Shelley Camp

3.1k total citations
40 papers, 2.6k citations indexed

About

Shelley Camp is a scholar working on Pharmacology, Computational Theory and Mathematics and Molecular Biology. According to data from OpenAlex, Shelley Camp has authored 40 papers receiving a total of 2.6k indexed citations (citations by other indexed papers that have themselves been cited), including 36 papers in Pharmacology, 26 papers in Computational Theory and Mathematics and 21 papers in Molecular Biology. Recurrent topics in Shelley Camp's work include Cholinesterase and Neurodegenerative Diseases (35 papers), Computational Drug Discovery Methods (26 papers) and Nicotinic Acetylcholine Receptors Study (8 papers). Shelley Camp is often cited by papers focused on Cholinesterase and Neurodegenerative Diseases (35 papers), Computational Drug Discovery Methods (26 papers) and Nicotinic Acetylcholine Receptors Study (8 papers). Shelley Camp collaborates with scholars based in United States, France and Italy. Shelley Camp's co-authors include Palmer Taylor, Zoran Radić, Daniel C. Vellom, Natilie A. Pickering, Tara L. Rachinsky, Yves Maulet, Michael Newton, K MacPhee-Quigley, Mark Schumacher and Susan S. Taylor and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Shelley Camp

40 papers receiving 2.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Shelley Camp United States 24 2.0k 1.2k 1.2k 590 385 40 2.6k
S. Bon France 15 1.6k 0.8× 811 0.7× 804 0.7× 499 0.8× 260 0.7× 17 1.9k
Tony Giordano United States 30 913 0.5× 1.3k 1.1× 472 0.4× 123 0.2× 465 1.2× 45 3.2k
Cecilio J. Vidal Spain 20 794 0.4× 678 0.6× 443 0.4× 278 0.5× 119 0.3× 95 1.3k
Kazuma Murakami Japan 31 808 0.4× 1.5k 1.2× 397 0.3× 171 0.3× 110 0.3× 80 3.0k
Fiona Fraser United Kingdom 16 661 0.3× 1.4k 1.1× 459 0.4× 161 0.3× 73 0.2× 23 3.5k
Donald B. Carter United States 20 488 0.2× 969 0.8× 344 0.3× 89 0.2× 232 0.6× 44 2.3k
Surendra S. Ambegaokar United States 14 631 0.3× 1.0k 0.8× 224 0.2× 157 0.3× 105 0.3× 18 3.0k
María‐Salud García‐Ayllón Spain 21 506 0.3× 472 0.4× 238 0.2× 96 0.2× 85 0.2× 48 1.4k
Wenming Li China 24 389 0.2× 788 0.6× 167 0.1× 77 0.1× 99 0.3× 54 1.8k
Thota Ganesh United States 31 486 0.2× 1.1k 0.9× 53 0.0× 171 0.3× 450 1.2× 77 2.7k

