E. Žerovnik

V. Stoka, M. Škarabot, E. Žerovnik, 2007, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis.

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1

Mark R. Marten, Erinna F. Lee, Dana L. Miller, 2021, Autophagy.

Protein conformational pathology in Alzheimer's and other neurodegenerative diseases; new targets for therapy.

E. Žerovnik, Eva Zerovnik, 2009, Current Alzheimer research.

Membrane Damage by an α-Helical Pore-forming Protein, Equinatoxin II, Proceeds through a Succession of Ordered Steps*

G. Anderluh, K. Kristan, P. Maček, 2013, The Journal of Biological Chemistry.

A central role for protein aggregation in neurodegenerative disease; Mechanistic and structural studies of human stefins

D. Turk, G. Guncar, M. Kenig, 2005 .

A single prion protein peptide can elicit a panel of isoform specific monoclonal antibodies

E. Žerovnik, M. Popović, T. Vranac, 2006, Peptides.

Differences in aggregation properties of three site‐specific mutants of recombinant human stefin B

M. Kenig, M. Pompe-Novak, E. Žerovnik, 2004, Protein science : a publication of the Protein Society.

Interaction of human stefin B in the prefibrillar oligomeric form with membranes

V. Turk, G. Anderluh, N. Kopitar-Jerala, 2005, The FEBS journal.

Synergy of the Inhibitory Action of Polyphenols Plus Vitamin C on Amyloid Fibril Formation: Case Study of Human Stefin B

E. Žerovnik, M. Tušek Žnidarič, S. Berbić, 2021, Antioxidants.

Possible Mechanisms by which Stefin B could Regulate Proteostasis and Oxidative Stress

E. Žerovnik, 2019, Cells.

Human stefin B readily forms amyloid fibrils in vitro.

V. Turk, M. Škarabot, I. Musevic, 2002, Biochimica et biophysica acta.

The three-dimensional solution structure of human stefin A.

J. Waltho, V. Turk, C. Craven, 1995, Journal of molecular biology.

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.

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.

Accessing the global minimum conformation of stefin A dimer by annealing under partially denaturing conditions.

R. Jerala, E. Žerovnik, 1999, Journal of molecular biology.

Prediction of Transmembrane Regions, Cholesterol, and Ganglioside Binding Sites in Amyloid-Forming Proteins Indicate Potential for Amyloid Pore Formation

M. Novič, V. Stoka, E. Žerovnik, 2021, Frontiers in Molecular Neuroscience.

Stefin B Interacts with Histones and Cathepsin L in the Nucleus*

N. Kopitar-Jerala, B. Turk, M. Renko, 2010, The Journal of Biological Chemistry.

Assessing Autophagy in Archived Tissue or How to Capture Autophagic Flux from a Tissue Snapshot

R. Langer, L. Eckhart, M. Tschan, 2020, Biology.

In vitro propagation of Ziziphus mauritiana cultivar Umran by shoot tip and nodal multiplication

G. Semisotnov, E. Žerovnik, 2001 .

Human stefin B: from its structure, folding, and aggregation to its function in health and disease

E. Žerovnik, 2022, Frontiers in Molecular Neuroscience.

Chapter 10 Structure and Function of Stefin B Oligomers – Important Role in

E. Žerovnik, Mira Polajnar, Ajda Taler-Verčič, 2017 .

Structure and Function of Stefin B Oligomers – Important Role in Amyloidogenesis

E. Žerovnik, Mira Polajnar, Ajda Taler-Verčič, 2014 .

On Possible Function and Toxicity of Multiple Oligomeric/Conformational States of a Globular Protein – Human Stefin B

E. Žerovnik, 2014 .

Amyloid fibril formation by human stefins: Structure, mechanism & putative functions.

D. Turk, E. Žerovnik, R. A. Staniforth, 2010, Biochimie.

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

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

High affinity copper binding by stefin B (cystatin B) and its role in the inhibition of amyloid fibrillation

David R. Brown, E. Žerovnik, Marcus W. Brazier, 2006, The FEBS journal.

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.

The effect of three polyphenols and some other antioxidant substances on amyloid fibril formation by Human cystatin C

E. Žerovnik, M. Tušek Žnidarič, S. Berbić, 2020, Neurochemistry International.

Human Stefin B Role in Cell's Response to Misfolded Proteins and Autophagy

S. Ventura, N. Kopitar-Jerala, M. Fonović, 2014, PloS one.

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

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

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.

The emerging role of cystatins in Alzheimer's disease

E. Žerovnik, 2009, BioEssays : news and reviews in molecular, cellular and developmental biology.

Prolines Affect the Nucleation Phase of Amyloid Fibrillation Reaction; Mutational Analysis of Human Stefin B

V. Puizdar, V. Stoka, A. Vilfan, 2019, ACS chemical neuroscience.

E. Žerovnik, 2021, Journal of Biotechnology and Biomedicine.

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.

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 myoglobin with urea and some alkylureas. II. Calorimetric and circular dichroic studies.

E. Žerovnik, S. Lapanje, Z. Kranjc, 1986, Biophysical chemistry.

Different propensity to form amyloid fibrils by two homologous proteins—Human stefins A and B: Searching for an explanation

D. Turk, G. Guncar, M. Kenig, 2004, Proteins.

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.

Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease.

E. Žerovnik, Eva Zerovnik, 2002, European journal of biochemistry.

Inhibition of Protein Aggregation by Several Antioxidants

E. Žerovnik, S. Berbić, Alma Jahić, 2018, Oxidative medicine and cellular longevity.

Evidence for a molten globule state as a general intermediate in protein folding

O. Ptitsyn, R. Pain, R. Pain, 1990, FEBS letters.

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

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

Amyloid Fibrils of Stefin B Show Anisotropic Properties

M. Škarabot, E. Žerovnik, Matjaž Žganec, 2023, International journal of molecular sciences.

Mechanisms of amyloid fibril formation – focus on domain‐swapping

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

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.

