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

    Žerovnik, Eva

    Frontiers in molecular neuroscience

    2022  Volume 15, Page(s) 1009976

    Abstract: Mutations in the gene for human stefin B (cystatin B) cause progressive myoclonic epilepsy type 1 (EPM1), a neurodegenerative disorder. The most common change is dodecamer repeats in the promoter region of the gene, though missense and frameshift ... ...

    Abstract Mutations in the gene for human stefin B (cystatin B) cause progressive myoclonic epilepsy type 1 (EPM1), a neurodegenerative disorder. The most common change is dodecamer repeats in the promoter region of the gene, though missense and frameshift mutations also appear. Human stefin B primarily acts as a cysteine cathepsin inhibitor, and it also exhibits alternative functions. It plays a protective role against oxidative stress, likely
    Language English
    Publishing date 2022-10-21
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2452967-9
    ISSN 1662-5099
    ISSN 1662-5099
    DOI 10.3389/fnmol.2022.1009976
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Viroporins vs. Other Pore-Forming Proteins: What Lessons Can We Take?

    Žerovnik, Eva

    Frontiers in chemistry

    2021  Volume 9, Page(s) 626059

    Abstract: Pore-forming proteins (PFPs) exist in virtually all domains of life, and by disrupting cellular membranes, depending on the pore size, they cause ion dis-balance, small substances, or even protein efflux/influx, influencing cell's signaling routes and ... ...

    Abstract Pore-forming proteins (PFPs) exist in virtually all domains of life, and by disrupting cellular membranes, depending on the pore size, they cause ion dis-balance, small substances, or even protein efflux/influx, influencing cell's signaling routes and fate. Such pore-forming proteins exist from bacteria to viruses and also shape host defense systems, including innate immunity. There is strong evidence that amyloid toxicity is also caused by prefibrillar oligomers making "amyloid pores" into cellular membranes. For most of the PFPs, a 2-step mechanism of protein-membrane interaction takes place on the "lipid rafts," membrane microdomains rich in gangliosides and cholesterol. In this mini-review paper, common traits of different PFPs are looked at. Possible ways for therapy of channelopathies and/or modulating immunity relevant to the new threat of SARS-CoV-2 infections could be learnt from such comparisons.
    Language English
    Publishing date 2021-02-18
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2711776-5
    ISSN 2296-2646
    ISSN 2296-2646
    DOI 10.3389/fchem.2021.626059
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Protein Condensates and Protein Aggregates:

    Venko, Katja / Žerovnik, Eva

    Frontiers in bioscience (Landmark edition)

    2023  Volume 28, Issue 8, Page(s) 183

    Abstract: Similar to other polypeptides and electrolytes, proteins undergo phase transitions, obeying physicochemical laws. They can undergo liquid-to-gel and liquid-to-liquid phase transitions. Intrinsically disordered proteins are particularly susceptible to ... ...

    Abstract Similar to other polypeptides and electrolytes, proteins undergo phase transitions, obeying physicochemical laws. They can undergo liquid-to-gel and liquid-to-liquid phase transitions. Intrinsically disordered proteins are particularly susceptible to phase separation. After a general introduction, the principles of
    MeSH term(s) Protein Aggregates ; Computational Biology ; Phase Transition ; Protein Domains
    Chemical Substances Protein Aggregates
    Language English
    Publishing date 2023-09-04
    Publishing country Singapore
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 2704569-9
    ISSN 2768-6698 ; 2768-6698
    ISSN (online) 2768-6698
    ISSN 2768-6698
    DOI 10.31083/j.fbl2808183
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  4. Article ; Online: Viroporins vs. Other Pore-Forming Proteins

    Eva Žerovnik

    Frontiers in Chemistry, Vol

    What Lessons Can We Take?

    2021  Volume 9

    Abstract: Pore-forming proteins (PFPs) exist in virtually all domains of life, and by disrupting cellular membranes, depending on the pore size, they cause ion dis-balance, small substances, or even protein efflux/influx, influencing cell’s signaling routes and ... ...

    Abstract Pore-forming proteins (PFPs) exist in virtually all domains of life, and by disrupting cellular membranes, depending on the pore size, they cause ion dis-balance, small substances, or even protein efflux/influx, influencing cell’s signaling routes and fate. Such pore-forming proteins exist from bacteria to viruses and also shape host defense systems, including innate immunity. There is strong evidence that amyloid toxicity is also caused by prefibrillar oligomers making “amyloid pores” into cellular membranes. For most of the PFPs, a 2-step mechanism of protein-membrane interaction takes place on the “lipid rafts,” membrane microdomains rich in gangliosides and cholesterol. In this mini-review paper, common traits of different PFPs are looked at. Possible ways for therapy of channelopathies and/or modulating immunity relevant to the new threat of SARS-CoV-2 infections could be learnt from such comparisons.
    Keywords SARS-CoV-2 E protein ; amyloid pore ; channel formation ; ion conductance activity ; drug target ; Chemistry ; QD1-999
    Language English
    Publishing date 2021-02-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article: Possible Mechanisms by which Stefin B could Regulate Proteostasis and Oxidative Stress.

