Charles E. Nolan

2.2k total citations
30 papers, 1.1k citations indexed

About

Charles E. Nolan is a scholar working on Physiology, Molecular Biology and Oncology. According to data from OpenAlex, Charles E. Nolan has authored 30 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Physiology, 9 papers in Molecular Biology and 6 papers in Oncology. Recurrent topics in Charles E. Nolan's work include Alzheimer's disease research and treatments (10 papers), Drug Transport and Resistance Mechanisms (6 papers) and Computational Drug Discovery Methods (5 papers). Charles E. Nolan is often cited by papers focused on Alzheimer's disease research and treatments (10 papers), Drug Transport and Resistance Mechanisms (6 papers) and Computational Drug Discovery Methods (5 papers). Charles E. Nolan collaborates with scholars based in United States, United Kingdom and Sweden. Charles E. Nolan's co-authors include Firoze B. Jungalwala, K. H. Chou, James E. Finley, K. Richter, Joel B. Schachter, Lit‐Fui Lau, Robert B. Nelson, Mathieu Herman, Pavan Krishnamurthy and Wen Yi and has published in prestigious journals such as Nature Communications, Journal of Neuroscience and Journal of Medicinal Chemistry.

In The Last Decade

Charles E. Nolan

27 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Charles E. Nolan United States 17 436 419 200 187 143 30 1.1k
Alfredo Giménez-Cassina Spain 21 382 0.9× 979 2.3× 314 1.6× 91 0.5× 61 0.4× 29 1.5k
Tomomi Kiyota United States 21 838 1.9× 518 1.2× 246 1.2× 101 0.5× 174 1.2× 34 1.8k
Lee‐Way Jin United States 21 1.0k 2.4× 690 1.6× 324 1.6× 190 1.0× 61 0.4× 39 1.7k
Mary Lou Previti United States 18 930 2.1× 409 1.0× 236 1.2× 118 0.6× 42 0.3× 27 1.5k
Hervé Paris France 21 271 0.6× 1.0k 2.5× 621 3.1× 94 0.5× 28 0.2× 43 1.5k
James J. Vornov United States 23 254 0.6× 835 2.0× 936 4.7× 78 0.4× 170 1.2× 39 1.8k
Masafumi Fujimoto Japan 25 441 1.0× 996 2.4× 573 2.9× 184 1.0× 45 0.3× 99 1.9k
Diana W. Shineman United States 14 635 1.5× 786 1.9× 322 1.6× 216 1.2× 41 0.3× 27 1.6k
Jingqi Huang Canada 13 736 1.7× 734 1.8× 201 1.0× 160 0.9× 26 0.2× 17 1.4k
Kenneth Banasiak United States 12 209 0.5× 551 1.3× 285 1.4× 56 0.3× 71 0.5× 15 1.1k

Countries citing papers authored by Charles E. Nolan

Since Specialization
Citations

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

Fields of papers citing papers by Charles E. Nolan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Charles E. Nolan. 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 Charles E. Nolan. The network helps show where Charles E. Nolan may publish in the future.

