Mirosław Cygler

17.0k total citations · 2 hit papers
246 papers, 13.8k citations indexed

About

Mirosław Cygler is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Mirosław Cygler has authored 246 papers receiving a total of 13.8k indexed citations (citations by other indexed papers that have themselves been cited), including 184 papers in Molecular Biology, 63 papers in Materials Chemistry and 55 papers in Cell Biology. Recurrent topics in Mirosław Cygler's work include Enzyme Structure and Function (61 papers), Glycosylation and Glycoproteins Research (38 papers) and Bacterial Genetics and Biotechnology (28 papers). Mirosław Cygler is often cited by papers focused on Enzyme Structure and Function (61 papers), Glycosylation and Glycoproteins Research (38 papers) and Bacterial Genetics and Biotechnology (28 papers). Mirosław Cygler collaborates with scholars based in Canada, United States and France. Mirosław Cygler's co-authors include Joseph D. Schrag, Yunge Li, Paweł Grochulski, Allan Matte, Israel Silman, Michal Harel, Joel L. Sussman, J. Sivaraman, Marie-Line Garron and Shan Wu and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Mirosław Cygler

241 papers receiving 13.5k citations

Hit Papers

The α/β hydrolase fold 1992 2026 2003 2014 1992 1993 500 1000 1.5k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Mirosław Cygler Canada 59 10.2k 2.1k 1.5k 1.4k 1.1k 246 13.8k
Zygmunt S. Derewenda United States 60 9.3k 0.9× 1.7k 0.8× 2.2k 1.5× 909 0.7× 978 0.9× 154 12.2k
Daan M. F. van Aalten United Kingdom 66 14.1k 1.4× 1.4k 0.7× 1.5k 1.0× 3.6k 2.6× 1.6k 1.5× 214 18.2k
Christian Cambillau France 80 11.5k 1.1× 808 0.4× 1.5k 1.0× 1.0k 0.8× 834 0.8× 347 20.0k
Harold R. Powell United Kingdom 22 9.2k 0.9× 991 0.5× 3.9k 2.6× 1.5k 1.1× 906 0.8× 73 14.2k
G. Bunkóczi United Kingdom 21 15.4k 1.5× 2.0k 0.9× 3.8k 2.6× 901 0.7× 858 0.8× 28 21.3k
Michael N.G. James Canada 63 8.8k 0.9× 724 0.4× 2.6k 1.8× 1.4k 1.0× 1.5k 1.4× 229 12.7k
M.E.M. Noble United Kingdom 63 9.9k 1.0× 2.9k 1.4× 2.1k 1.4× 1.5k 1.1× 306 0.3× 144 13.7k
A. A. Vagin Russia 14 13.4k 1.3× 1.7k 0.8× 4.8k 3.3× 1.2k 0.9× 1.3k 1.2× 20 18.6k
Stuart McNicholas United Kingdom 13 9.6k 0.9× 1.1k 0.5× 3.6k 2.4× 783 0.6× 959 0.9× 19 13.4k
Elizabeth Potterton United Kingdom 8 8.9k 0.9× 989 0.5× 3.3k 2.3× 723 0.5× 901 0.8× 8 12.5k

