteine proteinase inhibitors. Structural diversity and evolutionary origin

V. Turk, F. Lottspeich, J. Kellermann, 1986 .

Human cathepsins B, H and L: characterization by amino acid sequences and some kinetics of inhibition by the kininogens

V. Turk, W. Machleidt, W. Müller-Esterl, 1986 .

The possibility of differentiation of cathepsins on the basis of their ability to degrade various protein substrates.

V. Turk, I. Kregar, D. Lebez, 1968, Enzymologia.

Some properties of cathepsin E from bovine spleen.

V. Turk, I. Kregar, D. Lebez, 1968, Enzymologia.

CARBOXYL AND THIOL INTRACELLULAR PROTEINASES

V. Turk, F. Gubensek, T. Lah, 1980 .

Application of Crumpled Aluminum Hydroxide Nanostructures for Cancer Treatment

O. Vasiljeva, V. Turk, B. Turk, 2020, Springer Tracts in Mechanical Engineering.

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.

Complete primary structure of lamb preprochymosin deduced from cDNA.

V. Turk, B. Strukelj, F. Gubensek, 1990, Nucleic Acids Research.

Amino acid sequence of lamb preprochymosin and its comparison to other chymosins.

V. Turk, B. Strukelj, F. Gubensek, 1991, Advances in experimental medicine and biology.

Denaturation of stefin B by GuHCl, pH and heat; evidence for molten globule intermediates.

R. Pain, V. Turk, R. Jerala, 1992, Biological chemistry Hoppe-Seyler.

Interactions of papaya proteinase IV with inhibitors

A. Barrett, V. Turk, E. Shaw, 1990, FEBS letters.

Nucleotide and deduced amino acid sequence of an aspartic proteinase inhibitor homologue from potato tubers (Solanum tuberosum L.).

V. Turk, B. Strukelj, I. Križaj, 1990, Nucleic acids research.

Rapid isolation of cathepsin D by affinity chromatography on the immobilized synthetic inhibitor

V. Turk, F. Gubensek, I. Kregar, 1976, FEBS letters.

Molecular cloning and immunocytochemical localization of jasmonic acid inducible cathepsin D inhibitors from potato.

V. Turk, B. Strukelj, M. Ravnikar, 1995, Advances in experimental medicine and biology.

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.

Mechanism of interaction of cysteine proteinases and their protein inhibitors as compared to the serine proteinase-inhibitor interaction.

R. Huber, W. Bode, R. Engh, 1990, Biological chemistry Hoppe-Seyler.

Equistatin, a protease inhibitor from the sea anemone actinia equina, is composed of three structural and functional domains.

K. Gruden, D. Bosch, B. Lenarčič, 2000, Biochemical and biophysical research communications.

Conformation and processing of cathepsin D

R. Pain, V. Turk, Tamara Lan, 1985, Bioscience reports.

Lysozyme-catalyzed reaction of the N-acetylglucosamine hexasaccharide. Dependence of rate on pH.

V. Turk, J. A. Rupley, S. Banerjee, 1973, The Journal of biological chemistry.

Intermediates in denaturation of a small globular protein, recombinant human stefin B.

R. Pain, V. Turk, R. Jerala, 1992, The Journal of biological chemistry.

Mechanisms of amyloid fibril formation – focus on domain‐swapping

D. Turk, J. Grdadolnik, V. Turk, 2011, The FEBS journal.

Human cathepsin F: expression in baculovirus system, characterization and inhibition by protein inhibitors

V. Turk, D. Brömme, B. Turk, 2004, Biological chemistry.

Selective Targeting of Tumor and Stromal Cells By a Nanocarrier System Displaying Lipidated Cathepsin B Inhibitor

O. Vasiljeva, V. Turk, M. Fonović, 2014, Angewandte Chemie.

Special issue: Proteolysis 50 years after the discovery of lysosome in honor of Christian de Duve.

V. Turk, 2012, Biochimica et biophysica acta.

On the mechanism of human stefin B folding: II. Folding from GuHCl unfolded, TFE denatured, acid denatured, and acid intermediate states

J. Waltho, V. Turk, R. Jerala, 1998, Proteins.

Lysosomal cysteine proteinases: Structure and regulation

D. Turk, V. Turk, G. Guncar, 1999 .

Increased expression of stefin B in the nucleus of T98G astrocytoma cells delays caspase activation

V. Turk, N. Kopitar-Jerala, B. Turk, 2012, Front. Mol. Neurosci..

STREPTOMYCES RIMOSUS ALKALINE AND TRYPSIN-LIKE SERINE PROTEINASES

V. Turk, L. Vitale, M. Longer, 1981 .

Inhibitory effect of carnosic acid on HIV-1 protease in cell-free assays [corrected].

