Michael J. Bogusky

2.2k total citations
28 papers, 1.2k citations indexed

About

Michael J. Bogusky is a scholar working on Molecular Biology, Materials Chemistry and Organic Chemistry. According to data from OpenAlex, Michael J. Bogusky has authored 28 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Molecular Biology, 8 papers in Materials Chemistry and 6 papers in Organic Chemistry. Recurrent topics in Michael J. Bogusky's work include Protein Structure and Dynamics (12 papers), Enzyme Structure and Function (6 papers) and Glycosylation and Glycoproteins Research (4 papers). Michael J. Bogusky is often cited by papers focused on Protein Structure and Dynamics (12 papers), Enzyme Structure and Function (6 papers) and Glycosylation and Glycoproteins Research (4 papers). Michael J. Bogusky collaborates with scholars based in United States, Slovakia and Germany. Michael J. Bogusky's co-authors include Paul Anderson, Stanley J. Opella, Theresa Wood, Keith M. Witherup, Richard W. Ransom, Harri G. Ramjit, Mohinder K. Sardana, Victor M. Garsky, Joseph G. Joyce and Richard A. Smith and has published in prestigious journals such as Nature, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Michael J. Bogusky

28 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Michael J. Bogusky United States 18 836 195 150 144 141 28 1.2k
Gregor Zlokarnik United States 10 1.1k 1.3× 97 0.5× 30 0.2× 279 1.9× 58 0.4× 11 1.7k
Kazuo Shinozuka Japan 21 1.9k 2.3× 195 1.0× 245 1.6× 105 0.7× 46 0.3× 107 2.7k
Jennifer Reed Germany 22 1.6k 1.9× 113 0.6× 51 0.3× 122 0.8× 102 0.7× 44 2.4k
Kevin Ryan United States 28 2.4k 2.9× 97 0.5× 81 0.5× 323 2.2× 92 0.7× 68 3.2k
Per Haberkant Germany 20 1.5k 1.8× 194 1.0× 281 1.9× 75 0.5× 63 0.4× 37 2.0k
Gerald W. Gordon United States 11 1.4k 1.6× 173 0.9× 36 0.2× 211 1.5× 86 0.6× 19 2.3k
Jacqueline R. Wyatt United States 23 2.6k 3.1× 104 0.5× 136 0.9× 110 0.8× 88 0.6× 34 3.1k
Asami Makino Japan 27 2.1k 2.5× 186 1.0× 36 0.2× 225 1.6× 31 0.2× 54 2.8k
M. Ohno Japan 16 768 0.9× 272 1.4× 79 0.5× 123 0.9× 35 0.2× 29 1.3k
Arnaud Leroy France 23 1.0k 1.2× 194 1.0× 32 0.2× 175 1.2× 70 0.5× 38 1.6k

Countries citing papers authored by Michael J. Bogusky

Since Specialization
Citations

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

Fields of papers citing papers by Michael J. Bogusky

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Michael J. Bogusky. 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 Michael J. Bogusky. The network helps show where Michael J. Bogusky may publish in the future.

