M. Ruszkowski

938 total citations
51 papers, 652 citations indexed

About

M. Ruszkowski is a scholar working on Molecular Biology, Materials Chemistry and Plant Science. According to data from OpenAlex, M. Ruszkowski has authored 51 papers receiving a total of 652 indexed citations (citations by other indexed papers that have themselves been cited), including 35 papers in Molecular Biology, 21 papers in Materials Chemistry and 18 papers in Plant Science. Recurrent topics in M. Ruszkowski's work include Enzyme Structure and Function (21 papers), Biochemical and Molecular Research (9 papers) and Amino Acid Enzymes and Metabolism (8 papers). M. Ruszkowski is often cited by papers focused on Enzyme Structure and Function (21 papers), Biochemical and Molecular Research (9 papers) and Amino Acid Enzymes and Metabolism (8 papers). M. Ruszkowski collaborates with scholars based in Poland, United States and Italy. M. Ruszkowski's co-authors include Zbigniew Dauter, Agnieszka Ruszkowska, B. Sekula, Mariusz Jaskólski, Jessica A. Brown, Joanna Śliwiak, B. Nocek, Giuseppe Forlani, M. Sikorski and Michele Bertazzini and has published in prestigious journals such as Nucleic Acids Research, Journal of Biological Chemistry and Scientific Reports.

In The Last Decade

M. Ruszkowski

48 papers receiving 646 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
M. Ruszkowski Poland 16 465 228 97 66 47 51 652
Eerappa Rajakumara India 14 728 1.6× 101 0.4× 67 0.7× 18 0.3× 35 0.7× 42 975
Jodie E. Guy Sweden 13 434 0.9× 91 0.4× 103 1.1× 146 2.2× 15 0.3× 18 602
Antonia María Romero Spain 14 385 0.8× 122 0.5× 43 0.4× 12 0.2× 20 0.4× 29 715
Susumu Morigasaki Japan 16 590 1.3× 205 0.9× 42 0.4× 77 1.2× 13 0.3× 30 893
Clare L. Lawrence United Kingdom 15 477 1.0× 142 0.6× 26 0.3× 13 0.2× 28 0.6× 31 736
Karine Blondeau France 18 663 1.4× 224 1.0× 104 1.1× 25 0.4× 19 0.4× 35 986
Meinhard Hasslacher Austria 13 620 1.3× 118 0.5× 112 1.2× 112 1.7× 9 0.2× 19 858
Jianbin Shi China 17 277 0.6× 302 1.3× 144 1.5× 11 0.2× 28 0.6× 61 839
Seiichiro Ikeda Japan 14 351 0.8× 114 0.5× 114 1.2× 64 1.0× 10 0.2× 35 571
K. Kita Japan 12 603 1.3× 64 0.3× 53 0.5× 87 1.3× 15 0.3× 17 837