V. Turk, B. Strukelj, M. Renko, 1993, Journal of natural products.

Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase.

D. Turk, L. Juliano, M. Juliano, 2000, European journal of biochemistry.

Inhibition mechanism of cathepsin L-specific inhibitors based on the crystal structure of papain-CLIK148 complex.

D. Turk, V. Turk, H. Tsuge, 1999, Biochemical and biophysical research communications.

The p41 Fragment Story

D. Turk, V. Turk, G. Guncar, 1999, IUBMB Life - A Journal of the International Union of Biochemistry and Molecular Biology.

Intracellular and extracellular cathepsin B facilitate invasion of MCF-10A neoT cells through reconstituted extracellular matrix in vitro.

J. Kos, V. Turk, Valentina Zavasnik-Bergant, 2003, Experimental cell research.

Comparative studies on fast acting PA-inhibitors from pig and human peripheral leucocytes.

V. Turk, R. Jerala, D. Gabrijelčič, 1989, Advances in experimental medicine and biology.

Crumpled Aluminum Hydroxide Nanostructures as a Microenvironment Dysregulation Agent for Cancer Treatment.

O. Vasiljeva, E. Gutmanas, V. Turk, 2018, Nano letters.

Cathepsin H deficiency decreases hypoxia-ischemia-induced hippocampal atrophy in neonatal mice through attenuated TLR3/IFN-β signaling

H. Nakanishi, T. Reinheckel, V. Turk, 2021, Journal of Neuroinflammation.

Theranostic Applications of an Ultra-Sensitive T1 and T2 Magnetic Resonance Contrast Agent Based on Cobalt Ferrite Spinel Nanoparticles

O. Vasiljeva, V. Turk, B. Turk, 2022, Cancers.

Regen: program for designing gene assembly.

V. Turk, R. Jerala, 1988, Nucleic acids research.

Interaction with model membranes and pore formation by human stefin B – studying the native and prefibrillar states

V. Turk, G. Anderluh, I. Gutiérrez-Aguirre, 2008, The FEBS journal.

Protein aggregation as a possible cause for pathology in a subset of familial Unverricht-Lundborg disease.

V. Turk, N. Kopitar-Jerala, E. Žerovnik, 2005, Medical hypotheses.

Human cysteine proteinases and their protein inhibitors stefins, cystatins and kininogens.

B. Lenarčič, V. Turk, W. Machleidt, 1986, Biomedica biochimica acta.

The pH dependence of breakdown of various purified brain proteins by cathepsin D preparations

A. Lajtha, F. Bracco, V. Turk, 1985, Neurochemistry International.

Conformational variability of chicken cystatin. Comparison of structures determined by X-ray diffraction and NMR spectroscopy.

R. Huber, W. Bode, R. Engh, 1993, Journal of molecular biology.

The mechanisms and regulation of procathepsin L secretion from osteoclasts in bone resorption

V. Turk, N. Katunuma, K. Sumitani, 1994, FEBS letters.

Mouse stefins A1 and A2 (Stfa1 and Stfa2) differentiate between papain‐like endo‐ and exopeptidases

D. Turk, V. Turk, C. Teuscher, 2006, FEBS letters.

Elongation on the amino-terminal part of stefin B decreases inhibition of cathepsin H.

V. Turk, R. Jerala, T. Popović, 1994, European journal of biochemistry.

Determination of cathepsins B, H, L and kininogen in breast cancer patients.

V. Turk, D. Gabrijelčič, J. Škrk, 1992, Agents and actions. Supplements.

Erratum to: Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) (Autophagy, 12, 1, 1-222, 10.1080/15548627.2015.1100356

Sara W. Bird, Erinna F. Lee, Michael D. Kim, 2016 .

Exoerythrocytic Plasmodium Parasites Secrete a Cysteine Protease Inhibitor Involved in Sporozoite Invasion and Capable of Blocking Cell Death of Host Hepatocytes

R. Hilgenfeld, V. Turk, V. Heussler, 2010, PLoS pathogens.

Selective activity-based probes for cysteine cathepsins.