Countries citing papers authored by Shelley Camp

Since Specialization
Citations

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

Fields of papers citing papers by Shelley Camp

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Shelley Camp

This figure shows the co-authorship network connecting the top 25 collaborators of Shelley Camp. A scholar is included among the top collaborators of Shelley Camp 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 Shelley Camp. Shelley Camp 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.
Jaco, Antonella De, Davide Comoletti, Noga Dubi, Shelley Camp, & Palmer Taylor. (2012). Processing of Cholinesterase-like α/β-Hydrolase Fold Proteins: Alterations Associated with Congenital Disorders. Protein and Peptide Letters. 19(2). 173–179. 9 indexed citations
2.
Taylor, Palmer, Antonella De Jaco, Davide Comoletti, Meghan T. Miller, & Shelley Camp. (2012). Cholinesterase confabs and cousins: Approaching forty years. Chemico-Biological Interactions. 203(1). 10–13. 5 indexed citations
3.
Jaco, Antonella De, Michael Z. Lin, Noga Dubi, et al.. (2010). Neuroligin Trafficking Deficiencies Arising from Mutations in the α/β-Hydrolase Fold Protein Family. Journal of Biological Chemistry. 285(37). 28674–28682. 34 indexed citations
4.
Camp, Shelley, Limin Zhang, Éric Krejci, et al.. (2010). Contributions of selective knockout studies to understanding cholinesterase disposition and function. Chemico-Biological Interactions. 187(1-3). 72–77. 15 indexed citations
5.
Dobbertin, Alexandre, Anna Hrabovská, Shelley Camp, et al.. (2009). Targeting of Acetylcholinesterase in NeuronsIn Vivo: A Dual Processing Function for the Proline-Rich Membrane Anchor Subunit and the Attachment Domain on the Catalytic Subunit. Journal of Neuroscience. 29(14). 4519–4530. 56 indexed citations
6.
Camp, Shelley, et al.. (2008). Acetylcholinesterase Expression in Muscle Is Specifically Controlled by a Promoter-Selective Enhancesome in the First Intron. Journal of Neuroscience. 28(10). 2459–2470. 23 indexed citations
7.
Boudinot, Éliane, Véronique Bernard, Shelley Camp, et al.. (2008). Influence of differential expression of acetylcholinesterase in brain and muscle on respiration. Respiratory Physiology & Neurobiology. 165(1). 40–48. 11 indexed citations
8.
Luo, Z. David, Yibin Wang, Guy Werlen, et al.. (1999). Calcineurin Enhances Acetylcholinesterase mRNA Stability during C2-C12 Muscle Cell Differentiation. Molecular Pharmacology. 56(5). 886–894. 3 indexed citations
9.
Luo, Z. David, Shelley Camp, Annick Mutero, & Palmer Taylor. (1998). Splicing of 5′ Introns Dictates Alternative Splice Selection of Acetylcholinesterase Pre-mRNA and Specific Expression during Myogenesis. Journal of Biological Chemistry. 273(43). 28486–28495. 20 indexed citations
10.
Marchot, P., Joan R. Kanter, Shelley Camp, et al.. (1997). Expression and Activity of Mutants of Fasciculin, a Peptidic Acetylcholinesterase Inhibitor from Mamba Venom. Journal of Biological Chemistry. 272(6). 3502–3510. 34 indexed citations
11.
Marchot, P., Raimond B. G. Ravelli, Mia L. Raves, et al.. (1996). Soluble monomeric acetylcholinesterase from mouse: Expression, purification, and crystallization in complex with fasciculin. Protein Science. 5(4). 672–679. 50 indexed citations
12.
Barrow, A., et al.. (1995). Kinetics and disposition of picumeterol in animals. Xenobiotica. 25(9). 993–1007. 1 indexed citations
13.
Taylor, Palmer, Zoran Radić, Natilie Hosea, et al.. (1995). Structural bases for the specificity of cholinesterase catalysis and inhibition. Toxicology Letters. 82-83. 453–458. 83 indexed citations
14.
Radić, Zoran, Daniel M. Quinn, Daniel C. Vellom, Shelley Camp, & Palmer Taylor. (1995). Allosteric control of acetylcholinesterase catalysis by fasciculin.. Journal of Biological Chemistry. 270(52). 31414–31414. 2 indexed citations
15.
Taylor, Palmer, Ying Li, Shelley Camp, et al.. (1993). Structure and regulation of expression of the acetylcholinesterase gene. Chemico-Biological Interactions. 87(1-3). 199–207. 13 indexed citations
16.
Radić, Zoran, Natilie A. Pickering, Daniel C. Vellom, Shelley Camp, & Palmer Taylor. (1993). Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors. Biochemistry. 32(45). 12074–12084. 382 indexed citations
17.
Hutchinson, David, Andrew G. Engel, Timothy J. Walls, et al.. (1993). The Spectrum of Congenital End‐plate Acetylcholinesterase Deficiencya. Annals of the New York Academy of Sciences. 681(1). 469–486. 15 indexed citations
18.
Hutchinson, David, Timothy J. Walls, Satoshi Nakano, et al.. (1993). Congential Endplate acetylocholinesterase deficiency. Brain. 116(3). 633–653. 99 indexed citations
19.
Schumacher, Mark, Shelley Camp, Yves Maulet, et al.. (1986). Primary structure of acetylcholinesterase: implications for regulation and function.. PubMed. 45(13). 2976–81. 15 indexed citations
20.
Camp, Shelley, et al.. (1982). Characterization of a hydrophobic, dimeric form of acetylcholinesterase from Torpedo.. Journal of Biological Chemistry. 257(20). 12302–12309. 60 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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