Co-authorship network of co-authors of Charles E. Nolan

This figure shows the co-authorship network connecting the top 25 collaborators of Charles E. Nolan. A scholar is included among the top collaborators of Charles E. Nolan 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 Charles E. Nolan. Charles E. Nolan 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.
Takano, Akihiro, Laigao Chen, Sangram Nag, et al.. (2018). Quantitative Analysis of 18F-PF-06684511, a Novel PET Radioligand for Selective β-Secretase 1 Imaging, in Nonhuman Primate Brain. Journal of Nuclear Medicine. 60(7). 992–997. 6 indexed citations
2.
Zhang, Lei, Laigao Chen, Jason K. Dutra, et al.. (2018). Identification of a Novel Positron Emission Tomography (PET) Ligand for Imaging β-Site Amyloid Precursor Protein Cleaving Enzyme 1 (BACE-1) in Brain. Journal of Medicinal Chemistry. 61(8). 3296–3308. 15 indexed citations
3.
Zuhl, Andrea M., Charles E. Nolan, Michael A. Brodney, et al.. (2016). Chemoproteomic profiling reveals that cathepsin D off-target activity drives ocular toxicity of β-secretase inhibitors. Nature Communications. 7(1). 13042–13042. 59 indexed citations
4.
Hajós, Mihály, Elena Morozova, Chester J. Siok, et al.. (2013). Effects of the γ-secretase inhibitor semagacestat on hippocampal neuronal network oscillation. Frontiers in Pharmacology. 4. 72–72. 10 indexed citations
5.
Lu, Yasong, Hugh A. Barton, Louis Leung, et al.. (2012). Cerebrospinal Fluid β-Amyloid Turnover in the Mouse, Dog, Monkey and Human Evaluated by Systematic Quantitative Analyses. Neurodegenerative Diseases. 12(1). 36–50. 18 indexed citations
6.
7.
Lu, Yasong, David Riddell, Éva Hajós‐Korcsok, et al.. (2012). Cerebrospinal Fluid Amyloid-β (Aβ) as an Effect Biomarker for Brain Aβ Lowering Verified by Quantitative Preclinical Analyses. Journal of Pharmacology and Experimental Therapeutics. 342(2). 366–375. 24 indexed citations
8.
Lu, Yasong, Liming Zhang, Charles E. Nolan, et al.. (2011). Quantitative Pharmacokinetic/Pharmacodynamic Analyses Suggest That the 129/SVE Mouse Is a Suitable Preclinical Pharmacology Model for Identifying Small-Molecule γ-Secretase Inhibitors. Journal of Pharmacology and Experimental Therapeutics. 339(3). 922–934. 19 indexed citations
9.
Lanz, Thomas A., Kathleen M. Wood, K. Richter, et al.. (2010). Pharmacodynamics and Pharmacokinetics of the γ-Secretase Inhibitor PF-3084014. Journal of Pharmacology and Experimental Therapeutics. 334(1). 269–277. 39 indexed citations
10.
Wood, Kathleen M., Thomas A. Lanz, Karen J. Coffman, et al.. (2008). P2‐375: Efficacy of the novel γ‐secretase inhibitor, PF‐3084014, in reducing Aβ in brain, CSF, and plasma in guinea pigs and Tg2576 mice. Alzheimer s & Dementia. 4(4S_Part_14). 11 indexed citations
11.
Planel, Emmanuel, K. Richter, Charles E. Nolan, et al.. (2007). Anesthesia Leads to Tau Hyperphosphorylation through Inhibition of Phosphatase Activity by Hypothermia. Journal of Neuroscience. 27(12). 3090–3097. 312 indexed citations
12.
Nason, Deane M., Steven D. Heck, John Lowe, et al.. (2004). Substituted 6-phenyl-pyridin-2-ylamines: selective and potent inhibitors of neuronal nitric oxide synthase. Bioorganic & Medicinal Chemistry Letters. 14(17). 4511–4514. 14 indexed citations
13.
Lowe, John, Robert A. Volkmann, Steven D. Heck, et al.. (1999). A new class of selective and potent inhibitors of neuronal nitric oxide synthase. Bioorganic & Medicinal Chemistry Letters. 9(17). 2569–2572. 15 indexed citations
14.
Stegall, Mark D., et al.. (1997). MYCOPHENOLATE MOFETIL DECREASES REJECTION IN SIMULTANEOUS PANCREAS-KIDNEY TRANSPLANTATION WHEN COMBINED WITH TACROLIMUS OR CYCLOSPORINE1. Transplantation. 64(12). 1695–1700. 70 indexed citations
15.
16.
Sapirstein, Victor S., et al.. (1992). Identification of Plasmolipin as a Major Constituent of White Matter Clathrin‐Coated Vesicles. Journal of Neurochemistry. 58(4). 1372–1378. 14 indexed citations
17.
Sapirstein, Victor S., et al.. (1992). Expression of plasmolipin in the developing rat brain. Journal of Neuroscience Research. 31(1). 96–102. 10 indexed citations
18.
Sapirstein, Victor S., et al.. (1991). The phylogenic expression of plasmolipin in the vertebrate nervous system. Neurochemical Research. 16(2). 123–128. 10 indexed citations
19.
Bizzozero, Oscar A., et al.. (1990). Presence of the Plasma Membrane Proteolipid (Plasmolipin) in Myelin. Journal of Neurochemistry. 55(2). 602–610. 31 indexed citations
20.
Nolan, Charles E., et al.. (1976). [17] Ancrod, the coagulating enzyme from Malayan pit viper (Agkistrodon rhodostoma) venom. Methods in enzymology on CD-ROM/Methods in enzymology. 45. 205–213. 70 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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