V. Turk, B. Turk, H. Nestler, 2008, Angewandte Chemie.

The preparation of catalytically active human cathepsin B from its precursor expressed in Escherichia coli in the form of inclusion bodies.

V. Turk, J. Pungerčar, M. Dolinar, 1995, European journal of biochemistry.

Murine and human cathepsin B exhibit similar properties: possible implications for drug discovery

Thomas Reinheckel, T. Reinheckel, V. Turk, 2009, Biological chemistry.

Dual concentration-dependent activity of thyroglobulin type-1 domain of testican: specific inhibitor and substrate of cathepsin L

B. Lenarčič, A. Baici, V. Turk, 2005, Biological chemistry.

Conformation, structure and activation of bovine cathepsin D. Unfolding and refolding studies.

R. Pain, V. Turk, T. Lah, 1984, Biochemical Journal.

Prediction of the secondary structures of stefins and cystatins, the low-molecular mass protein inhibitors of cysteine proteinases.

A. Sali, V. Turk, 1987, Biological chemistry Hoppe-Seyler.

Cysteine cathepsins (proteases)--on the main stage of cancer?

J. Kos, V. Turk, B. Turk, 2004, Cancer cell.

Proteolytic cleavage of human fibrinogen by cathepsin B.

V. Turk, D. Gabrijelčič, T. Popović, 1988, Biological chemistry Hoppe-Seyler.

Compactness of the molten globule in comparison to unfolded states as observed by size-exclusion chromatography.

V. Turk, R. Jerala, E. Žerovnik, 1994, Biochimica et biophysica acta.

Purification and Some Properties of Native and Immobilized Cathepsin D

V. Turk, F. Gubensek, J. Babnik, 1977 .

Sequence and structure similarities of cathepsin B from the parasite Schistosoma mansoni and human liver

W. Bode, V. Turk, E. Shaw, 1994, FEBS letters.

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

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

Calorimetric measurements of thermal denaturation of stefins A and B. Comparison to predicted thermodynamics of stefin-B unfolding.

V. Turk, P. Laggner, R. Jerala, 1992, European journal of biochemistry.

Isolation and characterization of bovine stefin B.

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

The complete primary structure of bovine stefin B

V. Turk, B. Turk, I. Križaj, 1992, FEBS letters.

Autolysis studies of cathepsin D.

V. Turk, T. Lah, 1982, Hoppe-Seyler's Zeitschrift fur physiologische Chemie.

Low molecular mass protein inhibitor of cysteine proteinases from soybean.

V. Turk, T. Popović, J. Brzin, 1990, Biological chemistry Hoppe-Seyler.

Structural characterisation of human stefin A in solution and implications for binding to cysteine proteinases.

J. Waltho, V. Turk, R. Jerala, 1994, European journal of biochemistry.

Stoichiometry and heterogeneity of the pro-region chain in tetrameric human cathepsin C.

R. Pain, V. Turk, I. Križaj, 1998, Biochimica et biophysica acta.

BOVINE SPLEEN CATHEPSINS D AND S: PURIFICATION, CHARACTERIZATION, AND STRUCTURAL STUDIES

V. Turk, F. Gubensek, I. Kregar, 1978 .

The mechanism of amyloid‐fibril formation by stefin B: Temperature and protein concentration dependence of the rates

D. Turk, J. Waltho, V. Turk, 2009, Proteins.

Exclusion of the native alpha-helix from the amyloid fibrils of a mixed alpha/beta protein.

A. Hounslow, J. Waltho, V. Turk, 2008, Journal of molecular biology.

Differential regulation of the intrinsic pathway of apoptosis in brain and liver during ageing

D. Bredesen, V. Turk, V. Stoka, 2006, FEBS letters.

Cathepsin B and cysteine proteinase inhibitors in bronchoalveolar lavage fluid of lung cancer patients.

V. Turk, D. Gabrijelčič, T. Lah, 1993, Cancer detection and prevention.

Cystatins: biochemical and structural properties, and medical relevance.

D. Turk, V. Turk, V. Stoka, 2008 .

Origin and Early Diversification of the Papain Family of Cysteine Peptidases

V. Turk, D. Kordis, 2023, International journal of molecular sciences.

Interaction of human cathepsin C with chicken cystatin

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

Structural basis for the difference in thermodynamic properties between the two cysteine proteinase inhibitors human stefins A and B.

V. Turk, R. Jerala, K. Lohner, 1994, Protein engineering.

Papain-like lysosomal cysteine proteases and their inhibitors: drug discovery targets?

