Richard L. Rotundo

3.6k total citations
42 papers, 2.5k citations indexed

About

Richard L. Rotundo is a scholar working on Pharmacology, Computational Theory and Mathematics and Molecular Biology. According to data from OpenAlex, Richard L. Rotundo has authored 42 papers receiving a total of 2.5k indexed citations (citations by other indexed papers that have themselves been cited), including 35 papers in Pharmacology, 18 papers in Computational Theory and Mathematics and 17 papers in Molecular Biology. Recurrent topics in Richard L. Rotundo's work include Cholinesterase and Neurodegenerative Diseases (35 papers), Computational Drug Discovery Methods (18 papers) and Pesticide Exposure and Toxicity (14 papers). Richard L. Rotundo is often cited by papers focused on Cholinesterase and Neurodegenerative Diseases (35 papers), Computational Drug Discovery Methods (18 papers) and Pesticide Exposure and Toxicity (14 papers). Richard L. Rotundo collaborates with scholars based in United States, Canada and Israel. Richard L. Rotundo's co-authors include Susana G. Rossi, Douglas M. Fambrough, H. Benjamin Peng, D M Fambrough, Hongbo Xie, Christian Jacobson, Patrice D. Côté, Salvatore Carbonetto, Eri Arikawa‐Hirasawa and Yoshihiko Yamada and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Richard L. Rotundo

42 papers receiving 2.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Richard L. Rotundo United States 28 1.5k 1.1k 583 453 422 42 2.5k
Claire Legay France 21 897 0.6× 795 0.7× 440 0.8× 428 0.9× 206 0.5× 48 1.7k
Hugo L. Fernández United States 25 690 0.5× 652 0.6× 619 1.1× 174 0.4× 290 0.7× 62 1.8k
Luigi Di Giamberardino France 26 1.1k 0.7× 468 0.4× 608 1.0× 144 0.3× 270 0.6× 56 2.1k
Richard Killick United Kingdom 29 2.1k 1.4× 453 0.4× 887 1.5× 184 0.4× 310 0.7× 84 4.0k
Jeanine Koenig France 21 845 0.6× 566 0.5× 543 0.9× 119 0.3× 245 0.6× 51 1.5k
Wenming Li China 24 788 0.5× 389 0.3× 323 0.6× 167 0.4× 216 0.5× 54 1.8k
William J. Netzer United States 17 1.4k 0.9× 328 0.3× 361 0.6× 178 0.4× 393 0.9× 29 2.4k
J. Steven Jacobsen United States 26 1.2k 0.8× 457 0.4× 568 1.0× 254 0.6× 218 0.5× 44 2.8k
David Westaway Canada 18 1.2k 0.8× 660 0.6× 554 1.0× 515 1.1× 340 0.8× 29 2.8k
Amaya García-Muñoz Ireland 12 1.6k 1.1× 637 0.6× 933 1.6× 438 1.0× 426 1.0× 15 3.8k

Countries citing papers authored by Richard L. Rotundo

Since Specialization
Citations

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

Fields of papers citing papers by Richard L. Rotundo

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Richard L. Rotundo. 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 Richard L. Rotundo. The network helps show where Richard L. Rotundo may publish in the future.

