József Kardos

6.9k total citations · 3 hit papers
99 papers, 5.3k citations indexed

About

József Kardos is a scholar working on Molecular Biology, Physiology and Materials Chemistry. According to data from OpenAlex, József Kardos has authored 99 papers receiving a total of 5.3k indexed citations (citations by other indexed papers that have themselves been cited), including 67 papers in Molecular Biology, 33 papers in Physiology and 14 papers in Materials Chemistry. Recurrent topics in József Kardos's work include Protein Structure and Dynamics (34 papers), Alzheimer's disease research and treatments (30 papers) and Enzyme Structure and Function (14 papers). József Kardos is often cited by papers focused on Protein Structure and Dynamics (34 papers), Alzheimer's disease research and treatments (30 papers) and Enzyme Structure and Function (14 papers). József Kardos collaborates with scholars based in Hungary, Japan and France. József Kardos's co-authors include Yuji Goto, András Micsonai, Young‐Ho Lee, Frank Wien, Matthieu Réfrégiers, Péter Závodszky, Éva Bulyáki, Éva Moussong, Gregory A. Petsko and Judit Kun and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

József Kardos

96 papers receiving 5.2k citations

Hit Papers

Accurate secondary structure prediction and fold recognit... 2015 2026 2018 2022 2015 2018 2022 400 800 1.2k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
József Kardos Hungary 33 3.4k 1.1k 803 472 443 99 5.3k
Young‐Ho Lee Japan 31 3.4k 1.0× 1.5k 1.3× 649 0.8× 314 0.7× 625 1.4× 126 5.6k
Arthur Laganowsky United States 35 4.1k 1.2× 960 0.9× 678 0.8× 357 0.8× 401 0.9× 105 5.7k
Jean‐Marie Ruysschaert Belgium 41 4.4k 1.3× 1.1k 1.0× 414 0.5× 674 1.4× 702 1.6× 110 6.7k
Débora Foguel Brazil 38 3.0k 0.9× 945 0.9× 568 0.7× 319 0.7× 139 0.3× 126 4.8k
Frank Wien France 26 3.1k 0.9× 439 0.4× 768 1.0× 249 0.5× 474 1.1× 112 4.9k
Manuel Prieto Portugal 46 5.9k 1.7× 832 0.8× 598 0.7× 284 0.6× 350 0.8× 186 7.6k
Marie‐Isabel Aguilar Australia 47 4.7k 1.4× 649 0.6× 395 0.5× 461 1.0× 704 1.6× 213 7.0k
Ludmilla A. Morozova‐Roche Sweden 35 2.7k 0.8× 1.8k 1.6× 413 0.5× 312 0.7× 293 0.7× 91 4.1k
Sarah Rauscher Canada 14 4.3k 1.2× 451 0.4× 941 1.2× 239 0.5× 457 1.0× 32 5.8k
Saburo Aimoto Japan 46 5.5k 1.6× 1.6k 1.4× 503 0.6× 358 0.8× 394 0.9× 195 7.6k

Countries citing papers authored by József Kardos

Since Specialization
Citations

This map shows the geographic impact of József Kardos'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 József Kardos with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites József Kardos more than expected).

Fields of papers citing papers by József Kardos

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by József Kardos. 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 József Kardos. The network helps show where József Kardos may publish in the future.

