Leo Spyracopoulos

2.8k total citations
57 papers, 2.3k citations indexed

About

Leo Spyracopoulos is a scholar working on Molecular Biology, Cardiology and Cardiovascular Medicine and Materials Chemistry. According to data from OpenAlex, Leo Spyracopoulos has authored 57 papers receiving a total of 2.3k indexed citations (citations by other indexed papers that have themselves been cited), including 49 papers in Molecular Biology, 11 papers in Cardiology and Cardiovascular Medicine and 9 papers in Materials Chemistry. Recurrent topics in Leo Spyracopoulos's work include Ubiquitin and proteasome pathways (20 papers), Protein Structure and Dynamics (14 papers) and Cardiomyopathy and Myosin Studies (11 papers). Leo Spyracopoulos is often cited by papers focused on Ubiquitin and proteasome pathways (20 papers), Protein Structure and Dynamics (14 papers) and Cardiomyopathy and Myosin Studies (11 papers). Leo Spyracopoulos collaborates with scholars based in Canada, United States and United Kingdom. Leo Spyracopoulos's co-authors include Brian D. Sykes, Monica X. Li, Stéphane M. Gagné, Wei Xiao, Craig J. Markin, Samuel K. Sia, Landon Pastushok, Murali Chandra, R. John Solaro and Sean A. McKenna and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Nature Medicine.

In The Last Decade

Leo Spyracopoulos

57 papers receiving 2.2k citations

Peers

Leo Spyracopoulos
Dixie J. Goss United States
C. James McKnight United States
Terence Wagenknecht United States
M. Hennig United States
Steven M. Pascal United States
Deborah S. Wuttke United States
Dixie J. Goss United States
Leo Spyracopoulos
Citations per year, relative to Leo Spyracopoulos Leo Spyracopoulos (= 1×) peers Dixie J. Goss

