Paul R. Rosevear

2.9k total citations
67 papers, 2.4k citations indexed

About

Paul R. Rosevear is a scholar working on Molecular Biology, Cardiology and Cardiovascular Medicine and Spectroscopy. According to data from OpenAlex, Paul R. Rosevear has authored 67 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 43 papers in Molecular Biology, 29 papers in Cardiology and Cardiovascular Medicine and 12 papers in Spectroscopy. Recurrent topics in Paul R. Rosevear's work include Cardiomyopathy and Myosin Studies (21 papers), RNA and protein synthesis mechanisms (19 papers) and Cardiac electrophysiology and arrhythmias (12 papers). Paul R. Rosevear is often cited by papers focused on Cardiomyopathy and Myosin Studies (21 papers), RNA and protein synthesis mechanisms (19 papers) and Cardiac electrophysiology and arrhythmias (12 papers). Paul R. Rosevear collaborates with scholars based in United States, Sweden and Finland. Paul R. Rosevear's co-authors include R. John Solaro, Jack W. Howarth, Natosha L. Finley, Vadim Gaponenko, Albert S. Mildvan, Shelagh Ferguson‐Miller, Jeffrey H. Baxter, Ekram Abusamhadneh, M.Bret Abbott and Robert Barker and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Paul R. Rosevear

66 papers receiving 2.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Paul R. Rosevear United States 30 1.6k 1.1k 364 307 232 67 2.4k
Christine B. Karim United States 26 1.2k 0.8× 492 0.5× 369 1.0× 235 0.8× 43 0.2× 43 1.6k
Franck Travers France 24 1.1k 0.7× 689 0.6× 128 0.4× 164 0.5× 52 0.2× 70 1.7k
Vadim Gaponenko United States 33 2.0k 1.3× 270 0.3× 663 1.8× 580 1.9× 112 0.5× 77 3.1k
Nathaniel J. Traaseth United States 36 1.9k 1.2× 311 0.3× 1.0k 2.9× 579 1.9× 125 0.5× 73 3.0k
R.S. Taylor United Kingdom 5 934 0.6× 849 0.8× 83 0.2× 180 0.6× 81 0.3× 5 1.5k
Philippe Wahl France 22 727 0.5× 198 0.2× 203 0.6× 166 0.5× 90 0.4× 47 1.2k
Kazutoshi Yamamoto United States 28 740 0.5× 211 0.2× 912 2.5× 453 1.5× 129 0.6× 70 2.0k
Serge Fermandjian France 31 2.0k 1.3× 92 0.1× 410 1.1× 248 0.8× 486 2.1× 148 2.7k
J.M. Ruysschaert Belgium 21 1.1k 0.7× 172 0.2× 102 0.3× 67 0.2× 113 0.5× 57 1.6k
Ronald E. Reid Canada 23 928 0.6× 261 0.2× 132 0.4× 148 0.5× 60 0.3× 45 1.5k

Countries citing papers authored by Paul R. Rosevear

Since Specialization
Citations

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

Fields of papers citing papers by Paul R. Rosevear

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Paul R. Rosevear. 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 Paul R. Rosevear. The network helps show where Paul R. Rosevear may publish in the future.

