Katalin Illes

2.3k total citations · 1 hit paper
25 papers, 1.3k citations indexed

About

Katalin Illes is a scholar working on Molecular Biology, Physiology and Physiology. According to data from OpenAlex, Katalin Illes has authored 25 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Molecular Biology, 8 papers in Physiology and 8 papers in Physiology. Recurrent topics in Katalin Illes's work include Lysosomal Storage Disorders Research (7 papers), Adenosine and Purinergic Signaling (6 papers) and Sphingolipid Metabolism and Signaling (5 papers). Katalin Illes is often cited by papers focused on Lysosomal Storage Disorders Research (7 papers), Adenosine and Purinergic Signaling (6 papers) and Sphingolipid Metabolism and Signaling (5 papers). Katalin Illes collaborates with scholars based in Canada, United States and Austria. Katalin Illes's co-authors include Bhushan Nagar, A. Gorelik, Judit Pallos, Leslie M. Thompson, Joan Marsh, Natalia Slepko, Elena Cattaneo, Erica Rockabrand, Yazhen Zhu and Namita Agrawal and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Katalin Illes

25 papers receiving 1.3k citations

Hit Papers

SUMO Modification of Huntingtin and Huntington's Disease ... 2004 2026 2011 2018 2004 100 200 300 400 500

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Katalin Illes Canada 15 1.0k 583 188 162 160 25 1.3k
Zhen Xu China 18 847 0.8× 280 0.5× 197 1.0× 160 1.0× 114 0.7× 49 1.4k
Daniel W. Summers United States 17 1.1k 1.0× 537 0.9× 429 2.3× 244 1.5× 205 1.3× 24 2.1k
Franck Vandermoere France 21 1.5k 1.4× 220 0.4× 207 1.1× 51 0.3× 127 0.8× 32 1.8k
Natalia B. Nedelsky United States 9 1.1k 1.1× 392 0.7× 357 1.9× 297 1.8× 227 1.4× 9 1.8k
Brett A. McCray United States 13 889 0.9× 348 0.6× 393 2.1× 251 1.5× 215 1.3× 23 1.5k
Ghanashyam D. Ghadge United States 24 1.2k 1.1× 469 0.8× 128 0.7× 421 2.6× 323 2.0× 48 2.0k
Sylvain Féliciangéli France 20 1.3k 1.3× 430 0.7× 426 2.3× 38 0.2× 163 1.0× 27 1.9k
Elsa Lauwers Belgium 17 893 0.9× 197 0.3× 521 2.8× 86 0.5× 150 0.9× 24 1.3k
Greg L. Harris United States 21 1.1k 1.1× 450 0.8× 228 1.2× 34 0.2× 179 1.1× 26 1.6k
Mathieu Lavallée‐Adam Canada 21 1.1k 1.1× 115 0.2× 279 1.5× 86 0.5× 168 1.1× 47 1.6k