Countries citing papers authored by M. Ruszkowski

Since Specialization
Citations

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

Fields of papers citing papers by M. Ruszkowski

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of M. Ruszkowski

This figure shows the co-authorship network connecting the top 25 collaborators of M. Ruszkowski. A scholar is included among the top collaborators of M. Ruszkowski 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 M. Ruszkowski. M. Ruszkowski 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.
2.
Forlani, Giuseppe, et al.. (2025). Crystallographic fragment screening reveals new starting points for PYCR1 inhibitor design. Bioorganic Chemistry. 165. 109024–109024.
3.
Ruszkowski, M., et al.. (2025). ARR1 and AHP interactions in the multi-step phosphorelay system. Frontiers in Plant Science. 16. 1537021–1537021. 1 indexed citations
4.
Śliwiak, Joanna, et al.. (2024). Legume-type glutamate dehydrogenase: Structure, activity, and inhibition studies. International Journal of Biological Macromolecules. 278(Pt 2). 134648–134648. 5 indexed citations
5.
Śliwiak, Joanna, et al.. (2024). Probing the active site of Class 3 L-asparaginase by mutagenesis. I. Tinkering with the zinc coordination site of ReAV. Frontiers in Chemistry. 12. 1381032–1381032. 3 indexed citations
6.
7.
Zieleziński, Andrzej, M. Ruszkowski, Agnieszka Ludwików, et al.. (2023). The effects of nature‐inspired amino acid substitutions on structural and biochemical properties of the E. coli L‐asparaginase EcAIII. Protein Science. 32(6). e4647–e4647. 9 indexed citations
8.
Śliwiak, Joanna, et al.. (2023). Structural and functional studies of Arabidopsis thaliana glutamate dehydrogenase isoform 2 demonstrate enzyme dynamics and identify its calcium binding site. Plant Physiology and Biochemistry. 201. 107895–107895. 7 indexed citations
9.
Nogués, Isabel, et al.. (2023). Insights into the substrate specificity, structure, and dynamics of plant histidinol-phosphate aminotransferase (HISN6). Plant Physiology and Biochemistry. 196. 759–773. 3 indexed citations
10.
Nogués, Isabel, B. Sekula, Sebastiana Angelaccio, et al.. (2022). Arabidopsis thaliana serine hydroxymethyltransferases: functions, structures, and perspectives. Plant Physiology and Biochemistry. 187. 37–49. 13 indexed citations
11.
Urbanowicz, Anna, et al.. (2021). 3D Domain Swapping Dimerization of the Receiver Domain of Cytokinin Receptor CRE1 From Arabidopsis thaliana and Medicago truncatula. Frontiers in Plant Science. 12. 756341–756341. 5 indexed citations
12.
Lemak, Sofia, Anna N. Khusnutdinova, M. Ruszkowski, et al.. (2021). Structural and biochemical insights into CRISPR RNA processing by the Cas5c ribonuclease SMU1763 from Streptococcus mutans. Journal of Biological Chemistry. 297(5). 101251–101251. 2 indexed citations
13.
Sekula, B., M. Ruszkowski, S. Ranganathan, et al.. (2020). Base pairing, structural and functional insights into N4-methylcytidine (m4C) and N4,N4-dimethylcytidine (m42C) modified RNA. Nucleic Acids Research. 48(18). 10087–10100. 15 indexed citations
14.
Ruszkowska, Agnieszka, et al.. (2019). Molecular structure of a U•A-U-rich RNA triple helix with 11 consecutive base triples. Nucleic Acids Research. 48(6). 3304–3314. 11 indexed citations
15.
Sekula, B., M. Ruszkowski, & Zbigniew Dauter. (2018). Structural Analysis of Phosphoserine Aminotransferase (Isoform 1) From Arabidopsis thaliana– the Enzyme Involved in the Phosphorylated Pathway of Serine Biosynthesis. Frontiers in Plant Science. 9. 876–876. 20 indexed citations
16.
17.
Forlani, Giuseppe, et al.. (2015). Functional properties and structural characterization of rice δ1-pyrroline-5-carboxylate reductase. Frontiers in Plant Science. 6. 565–565. 24 indexed citations
18.
Forlani, Giuseppe, Kira S. Makarova, M. Ruszkowski, Michele Bertazzini, & B. Nocek. (2015). Evolution of plant δ1-pyrroline-5-carboxylate reductases from phylogenetic and structural perspectives. Frontiers in Plant Science. 6. 567–567. 20 indexed citations
19.
Ruszkowski, M., Krzysztof Brzeziński, R. Jedrzejczak, et al.. (2013). Medicago truncatula histidine‐containing phosphotransfer protein. FEBS Journal. 280(15). 3709–3720. 13 indexed citations
20.
Ruszkowski, M., et al.. (1970). Inheritance of the seed dormancy stage duration in winter wheat (Triticum aestivum L.).. Genetica Polonica. 11(2). 227–240. 2 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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