Co-authorship network of co-authors of Paul R. Rosevear

This figure shows the co-authorship network connecting the top 25 collaborators of Paul R. Rosevear. A scholar is included among the top collaborators of Paul R. Rosevear 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 Paul R. Rosevear. Paul R. Rosevear 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.
Cheng, Yuanhua, Steffen Lindert, Peter M. Kekenes–Huskey, et al.. (2014). Computational Studies of the Effect of the S23D/S24D Troponin I Mutation on Cardiac Troponin Structural Dynamics. Biophysical Journal. 107(7). 1675–1685. 45 indexed citations
2.
Michalek, Arthur J., Jack W. Howarth, James Gulick, et al.. (2013). Phosphorylation Modulates the Mechanical Stability of the Cardiac Myosin-Binding Protein C Motif. Biophysical Journal. 104(2). 442–452. 22 indexed citations
3.
Howarth, Jack W., et al.. (2012). Structural Insight into Unique Cardiac Myosin-binding Protein-C Motif. Journal of Biological Chemistry. 287(11). 8254–8262. 43 indexed citations
4.
Howarth, Jack W., Jarek Meller, R. John Solaro, Jill Trewhella, & Paul R. Rosevear. (2007). Phosphorylation-dependent Conformational Transition of the Cardiac Specific N-Extension of Troponin I in Cardiac Troponin. Journal of Molecular Biology. 373(3). 706–722. 77 indexed citations
5.
Sorsa, Tia, Piero Pollesello, Paul R. Rosevear, Torbjörn Drakenberg, & Ilkka Kilpeläinen. (2004). Stereoselective binding of levosimendan to cardiac troponin C causes Ca2+-sensitization. European Journal of Pharmacology. 486(1). 1–8. 53 indexed citations
6.
Abusamhadneh, Ekram, et al.. (2002). Solution Structure of Calcium-saturated Cardiac Troponin C Bound to Cardiac Troponin I. Journal of Biological Chemistry. 277(41). 38565–38570. 27 indexed citations
7.
Abusamhadneh, Ekram, et al.. (2001). Interaction of bepridil with the cardiac troponin C/troponin I complex. FEBS Letters. 506(1). 51–54. 15 indexed citations
8.
Finley, Natosha L., et al.. (2000). Magnesium–Calcium Exchange in Cardiac Troponin C Bound to Cardiac Troponin I. Journal of Molecular and Cellular Cardiology. 32(8). 1439–1446. 26 indexed citations
9.
Gaponenko, Vadim, Ekram Abusamhadneh, M.Bret Abbott, et al.. (1999). Effects of Troponin I Phosphorylation on Conformational Exchange in the Regulatory Domain of Cardiac Troponin C. Journal of Biological Chemistry. 274(24). 16681–16684. 64 indexed citations
10.
Finley, Natosha L., M.Bret Abbott, Ekram Abusamhadneh, et al.. (1999). NMR analysis of cardiac troponin C‐troponin I complexes: effects of phosphorylation. FEBS Letters. 453(1-2). 107–112. 87 indexed citations
11.
Zhou, Li & Paul R. Rosevear. (1995). Mutation of the Carboxy Terminal Zinc Finger of E. Coli Isoleucyl-tRNA Synthetase Alters Zinc Binding and Aminoacylation Activity. Biochemical and Biophysical Research Communications. 216(2). 648–654. 3 indexed citations
12.
Xu, Bo, et al.. (1994). Probing the metal binding sites of Escherichia coli isoleucyl-tRNA synthetase. Biochemistry. 33(2). 398–402. 9 indexed citations
13.
Xu, Baojun, George A. Krudy, & Paul R. Rosevear. (1993). Identification of the metal ligands and characterization of a putative zinc finger in methionyl-tRNA synthetase. Journal of Biological Chemistry. 268(22). 16259–16264. 15 indexed citations
14.
Williams, James S. & Paul R. Rosevear. (1991). A novel .alpha.-proton exchange reaction catalyzed by Escherichia coli methionyl-tRNA synthetase. Biochemistry. 30(26). 6412–6416. 3 indexed citations
15.
Williams, James S. & Paul R. Rosevear. (1991). Nuclear overhauser effect studies of the conformations of MG(α, β-Methylene)ATP bound to E. coli isoleucyl-tRNA synthetase. Biochemical and Biophysical Research Communications. 176(2). 682–689. 4 indexed citations
16.
Brito, Rui M. M., John A. Putkey, N.C.J. Strynadka, Michael N.G. James, & Paul R. Rosevear. (1991). Comparative NMR studies on cardiac troponin C and a mutant incapable of binding calcium at site II. Biochemistry. 30(42). 10236–10245. 25 indexed citations
17.
Rosevear, Paul R. & Albert S. Mildvan. (1989). [17] Ligand conformations and ligand-enzyme interactions as studied by the nuclear overhauser effect. Methods in enzymology on CD-ROM/Methods in enzymology. 177. 333–358. 29 indexed citations
18.
Krudy, George A., et al.. (1989). Protein matrix effects on glycan processing by mannosidase II and sialyl transferase from rat liver. Biochemistry. 28(9). 4077–4083. 7 indexed citations
19.
Rosevear, Paul R.. (1988). Purification and NMR studies of [13C-methyl]methionine-labeled truncated methionyl-tRNA synthetase. Biochemistry. 27(20). 7931–7939. 12 indexed citations
20.
Rosevear, Paul R., et al.. (1987). Nuclear Overhauser effect studies on the conformation of magnesium adenosine 5'-triphosphate bound to rabbit muscle creatine kinase. Biochemistry. 26(17). 5338–5344. 18 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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