Countries citing papers authored by Leo Spyracopoulos

Since Specialization
Citations

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

Fields of papers citing papers by Leo Spyracopoulos

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Leo Spyracopoulos

This figure shows the co-authorship network connecting the top 25 collaborators of Leo Spyracopoulos. A scholar is included among the top collaborators of Leo Spyracopoulos 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 Leo Spyracopoulos. Leo Spyracopoulos 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.
Joseph, Prem Raj B., Leo Spyracopoulos, & Krishna Rajarathnam. (2018). Dynamics-Derived Insights into Complex Formation between the CXCL8 Monomer and CXCR1 N-Terminal Domain: An NMR Study. Molecules. 23(11). 2825–2825. 4 indexed citations
2.
Rout, Manoj Kumar, et al.. (2018). Active Site Gate Dynamics Modulate the Catalytic Activity of the Ubiquitination Enzyme E2-25K. Scientific Reports. 8(1). 7002–7002. 12 indexed citations
3.
Ali, Mohammad, Hilmar Strickfaden, Brian L. Lee, Leo Spyracopoulos, & Michael J. Hendzel. (2018). RYBP Is a K63-Ubiquitin-Chain-Binding Protein that Inhibits Homologous Recombination Repair. Cell Reports. 22(2). 383–395. 23 indexed citations
4.
Lee, Brian, et al.. (2016). The Mechanism of Hsp90 ATPase Stimulation by Aha1. Scientific Reports. 6(1). 33179–33179. 52 indexed citations
5.
Baral, Pravas Kumar, Mridula Swayampakula, Manoj Kumar Rout, et al.. (2014). Structural Basis of Prion Inhibition by Phenothiazine Compounds. Structure. 22(2). 291–303. 49 indexed citations
6.
Anamika, Anamika, Craig J. Markin, Manoj Kumar Rout, & Leo Spyracopoulos. (2014). Molecular Basis for Impaired DNA Damage Response Function Associated with the RAP80 ΔE81 Defect. Journal of Biological Chemistry. 289(18). 12852–12862. 7 indexed citations
7.
Markin, Craig J. & Leo Spyracopoulos. (2012). Accuracy and precision of protein–ligand interaction kinetics determined from chemical shift titrations. Journal of Biomolecular NMR. 54(4). 355–376. 14 indexed citations
8.
Wu, Hong, Scott L. Pomeroy, Manuel Branco Ferreira, et al.. (2011). UBE4B promotes Hdm2-mediated degradation of the tumor suppressor p53. Nature Medicine. 17(3). 347–355. 96 indexed citations
9.
Slupsky, Carolyn M., Leo Spyracopoulos, Valerie Booth, Brian D. Sykes, & Matthew P. Crump. (2007). Probing nascent structures in peptides using natural abundance 13C NMR relaxation and reduced spectral density mapping. Proteins Structure Function and Bioinformatics. 67(1). 18–30. 7 indexed citations
10.
Pastushok, Landon, Leo Spyracopoulos, & Wei Xiao. (2007). Two Mms2 residues cooperatively interact with ubiquitin and are critical for Lys63 polyubiquitination in vitro and in vivo. FEBS Letters. 581(28). 5343–5348. 20 indexed citations
11.
Spyracopoulos, Leo. (2005). Thermodynamic Interpretation of Protein Dynamics from NMR Relaxation Measurements. Protein and Peptide Letters. 12(3). 235–240. 15 indexed citations
12.
Graether, Steffen P., Stéphane M. Gagné, Leo Spyracopoulos, et al.. (2003). Spruce Budworm Antifreeze Protein: Changes in Structure and Dynamics at Low Temperature. Journal of Molecular Biology. 327(5). 1155–1168. 28 indexed citations
13.
McKenna, Sean A., Leo Spyracopoulos, Trevor F. Moraes, et al.. (2001). Noncovalent Interaction between Ubiquitin and the Human DNA Repair Protein Mms2 Is Required for Ubc13-mediated Polyubiquitination. Journal of Biological Chemistry. 276(43). 40120–40126. 112 indexed citations
14.
Spyracopoulos, Leo & Brian D. Sykes. (2001). Thermodynamic insights into proteins from NMR spin relaxation studies. Current Opinion in Structural Biology. 11(5). 555–559. 25 indexed citations
15.
Suh, Jeong‐Yong, Leo Spyracopoulos, David W. Keizer, Randall T. Irvin, & Brian D. Sykes. (2001). Backbone Dynamics of Receptor Binding and Antigenic Regions of a Pseudomonas aeruginosa Pilin Monomer. Biochemistry. 40(13). 3985–3995. 15 indexed citations
16.
Campbell, A. Patricia, Leo Spyracopoulos, Randall T. Irvin, & Brian D. Sykes. (2000). Backbone dynamics of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pilin strain PAK from heteronuclear 1H-15N NMR spectroscopy. Journal of Biomolecular NMR. 17(3). 239–255. 22 indexed citations
17.
Crump, Matthew P., Leo Spyracopoulos, Pierre Lavigne, et al.. (1999). Backbone dynamics of the human cc chemokine eotaxin: Fast motions, slow motions, and implications for receptor binding. Protein Science. 8(10). 2041–2054. 31 indexed citations
18.
Gagné, Stéphane M., et al.. (1998). Backbone and methyl dynamics of the regulatory domain of troponin C: anisotropic rotational diffusion and contribution of conformational entropy to calcium affinity. Journal of Molecular Biology. 278(3). 667–686. 110 indexed citations
19.
Sia, Samuel K., Monica X. Li, Leo Spyracopoulos, et al.. (1997). Structure of Cardiac Muscle Troponin C Unexpectedly Reveals a Closed Regulatory Domain. Journal of Biological Chemistry. 272(29). 18216–18221. 165 indexed citations
20.
Spyracopoulos, Leo, et al.. (1996). Backbone dynamics of an alamethicin in methanol and aqueous detergent solution determined by heteronuclear 1H?15N NMR spectroscopy. Journal of Biomolecular NMR. 7(4). 283–94. 16 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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