D. Turk, V. Turk, B. Turk, 2003, Biochemical Society symposium.

Structural elucidation and antiviral activity of cathepsin L inhibitors with carbonyl and epoxide warheads

H. Chapman, D. Turk, W. Hinrichs, 2023, bioRxiv.

Denaturation studies of aspartic proteinases.

R. Pain, V. Turk, T. Lah, 1985, Biochemical Society transactions.

The cysteine proteinase inhibitor chicken cystatin is a phosphoprotein

J. Kos, W. Bode, V. Turk, 1989, FEBS letters.

INTRACELLULAR NEUTRAL PROTEINASES AND THEIR INHIBITORS

V. Turk, J. Brzin, J. Babnik, 1980 .

Major differences in stability and dimerization properties of two chimeric mutants of human stefins

V. Turk, M. Kenig, R. Jerala, 2001, Proteins.

Evidence for the presence of large amounts of cathepsin E in rat spleen

V. Turk, V. Puizdar, C. Lapresle, 1985, FEBS letters.

Recombinant human procathepsin S is capable of autocatalytic processing at neutral pH in the presence of glycosaminoglycans

O. Vasiljeva, V. Turk, B. Turk, 2005, FEBS letters.

Substrate inhibition of cruzipain is not affected by the C‐terminal domain

V. Turk, J. McKerrow, V. Stoka, 1998, FEBS letters.

Lysosomes and lysosomal cathepsins in cell death.

V. Turk, B. Turk, V. Stoka, 2012, Biochimica et biophysica acta.

Cystatin C deficiency suppresses tumor growth in a breast cancer model through decreased proliferation of tumor cells

O. Vasiljeva, V. Turk, J. Završnik, 2017, Oncotarget.

Protease signalling: the cutting edge

D. Turk, V. Turk, B. Turk, 2012, The EMBO journal.

Isolation and characterisation of chicken L- and H-kininogens and their interaction with chicken cysteine proteinases and papain.

J. Kos, V. Turk, M. Dolinar, 1992, Agents and actions. Supplements.

Proteases : new perspectives

V. Turk, 1999 .

1. Characterization and Evaluation of Various Crude Preparations

V. Turk, Rudjer Bo, M. Renko, 1979 .

Immunological studies of intracellular leukocyte proteinase inhibitor by granular extract and cathepsin D.

V. Turk, J. Babnik, M. Kopitar, 1979, Advances in experimental medicine and biology.

Crystallization of chicken egg white cystatin, a low molecular weight protein inhibitor of cysteine proteinases, and preliminary X-ray diffraction data.

W. Bode, V. Turk, J. Brzin, 1985, Journal of molecular biology.

Modulation of contact order effects in the two-state folding of stefins A and B.

D. Turk, J. Waltho, D. Clarke, 2011, Biophysical journal.

Correlation Between Stability and Propensity to form Amyloid-Like Fibrils

V. Turk, M. Kenig, E. Žerovnik, 2004 .

cystatins: protein inhibitors of cysteine proteinases

V. Turk, Wolfram, Bode, 2001 .

The fluorogenic peptide substrate for cathepsin S

V. Turk, I. Dolenc, A. C̆olić, 1993 .

Some further characteristics of endogenous proteinase inhibitors.

V. Turk, G. Sava, J. Brzin, 1982, Acta biologica et medica Germanica.

Studies on bovine spleen cathepsin D.

V. Turk, F. Gubensek, I. Kregar, 1977, Acta biologica et medica Germanica.

Biochemical Characterization and Substrate Specificity of Autophagin-2 from the Parasite Trypanosoma cruzi*

G. Salvesen, V. Turk, B. Turk, 2015, The Journal of Biological Chemistry.

Crumpled Aluminum Hydroxide Nanostructures as a Microenvironment Dysregulation Agent for Cancer Treatment.

O. Vasiljeva, E. Gutmanas, V. Turk, 2018, Nano letters.

A new inhibitor of plasmin and trypsin from porcine leukocytes.

V. Turk, R. Jerala, J. Babnik, 1990, Biological chemistry Hoppe-Seyler.

In vitro transition of beef spleen cathepsin E into cathepsin D.

V. Turk, F. Gubensek, I. Kregar, 1969, Enzymologia.

A curve-fitting approach to the determination of kinetic constants of proteinase inhibitors

V. Turk, W. Machleidt, W. Müller-Esterl, 1986 .