Co-authorship network of co-authors of Richard L. Rotundo

This figure shows the co-authorship network connecting the top 25 collaborators of Richard L. Rotundo. A scholar is included among the top collaborators of Richard L. Rotundo 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 Richard L. Rotundo. Richard L. Rotundo 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.
Rossi, Susana G., et al.. (2015). Rescue and Stabilization of Acetylcholinesterase in Skeletal Muscle by N-terminal Peptides Derived from the Noncatalytic Subunits. Journal of Biological Chemistry. 290(34). 20774–20781. 5 indexed citations
2.
Wang, Xiao, Alicia M. Pickrell, Susana G. Rossi, et al.. (2013). Transient systemic mtDNA damage leads to muscle wasting by reducing the satellite cell pool. Human Molecular Genetics. 22(19). 3976–3986. 45 indexed citations
3.
Mercado, Mary Lynn T., Hiroki Hagiwara, Beth A. McKechnie, et al.. (2012). Biglycan Is an Extracellular MuSK Binding Protein Important for Synapse Stability. Journal of Neuroscience. 32(7). 2324–2334. 56 indexed citations
4.
Rossi, Susana G., et al.. (2011). Translational Regulation of Acetylcholinesterase by the RNA-binding Protein Pumilio-2 at the Neuromuscular Synapse. Journal of Biological Chemistry. 286(42). 36492–36499. 14 indexed citations
5.
Rotundo, Richard L., et al.. (2009). Limiting Role of Protein Disulfide Isomerase in the Expression of Collagen-tailed Acetylcholinesterase Forms in Muscle. Journal of Biological Chemistry. 284(46). 31753–31763. 7 indexed citations
6.
Rotundo, Richard L., et al.. (2008). Assembly and regulation of acetylcholinesterase at the vertebrate neuromuscular junction. Chemico-Biological Interactions. 175(1-3). 26–29. 22 indexed citations
7.
Rotundo, Richard L., et al.. (2005). Targeting acetylcholinesterase to the neuromuscular synapse. Chemico-Biological Interactions. 157-158. 15–21. 24 indexed citations
8.
Ohno, Kinji, et al.. (2004). C-terminal and Heparin-binding Domains of Collagenic Tail Subunit Are Both Essential for Anchoring Acetylcholinesterase at the Synapse. Journal of Biological Chemistry. 279(12). 10997–11005. 67 indexed citations
9.
Rossi, Susana G., Ian M. Dickerson, & Richard L. Rotundo. (2003). Localization of the Calcitonin Gene-related Peptide Receptor Complex at the Vertebrate Neuromuscular Junction and Its Role in Regulating Acetylcholinesterase Expression. Journal of Biological Chemistry. 278(27). 24994–25000. 51 indexed citations
10.
Rotundo, Richard L.. (2003). Expression and localization of acetylcholinesterase at the neuromuscular junction. Journal of Neurocytology. 32(5-8). 743–766. 84 indexed citations
11.
Arikawa‐Hirasawa, Eri, Susana G. Rossi, Richard L. Rotundo, & Yoshihiko Yamada. (2002). Absence of acetylcholinesterase at the neuromuscular junctions of perlecan-null mice. Nature Neuroscience. 5(2). 119–123. 135 indexed citations
12.
Jacobson, Christian, Patrice D. Côté, Susana G. Rossi, Richard L. Rotundo, & Salvatore Carbonetto. (2001). The Dystroglycan Complex Is Necessary for Stabilization of Acetylcholine Receptor Clusters at Neuromuscular Junctions and Formation of the Synaptic Basement Membrane. The Journal of Cell Biology. 152(3). 435–450. 173 indexed citations
14.
Adams, Marvin E., Neal R. Kramarcy, Susana G. Rossi, et al.. (2000). Absence of α-Syntrophin Leads to Structurally Aberrant Neuromuscular Synapses Deficient in Utrophin. The Journal of Cell Biology. 150(6). 1385–1398. 196 indexed citations
15.
Peng, H. Benjamin, et al.. (1999). Acetylcholinesterase Clustering at the Neuromuscular Junction Involves Perlecan and Dystroglycan. The Journal of Cell Biology. 145(4). 911–921. 183 indexed citations
16.
Rotundo, Richard L., et al.. (1998). Targetting acetylcholinesterase molecules to the neuromuscular synapse. Journal of Physiology-Paris. 92(3-4). 195–198. 3 indexed citations
17.
Rossi, Susana G. & Richard L. Rotundo. (1996). Transient Interactions between Collagen-tailed Acetylcholinesterase and Sulfated Proteoglycans Prior to Immobilization on the Extracellular Matrix. Journal of Biological Chemistry. 271(4). 1979–1987. 37 indexed citations
18.
Jasmin, Bernard J., Richard K. Lee, & Richard L. Rotundo. (1993). Compartmentalization of acetylcholinesterase mRNA and enzyme at the vertebrate neuromuscular junction. Neuron. 11(3). 467–477. 90 indexed citations
19.
Rossi, Susana G. & Richard L. Rotundo. (1993). Localization of “non-extractable” acetylcholinesterase to the vertebrate neuromuscular junction.. Journal of Biological Chemistry. 268(25). 19152–19159. 33 indexed citations
20.
Rotundo, Richard L., Ana M. Gómez, Cristina Fernández‐Valle, & William R. Randall. (1988). Allelic variants of acetylcholinesterase: genetic evidence that all acetylcholinesterase forms in avian nerves and muscles are encoded by a single gene.. Proceedings of the National Academy of Sciences. 85(20). 7805–7809. 39 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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