Boguslaw Stec

6.6k total citations · 1 hit paper
106 papers, 5.3k citations indexed

About

Boguslaw Stec is a scholar working on Molecular Biology, Materials Chemistry and Biotechnology. According to data from OpenAlex, Boguslaw Stec has authored 106 papers receiving a total of 5.3k indexed citations (citations by other indexed papers that have themselves been cited), including 74 papers in Molecular Biology, 32 papers in Materials Chemistry and 13 papers in Biotechnology. Recurrent topics in Boguslaw Stec's work include Enzyme Structure and Function (30 papers), Biochemical and Molecular Research (18 papers) and Protein Structure and Dynamics (16 papers). Boguslaw Stec is often cited by papers focused on Enzyme Structure and Function (30 papers), Biochemical and Molecular Research (18 papers) and Protein Structure and Dynamics (16 papers). Boguslaw Stec collaborates with scholars based in United States, Poland and Japan. Boguslaw Stec's co-authors include Lukasz Lebioda, Evan R. Kantrowitz, Kathleen M. Holtz, Robert Liddington, Martha M. Teeter, Mary F. Roberts, Laurie A. Bankston, Wayne A. Marasco, Eugenio Santelli and W.C. Hwang and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Boguslaw Stec

104 papers receiving 5.2k citations

Hit Papers

Structural and functional... 2009 2026 2014 2020 2009 250 500 750

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Boguslaw Stec United States 38 3.1k 946 903 712 410 106 5.3k
Christine Ebel France 41 3.6k 1.1× 465 0.5× 795 0.9× 356 0.5× 335 0.8× 154 5.2k
Michael G. Prisant United States 13 5.2k 1.7× 462 0.5× 1.3k 1.5× 596 0.8× 507 1.2× 25 7.6k
A. D’Arcy Switzerland 41 4.0k 1.3× 470 0.5× 958 1.1× 832 1.2× 279 0.7× 61 7.0k
Andrew A. McCarthy France 32 2.9k 0.9× 700 0.7× 600 0.7× 1.0k 1.4× 572 1.4× 75 5.0k
W.F. Anderson United States 53 6.7k 2.2× 504 0.5× 1.2k 1.3× 714 1.0× 365 0.9× 217 9.5k
G.L. Taylor United Kingdom 46 3.8k 1.2× 1.8k 1.9× 1.4k 1.6× 538 0.8× 188 0.5× 109 6.1k
Sam‐Yong Park Japan 42 3.5k 1.1× 939 1.0× 539 0.6× 411 0.6× 286 0.7× 151 5.8k
Narayanaswamy Srinivasan India 38 3.7k 1.2× 403 0.4× 942 1.0× 429 0.6× 249 0.6× 232 5.1k
Osnat Herzberg United States 40 4.0k 1.3× 362 0.4× 1.4k 1.6× 531 0.7× 285 0.7× 135 6.4k
Dmitri Beglov United States 30 5.1k 1.7× 492 0.5× 626 0.7× 752 1.1× 228 0.6× 51 6.9k