Co-authorship network of co-authors of József Kardos

This figure shows the co-authorship network connecting the top 25 collaborators of József Kardos. A scholar is included among the top collaborators of József Kardos 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 József Kardos. József Kardos 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.
Kardos, József, Éva Moussong, Frank Wien, et al.. (2025). Guide to the structural characterization of protein aggregates and amyloid fibrils by CD spectroscopy. Protein Science. 34(3). e70066–e70066. 11 indexed citations
3.
Lin, Yuxi, Eugene Bok, Dong‐Hyun Seo, et al.. (2023). An amphiphilic material arginine–arginine–bile acid promotes α-synuclein amyloid formation. Nanoscale. 15(21). 9315–9328. 5 indexed citations
4.
Szabó, Beáta, et al.. (2023). In Vivo and In Vitro Characterization of the RNA Binding Capacity of SETD1A (KMT2F). International Journal of Molecular Sciences. 24(22). 16032–16032. 1 indexed citations
5.
Csősz, Éva, et al.. (2023). LPS-induced acute neuroinflammation, involving interleukin-1 beta signaling, leads to proteomic, cellular, and network-level changes in the prefrontal cortex of mice. Brain Behavior & Immunity - Health. 28. 100594–100594. 14 indexed citations
6.
Micsonai, András, Éva Moussong, Frank Wien, et al.. (2022). BeStSel: webserver for secondary structure and fold prediction for protein CD spectroscopy. Nucleic Acids Research. 50(W1). W90–W98. 237 indexed citations breakdown →
7.
Vadászi, Henrietta, Bence Kiss, András Micsonai, et al.. (2022). Competitive inhibition of the classical complement pathway using exogenous single-chain C1q recognition proteins. Journal of Biological Chemistry. 298(7). 102113–102113. 4 indexed citations
8.
Yamaguchi, K., Masatomo So, Eri Chatani, et al.. (2021). Breakdown of supersaturation barrier links protein folding to amyloid formation. Communications Biology. 4(1). 120–120. 47 indexed citations
9.
Györffy, Balázs A., György Török, Péter Gulyássy, et al.. (2020). Synaptic mitochondrial dysfunction and septin accumulation are linked to complement-mediated synapse loss in an Alzheimer’s disease animal model. Cellular and Molecular Life Sciences. 77(24). 5243–5258. 50 indexed citations
10.
So, Masatomo, Kenji Sasahara, Yohei Miyanoiri, et al.. (2020). Isoelectric point-amyloid formation of α-synuclein extends the generality of the solubility and supersaturation-limited mechanism. SHILAP Revista de lepidopterología. 2. 35–44. 24 indexed citations
11.
Kovács, Gábor M., Ádám Póti, Attila Reményi, et al.. (2019). High‐throughput competitive fluorescence polarization assay reveals functional redundancy in the S100 protein family. FEBS Journal. 287(13). 2834–2846. 26 indexed citations
12.
Sasahara, Kenji, K. Yamaguchi, Masatomo So, et al.. (2019). Heating during agitation of β2-microglobulin reveals that supersaturation breakdown is required for amyloid fibril formation at neutral pH. Journal of Biological Chemistry. 294(43). 15826–15835. 20 indexed citations
13.
Meißner, Robert H., Jonathan D. Hirst, András Micsonai, et al.. (2019). Impact of the Conformational Variability of Oligopeptides on the Computational Prediction of Their CD Spectra. The Journal of Physical Chemistry B. 123(31). 6694–6704. 6 indexed citations
14.
Horváth, Gergő, László Biczók, Zsuzsa Májer, et al.. (2017). Structural insight into a partially unfolded state preceding aggregation in an intracellular lipid‐binding protein. FEBS Journal. 284(21). 3637–3661. 8 indexed citations
15.
So, Masatomo, Masayuki Adachi, József Kardos, et al.. (2016). Thioflavin T-Silent Denaturation Intermediates Support the Main-Chain-Dominated Architecture of Amyloid Fibrils. Biochemistry. 55(28). 3937–3948. 7 indexed citations
16.
Micsonai, András, Frank Wien, Young‐Ho Lee, et al.. (2015). Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy. Proceedings of the National Academy of Sciences. 112(24). E3095–103. 1292 indexed citations breakdown →
17.
Hajdú, István, et al.. (2008). Adjustment of conformational flexibility of glyceraldehyde-3-phosphate dehydrogenase as a means of thermal adaptation and allosteric regulation. European Biophysics Journal. 37(7). 1139–1144. 9 indexed citations
18.
Kardos, József, Veronika Harmat, O. Barábas, et al.. (2007). Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: Structure of the active catalytic region of C1r. Molecular Immunology. 45(6). 1752–1760. 33 indexed citations
19.
Fodor, Krisztián, Veronika Harmat, Csaba Hetényi, et al.. (2005). Extended Intermolecular Interactions in a Serine Protease–Canonical Inhibitor Complex Account for Strong and Highly Specific Inhibition. Journal of Molecular Biology. 350(1). 156–169. 42 indexed citations
20.
Kardos, József, Péter Gál, László Szilágyi, et al.. (2001). The Role of the Individual Domains in the Structure and Function of the Catalytic Region of a Modular Serine Protease, C1r. The Journal of Immunology. 167(9). 5202–5208. 33 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.

Explore authors with similar magnitude of impact

Rankless by CCL
2026