    Žerovnik, Eva

    Cells

    2019  Volume 8, Issue 1

    Abstract: Human stefin B is a protease inhibitor from the family of cystatins. It was reported that it forms oligomers in cells. We have shown that it has a role in cell's response to misfolded proteins. We also have shown that its oligomers bind amyloid-beta (Aβ). ...

    Abstract Human stefin B is a protease inhibitor from the family of cystatins. It was reported that it forms oligomers in cells. We have shown that it has a role in cell's response to misfolded proteins. We also have shown that its oligomers bind amyloid-beta (Aβ). Here, we discuss ways, how stefin B could reduce build-up of protein aggregates by other proteins and consequently reduces ROS and, how this might be connected to autophagy. When overexpressed, stefin B forms protein aggregates itself and these protein aggregates induce autophagy. Similarly, cystatin C was shown to bind Aβ and to induce autophagy. It is also suggested how more knowledge about the role of stefin B in a cell's response to misfolded proteins could be used to modulate progressive myoclonus epilepsy of type 1 EPM1 disease.
    MeSH term(s) Amyloid/metabolism ; Cystatin B/genetics ; Cystatin B/metabolism ; Disease Progression ; Humans ; Mutation/genetics ; Oxidative Stress ; Proteostasis
    Chemical Substances Amyloid ; Cystatin B (88844-95-5)
    Language English
    Publishing date 2019-01-18
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2661518-6
    ISSN 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells8010070
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Possible Mechanisms by which Stefin B could Regulate Proteostasis and Oxidative Stress

    Eva Žerovnik

    Cells, Vol 8, Iss 1, p

    2019  Volume 70

    Abstract: Human stefin B is a protease inhibitor from the family of cystatins. It was reported that it forms oligomers in cells. We have shown that it has a role in cell’s response to misfolded proteins. We also have shown that its oligomers bind amyloid-beta (Aβ). ...

    Abstract Human stefin B is a protease inhibitor from the family of cystatins. It was reported that it forms oligomers in cells. We have shown that it has a role in cell’s response to misfolded proteins. We also have shown that its oligomers bind amyloid-beta (Aβ). Here, we discuss ways, how stefin B could reduce build-up of protein aggregates by other proteins and consequently reduces ROS and, how this might be connected to autophagy. When overexpressed, stefin B forms protein aggregates itself and these protein aggregates induce autophagy. Similarly, cystatin C was shown to bind Aβ and to induce autophagy. It is also suggested how more knowledge about the role of stefin B in a cell’s response to misfolded proteins could be used to modulate progressive myoclonus epilepsy of type 1 EPM1 disease.
    Keywords cystatin B ; amyloid ; oligomers toxicity ; protein aggregation ; autophagy ; oxidative stress ; Biology (General) ; QH301-705.5
    Language English
    Publishing date 2019-01-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: Putative alternative functions of human stefin B (cystatin B): binding to amyloid-beta, membranes, and copper.

    Žerovnik, Eva

    Journal of molecular recognition : JMR

    2017  Volume 30, Issue 1

    Abstract: We describe studies performed thus far on stefin B from the family of cystatins as a model protein for folding and amyloid fibril formation studies. We also briefly mention our studies on aggregation of some of the missense EPM1 mutants of stefin B in ... ...

    Abstract We describe studies performed thus far on stefin B from the family of cystatins as a model protein for folding and amyloid fibril formation studies. We also briefly mention our studies on aggregation of some of the missense EPM1 mutants of stefin B in cells, which mimic additional pathological traits (gain in toxic function) in selected patients with EPM1 disease. We collected data on the reported interactors of stefin B and discuss several hypotheses of possible cytosolic alternative functions.
    Language English
    Publishing date 2017-01
    Publishing country England
    Document type Journal Article
    ZDB-ID 1015084-5
    ISSN 1099-1352 ; 0952-3499
    ISSN (online) 1099-1352
    ISSN 0952-3499
    DOI 10.1002/jmr.2562
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2954: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  8. Article ; Online: Co-chaperoning by amyloid-forming proteins: cystatins vs. crystallins.

