Eva Žerovnik

5.6k total citations · 1 hit paper
98 papers, 2.7k citations indexed

About

Eva Žerovnik is a scholar working on Physiology, Molecular Biology and Rheumatology. According to data from OpenAlex, Eva Žerovnik has authored 98 papers receiving a total of 2.7k indexed citations (citations by other indexed papers that have themselves been cited), including 53 papers in Physiology, 50 papers in Molecular Biology and 19 papers in Rheumatology. Recurrent topics in Eva Žerovnik's work include Alzheimer's disease research and treatments (41 papers), Protein Structure and Dynamics (27 papers) and Lysosomal Storage Disorders Research (16 papers). Eva Žerovnik is often cited by papers focused on Alzheimer's disease research and treatments (41 papers), Protein Structure and Dynamics (27 papers) and Lysosomal Storage Disorders Research (16 papers). Eva Žerovnik collaborates with scholars based in Slovenia, United Kingdom and Bosnia and Herzegovina. Eva Žerovnik's co-authors include Vito Türk, Roger H. Pain, Gennady V. Semisotnov, Oleg B. Ptitsyn, Roman Jerala, Jonathan P. Waltho, Nataša Kopitar‐Jerala, Slavko Čeru, Rosemary A. Staniforth and Mira Polajnar and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and SHILAP Revista de lepidopterología.

In The Last Decade

Eva Žerovnik

97 papers receiving 2.6k citations

Hit Papers

Evidence for a molten globule state as a general intermed... 1990 2026 2002 2014 1990 200 400 600
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. Evidence for a molten globule state as a general intermediate in protein folding
    1990 606 citations Eva Žerovnik et al. profile →

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Eva Žerovnik Slovenia 27 1.6k 961 548 346 279 98 2.7k
N.H. Keep United Kingdom 35 2.5k 1.6× 225 0.2× 332 0.6× 296 0.9× 596 2.1× 53 3.7k
Maria Monti Italy 33 2.0k 1.3× 562 0.6× 212 0.4× 51 0.1× 400 1.4× 112 3.3k
Gary S. Shaw Canada 41 4.2k 2.6× 285 0.3× 279 0.5× 94 0.3× 430 1.5× 153 5.5k
Ludwig M.G. Heilmeyer Germany 33 2.4k 1.5× 318 0.3× 241 0.4× 313 0.9× 932 3.3× 88 3.4k
Michael O. Glocker Germany 30 1.6k 1.0× 135 0.1× 227 0.4× 185 0.5× 185 0.7× 133 3.0k
Ramón Campos‐Olivas Spain 28 2.0k 1.2× 530 0.6× 154 0.3× 65 0.2× 181 0.6× 62 3.1k
Josep Vendrell Spain 29 2.4k 1.5× 624 0.6× 336 0.6× 23 0.1× 308 1.1× 79 3.6k
Natalia Sánchez de Groot Israel 40 4.3k 2.7× 1.1k 1.1× 484 0.9× 26 0.1× 428 1.5× 107 5.3k
Elżbieta Jankowska Poland 21 894 0.6× 435 0.5× 132 0.2× 79 0.2× 135 0.5× 60 1.4k
F. Niesen United Kingdom 19 2.7k 1.7× 124 0.1× 443 0.8× 99 0.3× 401 1.4× 25 3.5k

Countries citing papers authored by Eva Žerovnik

Since Specialization
Citations

This map shows the geographic impact of Eva Žerovnik's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Eva Žerovnik with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Eva Žerovnik more than expected).

Fields of papers citing papers by Eva Žerovnik

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Eva Žerovnik. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Eva Žerovnik. The network helps show where Eva Žerovnik may publish in the future.

