Lukasz Lebioda

4.6k total citations
126 papers, 3.7k citations indexed

About

Lukasz Lebioda is a scholar working on Molecular Biology, Materials Chemistry and Organic Chemistry. According to data from OpenAlex, Lukasz Lebioda has authored 126 papers receiving a total of 3.7k indexed citations (citations by other indexed papers that have themselves been cited), including 71 papers in Molecular Biology, 54 papers in Materials Chemistry and 34 papers in Organic Chemistry. Recurrent topics in Lukasz Lebioda's work include Enzyme Structure and Function (44 papers), Biochemical and Molecular Research (19 papers) and S100 Proteins and Annexins (18 papers). Lukasz Lebioda is often cited by papers focused on Enzyme Structure and Function (44 papers), Biochemical and Molecular Research (19 papers) and S100 Proteins and Annexins (18 papers). Lukasz Lebioda collaborates with scholars based in United States, Poland and Canada. Lukasz Lebioda's co-authors include Boguslaw Stec, John M. Brewer, Daniel L. Reger, W. Minor, L.L. Lovelace, K. Lewiński, M. Chruszcz, Heping Zheng, Sondra H. Berger and Eric A. Ortlund and has published in prestigious journals such as Nature, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Lukasz Lebioda

125 papers receiving 3.6k citations

Peers

Lukasz Lebioda
J. W. Pflugrath United States
Peter F. Lindley United Kingdom
M.A. Carrondo Portugal
Nobutoshi Ito Japan
Karen N. Allen United States
W. Rypniewski Poland
Vilmos Fülöp United Kingdom
Matthew M. Benning United States
J.M. Guss Australia
Angela Lombardi Italy
J. W. Pflugrath United States
Lukasz Lebioda
Citations per year, relative to Lukasz Lebioda Lukasz Lebioda (= 1×) peers J. W. Pflugrath

Countries citing papers authored by Lukasz Lebioda

Since Specialization
Citations

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

Fields of papers citing papers by Lukasz Lebioda

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Lukasz Lebioda

This figure shows the co-authorship network connecting the top 25 collaborators of Lukasz Lebioda. A scholar is included among the top collaborators of Lukasz Lebioda 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 Lukasz Lebioda. Lukasz Lebioda 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.
Lebioda, Lukasz, et al.. (2011). Evolution of Metamorphism in Thymidylate Synthases Within the Primate Lineages. Journal of Molecular Evolution. 72(3). 306–314. 4 indexed citations
3.
Lovelace, L.L., Christopher L. Cooper, James M. Sodetz, & Lukasz Lebioda. (2011). Structure of Human C8 Protein Provides Mechanistic Insight into Membrane Pore Formation by Complement. Journal of Biological Chemistry. 286(20). 17585–17592. 80 indexed citations
4.
Minor, W., et al.. (2011). Mechanism of N10‐formyltetrahydrofolate synthetase derived from complexes with intermediates and inhibitors. Protein Science. 21(2). 219–228. 17 indexed citations
5.
Lovelace, L.L., et al.. (2009). Variants of human thymidylate synthase with loop 181–197 stabilized in the inactive conformation. Protein Science. 18(8). 1628–1636. 15 indexed citations
6.
Dingra, Nin N., et al.. (2008). Structure of the thioredoxin-like domain of yeast glutaredoxin 3. Acta Crystallographica Section D Biological Crystallography. 64(9). 927–932. 15 indexed citations
7.
Lovelace, L.L., et al.. (2007). Structural features of the ligand binding site on human complement protein C8γ: A member of the lipocalin family. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1774(5). 637–644. 10 indexed citations
8.
9.
Phan, Jason, David Steadman, W. Minor, et al.. (2001). Structure of Human Thymidylate Synthase Suggests Advantages of Chemotherapy with Noncompetitive Inhibitors. Journal of Biological Chemistry. 276(17). 14170–14177. 66 indexed citations
10.
Brewer, John M., Michael J. Holland, & Lukasz Lebioda. (2000). The H159A Mutant of Yeast Enolase 1 Has Significant Activity. Biochemical and Biophysical Research Communications. 276(3). 1199–1202. 9 indexed citations
11.
Lebioda, Lukasz. (2000). The honorary enzyme haemoglobin turns out to be a real enzyme. Cellular and Molecular Life Sciences. 57(13). 1817–1819. 7 indexed citations
12.
Chen, Yung Pin, et al.. (2000). The Crystal Structure and Amino Acid Sequence of Dehaloperoxidase from Amphitrite ornata Indicate Common Ancestry with Globins. Journal of Biological Chemistry. 275(25). 18712–18716. 95 indexed citations
13.
Lebioda, Lukasz, et al.. (1999). An enzymatic globin from a marine worm. Nature. 401(6752). 445–445. 80 indexed citations
14.
Brewer, John M., Claiborne V.C. Glover, Michael J. Holland, & Lukasz Lebioda. (1998). Significance of the enzymatic properties of yeast S39A enolase to the catalytic mechanism. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1383(2). 351–355. 19 indexed citations
15.
Brewer, John M., Claiborne V.C. Glover, Michael J. Holland, & Lukasz Lebioda. (1997). Effect of site-directed mutagenesis of His373 of yeast enolase on some of its physical and enzymatic properties. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1340(1). 88–96. 20 indexed citations
16.
17.
Lebioda, Lukasz, et al.. (1993). Fluoride inhibition of yeast enolase: Crystal structure of the enolase–Mg2+–F−–Pi complex at 2.6 Å resolution. Proteins Structure Function and Bioinformatics. 16(3). 219–225. 36 indexed citations
18.
Lebioda, Lukasz & Boguslaw Stec. (1991). Mechanism of enolase: the crystal structure of enolase-magnesium-2-phosphoglycerate/phosphoenolpyruvate complex at 2.2-.ANG. resolution. Biochemistry. 30(11). 2817–2822. 94 indexed citations
19.
Lebioda, Lukasz, et al.. (1990). X‐ray crystal structure of sangivamycin, a potent inhibitor of protein kinases. FEBS Letters. 266(1-2). 102–104. 5 indexed citations
20.
Lebioda, Lukasz & Boguslaw Stec. (1988). Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor. Nature. 333(6174). 683–686. 85 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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