Proposed mechanisms and relevance to conformational disease

E. Žerovnik, 2002 .

Gibbs free energy of transfer of glycine and diglycine from water to alkylurea solutions. Measured vs. calculated values.

E. Žerovnik, S. Lapanje, 1988, Biophysical chemistry.

Impaired autophagy: a link between neurodegenerative and neuropsychiatric diseases

E. Žerovnik, Mira Polajnar, 2014, Journal of cellular and molecular medicine.

Human stefin B normal and patho-physiological role: molecular and cellular aspects of amyloid-type aggregation of certain EPM1 mutants

N. Kopitar-Jerala, E. Žerovnik, Mira Polajnar, 2012, Front. Mol. Neurosci..

Assembly of Stefin B into Polymorphic Oligomers Probed by Discrete Molecular Dynamics.

B. Urbanc, E. Žerovnik, Matjaž Žganec, 2015, Journal of chemical theory and computation.

Gain in toxic function of stefin B EPM1 mutants aggregates: correlation between cell death, aggregate number/size and oxidative stress.

N. Kopitar-Jerala, E. Žerovnik, T. Zavašnik-Bergant, 2014, Biochimica et biophysica acta.

Pore formation by human stefin B in its native and oligomeric states and the consequent amyloid induced toxicity

G. Anderluh, E. Žerovnik, 2012, Front. Mol. Neurosci..

Co-chaperoning by amyloid-forming proteins: cystatins vs. crystallins

E. Žerovnik, 2017, European Biophysics Journal.

Putative alternative functions of human stefin B (cystatin B): binding to amyloid‐beta, membranes, and copper

E. Žerovnik, 2017, Journal of molecular recognition : JMR.

Influence of partial unfolding and aggregation of human stefin B (cystatin B) EPM1 mutants G50E and Q71P on selective cleavages by cathepsins B and S

N. Kopitar-Jerala, M. Fonović, M. Vizovišek, 2013, Biological chemistry.

Binding of amyloid peptides to domain-swapped dimers of other amyloid-forming proteins may prevent their neurotoxicity.

E. Žerovnik, Ajda Taler-Verčič, 2010, BioEssays : news and reviews in molecular, cellular and developmental biology.

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.

E. Žerovnik, S. Čeru, 2008, FEBS letters.

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.

Amyloid fibrils compared to peptide nanotubes.

E. Žerovnik, Matjaž Žganec, 2014, Biochimica et biophysica acta.

USING STEFIN B AS A MODEL AMYLOIDOGENIC PROTEIN –OVERVIEW

E. Žerovnik, 2008 .

Essential role of proline isomerization in stefin B tetramer formation.

D. Turk, J. Waltho, G. Guncar, 2007, Journal of molecular biology.

Recent Developments in Treating Alzheimers Disease

R. Layfield, E. Žerovnik, Nataša Kopitar Jerala, 2016 .

Interactions of alkylureas with l-valine, l-valyl-l-valine, l-leucine, and l-leucyl-l-leucine

E. Žerovnik, M. Senegačnik, S. Lapanje, 2009 .

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.

Special Issue: “Inflammation, Oxidative Stress and Protein Aggregation; Any Links?”

S. Ventura, E. Žerovnik, Nataša Kopitar Jerala, 2020, Cells.

Proline Residues as Switches in Conformational Changes Leading to Amyloid Fibril Formation

D. Turk, V. Stoka, E. Žerovnik, 2017, International journal of molecular sciences.

The cross-road between the mechanisms of protein folding and aggregation; study of human stefin B and its H75W mutant.

E. Žerovnik, S. Berbić, A. Smajlović, 2011, Biochemical and biophysical research communications.

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.

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.

Mapping local structural perturbations in the native state of stefin B (cystatin B) under amyloid forming conditions

A. Hounslow, J. Waltho, M. Cliff, 2012, Front. Mol. Neurosci..

Oligomerization preceding amyloid fibril formation: a process in common to intrinsically disordered and globular proteins

E. Žerovnik, 2011, Network.

Essential role of Pro 74 in stefin B amyloid‐fibril formation: Dual action of cyclophilin A on the process

D. Turk, C. Schiene‐Fischer, E. Žerovnik, 2009, FEBS letters.

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.

Folding and amyloid‐fibril formation for a series of human stefins' chimeras: Any correlation?

F. Avbelj, D. Turk, J. Waltho, 2005, Proteins.

The major transition state in folding need not involve the immobilization of side chains.

A. Clarke, J. Waltho, E. Žerovnik, 2000, Proceedings of the National Academy of Sciences of the United States of America.

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.

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

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

Antioxidants From the Class of Polyphenols, NAC and Vitamin C Act Differently on Amyloid Fibril Formation by Two Human Cystatins: Stefin B and Cystatin C.

E. Žerovnik, M. Tušek Žnidarič, S. Berbić, 2020 .

Amyloid Formation of Stefin B Protein Studied by Infrared Spectroscopy.

J. Grdadolnik, B. Zupančič, E. Žerovnik, 2023, Frontiers in bioscience.

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 .

Effect of temperature on the apparent molal volume of ethylurea in aqueous solutions

V. Vlachy, E. Žerovnik, S. Lapanje, 1985 .

Putative alternative functions of human stefin B (cystatin B): binding to amyloid‐beta, membranes, and copper

E. Žerovnik, 2017, Journal of molecular recognition : JMR.

Molecular and cellular processes underlying Unverricht-Lundborg disease—prospects for early interventions and a cure

E. Žerovnik, 2024, Exploration of Neuroscience.