Countries citing papers authored by Boguslaw Stec

Since Specialization
Citations

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

Fields of papers citing papers by Boguslaw Stec

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Boguslaw Stec

This figure shows the co-authorship network connecting the top 25 collaborators of Boguslaw Stec. A scholar is included among the top collaborators of Boguslaw Stec 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 Boguslaw Stec. Boguslaw Stec 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.
Stec, Boguslaw, et al.. (2022). Complete Model of Vinculin Suggests the Mechanism of Activation by Helical Super-Bundle Unfurling. The Protein Journal. 41(1). 55–70. 3 indexed citations
2.
Lipper, Colin H., Heidi Erlandsen, James L. Cole, et al.. (2019). Design of High-Affinity Metal-Controlled Protein Dimers. Biochemistry. 58(17). 2199–2207. 9 indexed citations
3.
Ratnikov, Boris I., Piotr Cieplak, Kosi Gramatikoff, et al.. (2014). Basis for substrate recognition and distinction by matrix metalloproteinases. Proceedings of the National Academy of Sciences. 111(40). 70 indexed citations
4.
Cheng, Jiongjia, et al.. (2012). Competition between Anion Binding and Dimerization Modulates Staphylococcus aureus Phosphatidylinositol-specific Phospholipase C Enzymatic Activity. Journal of Biological Chemistry. 287(48). 40317–40327. 11 indexed citations
5.
Stec, Boguslaw, et al.. (2011). Chinese hamster AP endonuclease operates by a two‐metal ion assisted catalytic mechanism. FEBS Letters. 586(3). 242–247. 1 indexed citations
6.
Remacle, Albert G., Sergey A. Shiryaev, Ilian Radichev, et al.. (2011). Dynamic Interdomain Interactions Contribute to the Inhibition of Matrix Metalloproteinases by Tissue Inhibitors of Metalloproteinases. Journal of Biological Chemistry. 286(23). 21002–21012. 15 indexed citations
7.
Aleshin, Alexander E., Svetlana Gramatikova, Greg L. Hura, et al.. (2009). Crystal and Solution Structures of a Prokaryotic M16B Peptidase: an Open and Shut Case. Structure. 17(11). 1465–1475. 27 indexed citations
8.
Rodionov, Dmitry A., Oleg V. Kurnasov, Boguslaw Stec, et al.. (2007). Genomic identification and in vitro reconstitution of a complete biosynthetic pathway for the osmolyte di- myo -inositol-phosphate. Proceedings of the National Academy of Sciences. 104(11). 4279–4284. 39 indexed citations
9.
Hwang, W.C., Eugenio Santelli, Lukasz Jaroszewski, et al.. (2007). Structural Basis of Neutralization By a Human Anti-Sars Spike Protein Antibody, 80r. Journal of Biological Chemistry. 281. 2 indexed citations
10.
Stec, Boguslaw, Mark Williams, Kimberly A. Stieglitz, & Evan R. Kantrowitz. (2007). Comparison of two T-state structures of regulatory-chain mutants ofEscherichia coliaspartate transcarbamoylase suggests that His20 and Asp19 modulate the response to heterotropic effectors. Acta Crystallographica Section D Biological Crystallography. 63(12). 1243–1253. 1 indexed citations
11.
Johnson, Kenneth A., et al.. (2005). Crystal structure of α‐hordothionin at 1.9 Å resolution. FEBS Letters. 579(11). 2301–2306. 12 indexed citations
12.
Stieglitz, Kimberly A., Boguslaw Stec, Darren P. Baker, & Evan R. Kantrowitz. (2004). Monitoring the Transition from the T to the R State in E.coli Aspartate Transcarbamoylase by X-ray Crystallography: Crystal Structures of the E50A Mutant Enzyme in Four Distinct Allosteric States. Journal of Molecular Biology. 341(3). 853–868. 33 indexed citations
13.
Bambai, Bijan, Corina E. Rogge, Boguslaw Stec, & Richard J. Kulmacz. (2004). Role of Asn-382 and Thr-383 in Activation and Inactivation of Human Prostaglandin H Synthase Cyclooxygenase Catalysis. Journal of Biological Chemistry. 279(6). 4084–4092. 24 indexed citations
14.
Stieglitz, Kimberly A., Barbara A. Seaton, J. W. Head, Boguslaw Stec, & Mary F. Roberts. (2003). Unexpected similarity in regulation between an archaeal inositol monophosphatase/fructose bisphosphatase and chloroplast fructose bisphosphatase. Protein Science. 12(4). 760–767. 6 indexed citations
15.
Stieglitz, Kimberly A., Kenneth A. Johnson, Hongying Yang, et al.. (2002). Crystal Structure of a Dual Activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. Journal of Biological Chemistry. 277(25). 22863–22874. 45 indexed citations
16.
Stec, Boguslaw, Robert F. Troxler, & Martha M. Teeter. (1999). Crystal Structure of C-Phycocyanin from Cyanidium caldarium Provides a New Perspective on Phycobilisome Assembly. Biophysical Journal. 76(6). 2912–2921. 78 indexed citations
17.
Jin, Lei, Boguslaw Stec, W. N. Lipscomb, & Evan R. Kantrowitz. (1999). Insights into the mechanisms of catalysis and heterotropic regulation ofEscherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogueN-phosphonacetyl-L-aspartate at 2.1 ?. Proteins Structure Function and Bioinformatics. 37(4). 729–742. 64 indexed citations
18.
Stec, Boguslaw, et al.. (1996). Expression, purification and characterization of recombinant crambin. Protein Engineering Design and Selection. 9(12). 1233–1239. 16 indexed citations
19.
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
20.
Stec, Boguslaw. (1985). Solution of the one-dimensional Schroedinger equation for a double-well potential with finite walls. Acta Physica Polonica A. 68(5). 681–693. 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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