B. Lenarčič

发表

A novel allosteric mechanism in the cysteine peptidase cathepsin K discovered by computational methods

Rama Ranganathan, Amedeo Caflisch, Antonio Baici, 2014, Nature Communications.

Saxiphilin, a Saxitoxin-binding Protein with Two Thyroglobulin Type 1 Domains, Is an Inhibitor of Papain-like Cysteine Proteinases*

B. Lenarčič, V. Turk, E. Moczydlowski, 2000, The Journal of Biological Chemistry.

The Central Region of Testican-2 Forms a Compact Core and Promotes Cell Migration

B. Lenarčič, A. Krajnc, Aljaž Gaber, 2020, International journal of molecular sciences.

Current View on EpCAM Structural Biology

B. Lenarčič, Aljaž Gaber, Miha Pavšič, 2020, Cells.

The cytosolic tail of the tumor marker protein Trop2 - a structural switch triggered by phosphorylation

B. Lenarčič, J. Plavec, Miha Pavšič, 2015, Scientific Reports.

EpCAM homo-oligomerization is not the basis for its role in cell-cell adhesion

Seung Joong Kim, Robyn M. Kaake, N. Krogan, 2018, Scientific Reports.

EpCAM ectodomain EpEX is a ligand of EGFR that counteracts EGF-mediated epithelial-mesenchymal transition through modulation of phospho-ERK1/2 in head and neck cancers

B. Lenarčič, J. Hess, K. Unger, 2018, PLoS biology.

Folding studies of the cysteine proteinase inhibitor--human stefin A.

B. Lenarčič, V. Turk, R. Jerala, 1991, Biochimica et biophysica acta.

Thyropins--new structurally related proteinase inhibitors.

B. Lenarčič, T. Bevec, 1998, Biological chemistry.

Human cathepsin L, a papain‐like collagenase without proline specificity

Marko Novinec, M. Korenč, B. Lenarčič, 2015, The FEBS journal.

Molecular cloning of a putative homolog of proline/arginine‐rich antibacterial peptides from porcine bone marrow

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

Molecular cloning and identification of a novel porcine cathelin-like antibacterial peptide precursor.

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

The Heparin-Binding Activity of Secreted Modular Calcium-Binding Protein 1 (SMOC-1) Modulates Its Cell Adhesion Properties

Marko Novinec, B. Lenarčič, S. Maier, 2013, PloS one.

Recombinant human SMOCs produced by in vitro refolding: calcium-binding properties and interactions with serum proteins.

Marko Novinec, B. Lenarčič, V. Turk, 2008, Protein expression and purification.

The cysteine protease activity of Colorado potato beetle (Leptinotarsa decemlineata Say) guts, which is insensitive to potato protease inhibitors, is inhibited by thyroglobulin type-1 domain inhibitors.

K. Gruden, W. Stiekema, D. Bosch, 1998, Insect biochemistry and molecular biology.

Acidic pH as a physiological regulator of human cathepsin L activity.

B. Lenarčič, V. Turk, I. Dolenc, 2001, European journal of biochemistry.

Papain-like peptidases: structure, function, and evolution

Marko Novinec, B. Lenarčič, 2013, Biomolecular concepts.

Structural insights into F-actin regulation and sarcomere assembly via myotilin

R. Konrat, D. Svergun, K. Djinović-Carugo, 2020, bioRxiv.

Interaction between Human Cathepsins K, L, and S and Elastins

W. Stark, R. Grass, Marko Novinec, 2007, Journal of Biological Chemistry.

Thyroglobulin Type-1 Domains in Equistatin Inhibit Both Papain-like Cysteine Proteinases and Cathepsin D*

B. Lenarčič, V. Turk, 1999, The Journal of Biological Chemistry.

Conformational plasticity and evolutionary analysis of the myotilin tandem Ig domains

K. Djinović-Carugo, B. Lenarčič, Miha Pavšič, 2017, Scientific Reports.

Viral therapy: Prospects for protease inhibitors

B. Lenarčič, V. Turk, T. Towatari, 1986, Journal of cellular biochemistry.

Differences in specificity for the interactions of stefins A, B and D with cysteine proteinases

B. Lenarčič, V. Turk, I. Križaj, 1996, FEBS letters.

Cathepsin S and Cruzipain Are Inhibited by Equistatin from Actinia equina

B. Lenarčič, V. Turk, V. Stoka, 1999, Biological chemistry.

Streptomyces rimosus extracellular proteases 3. Isolation and characterization of leucine aminopeptidase

B. Lenarčič, V. Turk, L. Vitale, 1986, Applied Microbiology and Biotechnology.

Inhibition of cruzipain, the major cysteine proteinase of the protozoan parasite, Trypanosoma cruzi, by proteinase inhibitors of the cystatin superfamily

B. Lenarčič, V. Turk, V. Stoka, 1995, FEBS letters.

Expression, crystallization and preliminary X-ray characterization of the human epithelial cell-adhesion molecule ectodomain.

B. Lenarčič, Miha Pavšič, 2011, Acta crystallographica. Section F, Structural biology and crystallization communications.

Structural characterization of thyroglobulin type‐1 domains of equistatin

R. Pain, B. Lenarčič, V. Turk, 2003, FEBS letters.

Identification of new peptide amides as selective cathepsin L inhibitors: the first step towards selective irreversible inhibitors?