Countries citing papers authored by Mirosław Cygler

Since Specialization
Citations

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

Fields of papers citing papers by Mirosław Cygler

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Mirosław Cygler

This figure shows the co-authorship network connecting the top 25 collaborators of Mirosław Cygler. A scholar is included among the top collaborators of Mirosław Cygler 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 Mirosław Cygler. Mirosław Cygler 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.
Dolgova, Natalia V., Muhammad Qureshi, Matthew J. Latimer, et al.. (2025). Structural Changes at the Zinc Active Site of ACE2 on Binding the SARS-CoV-2 Spike Protein Receptor Binding Domain. Inorganic Chemistry. 64(8). 3831–3841. 1 indexed citations
2.
Rolando, Monica, et al.. (2023). The SET and ankyrin domains of the secreted Legionella pneumophila histone methyltransferase work together to modify host chromatin. mBio. 14(5). e0165523–e0165523. 5 indexed citations
3.
Giogha, Cristina, Clare V. Oates, Paul J. McMillan, et al.. (2022). Targeting of microvillus protein Eps8 by the NleH effector kinases from enteropathogenic E. coli. Proceedings of the National Academy of Sciences. 119(34). e2204332119–e2204332119. 7 indexed citations
4.
Zhao, Jianhua, Yao Liu, Stephanie A. Bueler, et al.. (2017). Molecular basis for the binding and modulation of V-ATPase by a bacterial effector protein. PLoS Pathogens. 13(6). e1006394–e1006394. 53 indexed citations
5.
Wong, Kathy, et al.. (2017). Structural Mimicry by a Bacterial F Box Effector Hijacks the Host Ubiquitin-Proteasome System. Structure. 25(2). 376–383. 24 indexed citations
6.
Shi, Rong, Deqiang Yao, Ruo‐Xu Gu, et al.. (2016). Conformational flexibility of PL12 family heparinases: structure and substrate specificity of heparinase III fromBacteroides thetaiotaomicron(BT4657). Glycobiology. 27(2). 176–187. 16 indexed citations
7.
Cherney, M.M., Tara Condos, Kathryn R. Barber, et al.. (2014). Bacterial Effector Kinases. Acta Crystallographica Section A Foundations and Advances. 70(a1). C428–C428. 1 indexed citations
8.
Shi, Rong, Laura McDonald, Jason Baardsnes, et al.. (2014). Structure of CbpA J-Domain Bound to the Regulatory Protein CbpM Explains Its Specificity and Suggests Evolutionary Link between CbpM and Transcriptional Regulators. PLoS ONE. 9(6). e100441–e100441. 8 indexed citations
9.
Ajamian, Eunice, et al.. (2012). Protein-Protein Interactions in the β-Oxidation Part of the Phenylacetate Utilization Pathway. Journal of Biological Chemistry. 287(45). 37986–37996. 13 indexed citations
10.
Garron, Marie-Line, Bo Yang, Zhongping Xiao, et al.. (2011). Asparagine 405 of heparin lyase II prevents the cleavage of glycosidic linkages proximate to a 3‐O‐sulfoglucosamine residue. FEBS Letters. 585(15). 2461–2466. 16 indexed citations
11.
Shi, Rong, Yunge Li, Christine Munger, et al.. (2011). Structure of Hydrogenase Maturation Protein HypF with Reaction Intermediates Shows Two Active Sites. Structure. 19(12). 1773–1783. 30 indexed citations
12.
Ajamian, Eunice, et al.. (2010). Crystallization and preliminary X-ray analysis of PaaAC, the main component of the hydroxylase of theEscherichia coliphenylacetyl-coenzyme A oxygenase complex. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66(9). 1045–1049. 5 indexed citations
13.
Shi, Rong, Bijan Zakeri, Ariane Proteau, et al.. (2009). Structure and Function of the Glycopeptide N-methyltransferase MtfA, a Tool for the Biosynthesis of Modified Glycopeptide Antibiotics. Chemistry & Biology. 16(4). 401–410. 38 indexed citations
14.
Hung, Ming‐Ni, et al.. (2007). NMR structure of YcgL, a conserved protein from Escherichia coli representing the DUF709 family, with a novel α/β/α sandwich fold. Proteins Structure Function and Bioinformatics. 66(4). 1004–1007. 1 indexed citations
15.
Suits, M.D.L., Gour P. Pal, Kanji Nakatsu, et al.. (2005). Identification of an Escherichia coli O157:H7 heme oxygenase with tandem functional repeats. Proceedings of the National Academy of Sciences. 102(47). 16955–16960. 77 indexed citations
16.
Shaya, David, Yunge Li, & Mirosław Cygler. (2004). Crystallization and preliminary X-ray analysis of heparinase II fromPedobacter heparinus. Acta Crystallographica Section D Biological Crystallography. 60(9). 1644–1646. 5 indexed citations
17.
Sivaraman, J., P. Iannuzzi, Mirosław Cygler, & Allan Matte. (2003). Crystal Structure of the RluD Pseudouridine Synthase Catalytic Module, an Enzyme that Modifies 23S rRNA and is Essential for Normal Cell Growth of Escherichia coli. Journal of Molecular Biology. 335(1). 87–101. 34 indexed citations
18.
Tocilj, Ante, et al.. (2003). Molecules ofEscherichia coliMobB assemble into densely packed hollow cylinders in a crystal lattice with 75% solvent content. Acta Crystallographica Section D Biological Crystallography. 59(12). 2348–2352. 1 indexed citations
19.
Pawelek, Peter D., Marc Allaire, Mirosław Cygler, & Robert E. MacKenzie. (2000). Channeling efficiency in the bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase domain: the effects of site-directed mutagenesis of NADP binding residues. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1479(1-2). 59–68. 22 indexed citations
20.
Grochulski, Paweł, François Bouthillier, Romas J. Kazlauskas, et al.. (1994). Analogs of Reaction Intermediates Identify a Unique Substrate Binding Site in Candida rugosa Lipase. Biochemistry. 33(12). 3494–3500. 218 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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