Co-authorship network of co-authors of Eva Žerovnik

This figure shows the co-authorship network connecting the top 25 collaborators of Eva Žerovnik. A scholar is included among the top collaborators of Eva Žerovnik based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Eva Žerovnik. Eva Žerovnik is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Žerovnik, Eva. (2024). Molecular and cellular processes underlying Unverricht-Lundborg disease—prospects for early interventions and a cure. SHILAP Revista de lepidopterología. 3(4). 295–308.
2.
Žerovnik, Eva. (2017). Co-chaperoning by amyloid-forming proteins: cystatins vs. crystallins. European Biophysics Journal. 46(8). 789–793. 5 indexed citations
3.
Žerovnik, Eva, et al.. (2014). Amyloid fibrils compared to peptide nanotubes. Biochimica et Biophysica Acta (BBA) - General Subjects. 1840(9). 2944–2952. 11 indexed citations
4.
Polajnar, Mira, Tina Zavašnik‐Bergant, Matej Vizovišek, et al.. (2014). Human Stefin B Role in Cell's Response to Misfolded Proteins and Autophagy. PLoS ONE. 9(7). e102500–e102500. 15 indexed citations
5.
Anderluh, Gregor & Eva Žerovnik. (2012). Pore formation by human stefin B in its native and oligomeric states and the consequent amyloid induced toxicity. Frontiers in Molecular Neuroscience. 5. 85–85. 11 indexed citations
6.
Polajnar, Mira & Eva Žerovnik. (2011). Impaired autophagy: a link between neurodegenerative diseases and progressive myoclonus epilepsies. Trends in Molecular Medicine. 17(6). 293–300. 22 indexed citations
7.
Žerovnik, Eva, Rosemary A. Staniforth, & Vito Türk. (2010). Amyloid fibril formation by human stefins: Structure, mechanism & putative functions. Biochimie. 92(11). 1597–1607. 24 indexed citations
8.
Čeru, Slavko, Špela Konjar, Urška Repnik, et al.. (2010). Stefin B Interacts with Histones and Cathepsin L in the Nucleus. Journal of Biological Chemistry. 285(13). 10078–10086. 77 indexed citations
9.
Žerovnik, Eva. (2008). USING STEFIN B AS A MODEL AMYLOIDOGENIC PROTEIN –OVERVIEW. SHILAP Revista de lepidopterología. 1 indexed citations
10.
Vilfan, Andrej, et al.. (2008). The mechanism of amyloid‐fibril formation by stefin B: Temperature and protein concentration dependence of the rates. Proteins Structure Function and Bioinformatics. 74(2). 425–436. 43 indexed citations
11.
Morgan, Gareth J., Silva Giannini, Andrea M. Hounslow, et al.. (2007). Exclusion of the Native α-Helix from the Amyloid Fibrils of a Mixed α/β Protein. Journal of Molecular Biology. 375(2). 487–498. 30 indexed citations
12.
Žerovnik, Eva & Nataša Kopitar‐Jerala. (2006). Human stefins and cystatins. 22 indexed citations
13.
Gunčar, Gregor, Gareth J. Morgan, Manca Kenig, et al.. (2006). Essential Role of Proline Isomerization in Stefin B Tetramer Formation. Journal of Molecular Biology. 366(5). 1569–1579. 91 indexed citations
14.
Kenig, Manca, et al.. (2003). Differences in aggregation properties of three site‐specific mutants of recombinant human stefin B. Protein Science. 13(1). 63–70. 17 indexed citations
15.
Matsunaga, Yoichi, Eva Žerovnik, Tatsuo Yamada, & Vito Türk. (2002). Conformational Changes Preceding Amyloid-fibril Formation of Amyloid-beta and Stefin B; Parallels in pH Dependence. Current Medicinal Chemistry. 9(19). 1717–1724. 21 indexed citations
16.
Žerovnik, Eva, et al.. (1999). Equilibrium and transient intermediates in folding of human macrophage migration inhibitory factor. European Journal of Biochemistry. 260(3). 609–618. 8 indexed citations
17.
Jerala, Roman, Eva Žerovnik, Jurka Kidrič, & Vito Türk. (1998). pH-induced Conformational Transitions of the Propeptide of Human Cathepsin L. Journal of Biological Chemistry. 273(19). 11498–11504. 87 indexed citations
18.
Žerovnik, Eva, Richard Virden, Roman Jerala, Vito Türk, & Jonathan P. Waltho. (1998). 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. Proteins Structure Function and Bioinformatics. 32(3). 296–303. 1 indexed citations
19.
Žerovnik, Eva, et al.. (1997). Characterization of the Equilibrium Intermediates in Acid Denaturation of Human Stefin B. European Journal of Biochemistry. 245(2). 364–372. 39 indexed citations
20.
Martin, John R., et al.. (1995). The Three-dimensional Solution Structure of Human Stefin A. Journal of Molecular Biology. 246(2). 331–343. 96 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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