Countries citing papers authored by Katalin Illes

Since Specialization
Citations

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

Fields of papers citing papers by Katalin Illes

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Katalin Illes

This figure shows the co-authorship network connecting the top 25 collaborators of Katalin Illes. A scholar is included among the top collaborators of Katalin Illes 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 Katalin Illes. Katalin Illes 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.
Gorelik, A., et al.. (2024). Structural Analysis of Mammalian Sialic Acid Esterase. Journal of Molecular Biology. 436(22). 168801–168801. 4 indexed citations
2.
Liang, Yue, Katalin Illes, Philippe Gros, et al.. (2023). Deubiquitinase catalytic activity of MYSM1 is essential in vivo for hematopoiesis and immune cell development. Scientific Reports. 13(1). 338–338. 5 indexed citations
3.
Gorelik, A., Katalin Illes, Mohammad T. Mazhab‐Jafari, & Bhushan Nagar. (2023). Structure of the immunoregulatory sialidase NEU1. Science Advances. 9(20). eadf8169–eadf8169. 18 indexed citations
4.
Illes, Katalin, et al.. (2023). Dimerization of the CNNM extracellular domain. Protein Science. 33(2). e4860–e4860. 1 indexed citations
5.
Gorelik, A., et al.. (2021). Structure of the murine lysosomal multienzyme complex core. Science Advances. 7(20). 11 indexed citations
6.
Kozlov, Guennadi, et al.. (2020). PRL3 pseudophosphatase activity is necessary and sufficient to promote metastatic growth. Journal of Biological Chemistry. 295(33). 11682–11692. 24 indexed citations
7.
Gorelik, A., Katalin Illes, & Bhushan Nagar. (2020). Crystal Structure of the Mannose-6-Phosphate Uncovering Enzyme. Structure. 28(4). 426–436.e3. 6 indexed citations
8.
Gorelik, A., et al.. (2020). Crystal structure of the nucleotide‐metabolizing enzyme NTPDase4. Protein Science. 29(10). 2054–2061. 3 indexed citations
9.
Gorelik, A., Katalin Illes, & Bhushan Nagar. (2018). Crystal structure of the mammalian lipopolysaccharide detoxifier. Proceedings of the National Academy of Sciences. 115(5). E896–E905. 23 indexed citations
10.
Liang, Yingke, et al.. (2018). The structure of mammalian β‐mannosidase provides insight into β‐mannosidosis and nystagmus. FEBS Journal. 286(7). 1319–1331. 12 indexed citations
11.
Gorelik, A., et al.. (2018). Structural basis for the activation of acid ceramidase. Nature Communications. 9(1). 1621–1621. 60 indexed citations
12.
Dementiev, Alexey, A. Joachimiak, A. Gorelik, et al.. (2018). Molecular Mechanism of Inhibition of Acid Ceramidase by Carmofur. Journal of Medicinal Chemistry. 62(2). 987–992. 55 indexed citations
13.
Gorelik, A., Fangyu Liu, Katalin Illes, & Bhushan Nagar. (2017). Crystal structure of the human alkaline sphingomyelinase provides insights into substrate recognition. Journal of Biological Chemistry. 292(17). 7087–7094. 34 indexed citations
14.
Gorelik, A., Katalin Illes, Giulio Superti‐Furga, & Bhushan Nagar. (2016). Structural Basis for Nucleotide Hydrolysis by the Acid Sphingomyelinase-like Phosphodiesterase SMPDL3A. Journal of Biological Chemistry. 291(12). 6376–6385. 12 indexed citations
15.
Gorelik, A., Katalin Illes, Leonhard X. Heinz, Giulio Superti‐Furga, & Bhushan Nagar. (2016). Crystal structure of mammalian acid sphingomyelinase. Nature Communications. 7(1). 12196–12196. 80 indexed citations
16.
Gorelik, A., Leonhard X. Heinz, Katalin Illes, Giulio Superti‐Furga, & Bhushan Nagar. (2016). Crystal Structure of the Acid Sphingomyelinase-like Phosphodiesterase SMPDL3B Provides Insights into Determinants of Substrate Specificity. Journal of Biological Chemistry. 291(46). 24054–24064. 19 indexed citations
17.
Apostol, Barbara L., Danielle A. Simmons, Chiara Zuccato, et al.. (2008). CEP-1347 reduces mutant huntingtin-associated neurotoxicity and restores BDNF levels in R6/2 mice. Molecular and Cellular Neuroscience. 39(1). 8–20. 67 indexed citations
18.
Apostol, Barbara L., Katalin Illes, Judit Pallos, et al.. (2005). Mutant huntingtin alters MAPK signaling pathways in PC12 and striatal cells: ERK1/2 protects against mutant huntingtin-associated toxicity. Human Molecular Genetics. 15(2). 273–285. 117 indexed citations
19.
Steffan, Joan S., Namita Agrawal, Judit Pallos, et al.. (2004). SUMO Modification of Huntingtin and Huntington's Disease Pathology. Science. 304(5667). 100–104. 547 indexed citations breakdown →
20.
Apostol, Barbara L., Simona Raffioni, Katalin Illes, et al.. (2003). A cell-based assay for aggregation inhibitors as therapeutics of polyglutamine-repeat disease and validation in Drosophila. Proceedings of the National Academy of Sciences. 100(10). 5950–5955. 141 indexed citations

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