Co-authorship network of co-authors of Michael J. Bogusky

This figure shows the co-authorship network connecting the top 25 collaborators of Michael J. Bogusky. A scholar is included among the top collaborators of Michael J. Bogusky 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 Michael J. Bogusky. Michael J. Bogusky 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.
McGaughey, Georgia B., Christopher I. Bayly, Christopher D. Cox, et al.. (2014). Shaping suvorexant: application of experimental and theoretical methods for driving synthetic designs. Journal of Computer-Aided Molecular Design. 28(1). 5–12. 12 indexed citations
2.
Coleman, Paul J., John D. Schreier, Georgia B. McGaughey, et al.. (2010). Design and synthesis of conformationally constrained N,N-disubstituted 1,4-diazepanes as potent orexin receptor antagonists. Bioorganic & Medicinal Chemistry Letters. 20(7). 2311–2315. 12 indexed citations
3.
Cox, Christopher D., Georgia B. McGaughey, Michael J. Bogusky, et al.. (2009). Conformational analysis of N,N-disubstituted-1,4-diazepane orexin receptor antagonists and implications for receptor binding. Bioorganic & Medicinal Chemistry Letters. 19(11). 2997–3001. 43 indexed citations
4.
Nanda, Kausik K., Matthew J. Cato, Stefanie A. Kane, et al.. (2006). Potent antagonists of the Kv1.5 potassium channel: Synthesis and evaluation of analogous N,N-diisopropyl-2-(pyridine-3-yl)acetamides. Bioorganic & Medicinal Chemistry Letters. 16(22). 5897–5901. 11 indexed citations
5.
Bernier, Virginie, Rino Stocco, Michael J. Bogusky, et al.. (2006). Structure-Function Relationships in the Neuropeptide S Receptor. Journal of Biological Chemistry. 281(34). 24704–24712. 79 indexed citations
6.
Brady, Stephen F., Satendra Singh, M. Katharine Holloway, et al.. (2003). Rational design and synthesis of selective BACE-1 inhibitors. Bioorganic & Medicinal Chemistry Letters. 14(3). 601–604. 25 indexed citations
7.
Joyce, Joseph G., William M. Hurni, Michael J. Bogusky, et al.. (2002). Enhancement of α-Helicity in the HIV-1 Inhibitory Peptide DP178 Leads to an Increased Affinity for Human Monoclonal Antibody 2F5 but Does Not Elicit Neutralizing Responses in Vitro. Journal of Biological Chemistry. 277(48). 45811–45820. 96 indexed citations
8.
Dinsmore, Christopher J., Jeffrey M. Bergman, Michael J. Bogusky, et al.. (2001). 3,8-Diazabicyclo[3.2.1]octan-2-one Peptide Mimetics:  Synthesis of a Conformationally Restricted Inhibitor of Farnesyltransferase. Organic Letters. 3(6). 865–868. 25 indexed citations
9.
Bogusky, Michael J., Steven M. Pitzenberger, V M Garsky, et al.. (1999). Conformation of a novel tetrapeptide inhibitor NH2d‐Trp‐d‐Met‐Phe(pCl)‐Gla‐NH2bound to farnesyl‐protein transferase. Journal of Peptide Research. 54(1). 66–73. 7 indexed citations
10.
Kaufman, Michael J., et al.. (1996). Characterization of a Solid State Reaction Product from a Lyophilized Formulation of a Cyclic Heptapeptide. A Novel Example of an Excipient-Induced Oxidation. Pharmaceutical Research. 13(12). 1811–1814. 28 indexed citations
11.
Brady, Stephen F., John T. Sisko, Kenneth J. Stauffer, et al.. (1995). Amide and α-keto carbonyl inhibitors of thrombin based on arginine and lysine: Synthesis, stability and biological characterization. Bioorganic & Medicinal Chemistry. 3(8). 1063–1078. 25 indexed citations
12.
Koblan, Kenneth S., Scott D. Mosser, Charles A. Omer, et al.. (1995). NMR studies of novel inhibitors bound to farnesyl‐protein transferase. Protein Science. 4(4). 681–688. 30 indexed citations
13.
Witherup, Keith M., Michael J. Bogusky, Paul Anderson, et al.. (1994). Cyclopsychotride A, a Biologically Active, 31-Residue Cyclic Peptide Isolated from Psychotria longipes. Journal of Natural Products. 57(12). 1619–1625. 217 indexed citations
14.
Middaugh, C. Russell, James A. Ryan, Carl J. Burke, et al.. (1993). Structure of synthetic peptide analogues of an eggshell protein of Schistosoma mansoni. Protein Science. 2(6). 900–914. 3 indexed citations
15.
Bogusky, Michael J., Adel M. Naylor, Michael Mertzman, et al.. (1993). The solution conformation Ac‐Pen‐Arg‐Gly‐Asp‐Cys‐OH, a potent fibrinogen receptor antagonist. Biopolymers. 33(8). 1287–1297. 14 indexed citations
16.
Bogusky, Michael J., Adel M. Naylor, Steven M. Pitzenberger, et al.. (1992). NMR and molecular modeling characterization of RGD containing peptides. International journal of peptide & protein research. 39(1). 63–76. 48 indexed citations
17.
Bogusky, Michael J., Christopher M. Dobson, & Richard A. Smith. (1989). Reversible independent unfolding of the domains of urokinase monitored by proton NMR. Biochemistry. 28(16). 6728–6735. 34 indexed citations
18.
Oswald, Robert E., Michael J. Bogusky, Michelle Bamberger, Richard A. Smith, & Christopher M. Dobson. (1989). Dynamics of the multidomain fibrinolytic protein urokinase from two-dimensional NMR. Nature. 337(6207). 579–582. 55 indexed citations
19.
Bogusky, Michael J., Gregory C. Leo, & Stanley J. Opella. (1988). Comparison of the dynamics of the membrane‐bound form of fd coat protein in micelles and in bilayers by solution and solid‐state nitrogen‐15 nuclear magnetic resonance spectroscopy. Proteins Structure Function and Bioinformatics. 4(2). 123–130. 15 indexed citations
20.
Bogusky, Michael J., et al.. (1988). Secondary structure of filamentous bacteriophage coat protein is preserved in lipid environments. Journal of Molecular Biology. 200(4). 741–743. 9 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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