B. Lenarčič, V. Dive, L. Devel, 2013, Bioorganic & medicinal chemistry letters.

Cathepsin D inactivates cysteine proteinase inhibitors, cystatins.

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

Cysteine Cathepsin Activity Regulation by Glycosaminoglycans

Marko Novinec, B. Lenarčič, B. Turk, 2014, BioMed research international.

A Novel Photoaffinity‐Based Probe for Selective Detection of Cathepsin L Active Form

Marko Novinec, B. Lenarčič, V. Dive, 2012, Chembiochem : a European journal of chemical biology.

A simple and efficient protocol for the production of recombinant cathepsin V and other cysteine cathepsins in soluble form in Escherichia coli.

Marko Novinec, B. Lenarčič, Miha Pavšič, 2012, Protein expression and purification.

Interactions between a viral protease and cystatins.

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

Probing the Activity Modification Space of the Cysteine Peptidase Cathepsin K with Novel Allosteric Modifiers

Marko Novinec, B. Lenarčič, A. Baici, 2014, PloS one.

Participation of cathepsin L on bone resorption

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

Cleavage and Cell Adhesion Properties of Human Epithelial Cell Adhesion Molecule (HEPCAM)*

N. Stoecklein, B. Lenarčič, K. Lauber, 2015, The Journal of Biological Chemistry.

The death enzyme CP14 is a unique papain-like cysteine proteinase with a pronounced S2 subsite selectivity.

O. Schilling, Marko Novinec, B. Lenarčič, 2016, Archives of biochemistry and biophysics.

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.

Characterization and structure of pineapple stem inhibitor of cysteine proteinases.

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

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.

Inactivation of human cystatin C and kininogen by human cathepsin D

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

Purification and characterization of a recombinant human testican-2 expressed in baculovirus-infected Sf9 insect cells.

B. Lenarčič, Miha Pavšič, Turk Vito, 2008, Protein expression and purification.

Purification and structural characterization of bovine cathelicidins, precursors of antimicrobial peptides.

B. Lenarčič, P. Storici, A. Tossi, 1996, European journal of biochemistry.

Biochemical and preliminary X-ray characterization of the tumor-associated calcium signal transducer 2 (Trop2) ectodomain.

B. Lenarčič, Miha Pavšič, T. Vidmar, 2013, Protein expression and purification.

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.

Kinetics of the Interaction of Peptidases with Substrates and Modifiers

Marko Novinec, B. Lenarčič, A. Baici, 2013 .

Structure and calcium-binding studies of calmodulin-like domain of human non-muscle α-actinin-1

K. Djinović-Carugo, B. Lenarčič, J. Plavec, 2016, Scientific Reports.

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

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

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

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

Crystal structure and its bearing towards an understanding of key biological functions of EpCAM

Kristina Djinović-Carugo, Miha Pavšič, K. Djinović-Carugo, 2014, Nature Communications.

The catalytic domain of cathepsin C (dipeptidyl-peptidase I) alone is a fully functional endoprotease.

Marko Novinec, B. Lenarčič, Mateja Rebernik, 2019, Protein expression and purification.

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.

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.

Cathepsin K: a unique collagenolytic cysteine peptidase

Marko Novinec, B. Lenarčič, 2013, Biological chemistry.

Conformational plasticity and evolutionary analysis of the myotilin tandem Ig domains

K. Djinović-Carugo, B. Lenarčič, Miha Pavšič, 2017, Scientific Reports.

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.

Conformational flexibility and allosteric regulation of cathepsin K.

Marko Novinec, B. Lenarčič, A. Baici, 2010, The Biochemical journal.

Nicotiana benthamiana cathepsin B displays distinct enzymatic features which differ from its human relative and aleurain-like protease.

Marko Novinec, B. Lenarčič, D. Kracher, 2016, Biochimie.

Molecular basis of F-actin regulation and sarcomere assembly via myotilin

R. Konrat, D. Svergun, K. Djinović-Carugo, 2021, PLoS biology.

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

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

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.

EpCAM homo-oligomerization is not the basis for its role in cell-cell adhesion

Seung Joong Kim, Robyn M. Kaake, N. Krogan, 2018, Scientific Reports.

Cytotoxic and peptidase inhibitory activities of selected non-hepatotoxic cyclic peptides from cyanobacteria

Marko Novinec, B. Lenarčič, B. Sedmak, 2008, Biological chemistry.

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

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

An allosteric site enables fine‐tuning of cathepsin K by diverse effectors

Marko Novinec, B. Lenarčič, Mateja Rebernik, 2016, FEBS letters.

The Carboxypeptidase Activity of Cathepsin X is not Controlled by Endogenous Inhibitors.

J. Kos, B. Lenarčič, Urša Pečar Fonović, 2019, Acta Chimica Slovenica.

Cathepsin K cleavage of SDF-1α inhibits its chemotactic activity towards glioblastoma stem-like cells.

Marko Novinec, B. Lenarčič, C. Van Noorden, 2017, Biochimica et biophysica acta. Molecular cell research.

Conformational flexibility and allosteric regulation of cathepsin K.

Marko Novinec, B. Lenarčič, A. Baici, 2010, The Biochemical journal.

Mutations in the QVVAG region of the cysteine proteinase inhibitor stefin B.

B. Lenarčič, M. Trstenjak-Prebanda, L. Kroon‐Z̆itko, 1990, Biological chemistry Hoppe-Seyler.