    Žerovnik, Eva

    European biophysics journal : EBJ

    2017  Volume 46, Issue 8, Page(s) 789–793

    Abstract: Cystatins and crystallins are both neuroprotective proteins. Except for their function as cysteine cathepsins inhibitors, cystatins are Aβ binding proteins and presumably protect neurons from intracellular Aβ and extracellular Aβ plaques. Pathological ... ...

    Abstract Cystatins and crystallins are both neuroprotective proteins. Except for their function as cysteine cathepsins inhibitors, cystatins are Aβ binding proteins and presumably protect neurons from intracellular Aβ and extracellular Aβ plaques. Pathological mutations of cystatin C cause amyloid angiopathy. Crystallins, known as small heat shock proteins, bind not only Aβ peptide but also other crystallins in the eye lens and prevent their aggregation. Mutations in crystallins cause cataracts and myopathies. Cross-interactions between amyloidogenic proteins, intrinsically disordered and folded proteins, can also occur. I term the nonspecific binding between amyloidogenic proteins and peptides "co-chaperoning." A wide range of other Aβ binding proteins exist, such as catalase, lysozyme, β-lactoglobulin and some other abundant proteins found in plasma.
    Language English
    Publishing date 2017-12
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 283671-3
    ISSN 1432-1017 ; 0175-7571
    ISSN (online) 1432-1017
    ISSN 0175-7571
    DOI 10.1007/s00249-017-1214-x
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1121: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  9. Article: Correction: Jahić Mujkić et al. Synergy of the Inhibitory Action of Polyphenols Plus Vitamin C on Amyloid Fibril Formation: Case Study of Human Stefin B.

    Jahić Mujkić, Alma / Tušek Žnidarič, Magda / Berbić, Selma / Žerovnik, Eva

    Antioxidants (Basel, Switzerland)

    2023  Volume 13, Issue 1

    Abstract: In the original publication [ ... ]. ...

    Abstract In the original publication [...].
    Language English
    Publishing date 2023-12-28
    Publishing country Switzerland
    Document type Published Erratum
    ZDB-ID 2704216-9
    ISSN 2076-3921
    ISSN 2076-3921
    DOI 10.3390/antiox13010056
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Amyloid Formation of Stefin B Protein Studied by Infrared Spectroscopy.

    Novak, Urban / Žerovnik, Eva / Taler-Verčič, Ajda / Žnidarič, MagdaTušek / Zupančič, Barbara / Grdadolnik, Jože

    Frontiers in bioscience (Landmark edition)

    2023  Volume 28, Issue 3, Page(s) 46

    Abstract: Background: Stefin B, an established model protein for studying the stability and mechanism of protein folding, was used for monitoring protein aggregation and formation of amyloid structure by infrared spectroscopy.: Methods: The analyses of the ... ...

    Abstract Background: Stefin B, an established model protein for studying the stability and mechanism of protein folding, was used for monitoring protein aggregation and formation of amyloid structure by infrared spectroscopy.
    Methods: The analyses of the integral intensities of the low frequency part of the Amide I band, which is directly connected to the appearance of the cross-β structure reveals the temperature but not pH dependence of stefin B structure.
    Results: We show that pH value has significant role in the monomer stability of stefin B. Protein is less stable in acidic environment and becomes more stable in neutral or basic conditions. While in the case of the Amide I band area analysis we apply only spectral regions characteristic for only part of the protein in cross-β structure, the temperature study using multivariate curve resolution (MCR) analysis contains also information about the protein conformation states which do not correspond to native protein nor protein in cross-β structure.
    Conclusions: These facts results in the slightly different shapes of fitted sigmoid functions fitted to the weighted amount of the second basic spectrum (sc2), which is the closed approximation of the protein spectra with cross-β structure. Nevertheless, the applied method detects the initial change of the protein structure. Upon the analysis of infrared data a model for stefin B aggregation is proposed.
    MeSH term(s) Cystatin B ; Cystatins/chemistry ; Cystatins/metabolism ; Amyloid/chemistry ; Amyloid/metabolism ; Protein Conformation ; Spectrum Analysis
    Chemical Substances Cystatin B (88844-95-5) ; Cystatins ; Amyloid
    Language English
    Publishing date 2023-04-01
    Publishing country Singapore
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2704569-9
    ISSN 2768-6698 ; 2768-6698
    ISSN (online) 2768-6698
    ISSN 2768-6698
    DOI 10.31083/j.fbl2803046
    Database MEDical Literature Analysis and Retrieval System OnLINE

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