Terrone L. Rosenberry

11.0k total citations · 1 hit paper
149 papers, 8.9k citations indexed

About

Terrone L. Rosenberry is a scholar working on Pharmacology, Molecular Biology and Computational Theory and Mathematics. According to data from OpenAlex, Terrone L. Rosenberry has authored 149 papers receiving a total of 8.9k indexed citations (citations by other indexed papers that have themselves been cited), including 84 papers in Pharmacology, 82 papers in Molecular Biology and 48 papers in Computational Theory and Mathematics. Recurrent topics in Terrone L. Rosenberry's work include Cholinesterase and Neurodegenerative Diseases (84 papers), Computational Drug Discovery Methods (48 papers) and Enzyme function and inhibition (33 papers). Terrone L. Rosenberry is often cited by papers focused on Cholinesterase and Neurodegenerative Diseases (84 papers), Computational Drug Discovery Methods (48 papers) and Enzyme function and inhibition (33 papers). Terrone L. Rosenberry collaborates with scholars based in United States, Japan and Canada. Terrone L. Rosenberry's co-authors include William L. Roberts, William D. Mallender, Israel Silman, Joel L. Sussman, Michal Harel, William L. Roberts, Hay Dvir, T. Szegletes, M. Edward Medof and Dana Kim Reed and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Terrone L. Rosenberry

146 papers receiving 8.6k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Acetylcholinesterase: From 3D structure to function

2010 606 citations Terrone L. Rosenberry et al. Chemico-Biological Interactions profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Terrone L. Rosenberry United States	52	4.3k	4.1k	2.5k	2.1k	1.4k	149	8.9k
Yuan‐Ping Pang United States	50	3.0k 0.7×	3.5k 0.9×	1.9k 0.7×	765 0.4×	979 0.7×	187	7.8k
Jordan Tang United States	53	1.7k 0.4×	4.8k 1.2×	1.8k 0.7×	2.9k 1.4×	458 0.3×	173	9.1k
María Laura Bolognesi Italy	50	4.4k 1.0×	3.1k 0.8×	3.2k 1.3×	2.1k 1.0×	273 0.2×	200	9.2k
Yves Bourne France	48	1.5k 0.4×	5.4k 1.3×	993 0.4×	332 0.2×	943 0.7×	115	8.0k
Dieter Steinhilber Germany	49	2.2k 0.5×	3.9k 0.9×	462 0.2×	1.3k 0.6×	447 0.3×	296	9.6k
Roberto Cappai Australia	69	1.9k 0.4×	6.9k 1.7×	1.2k 0.5×	9.1k 4.4×	556 0.4×	235	15.9k
Wolfgang Sippl Germany	57	830 0.2×	6.4k 1.6×	1.3k 0.5×	419 0.2×	584 0.4×	303	10.3k
Hironobu Naiki Japan	61	1.2k 0.3×	8.2k 2.0×	933 0.4×	8.1k 3.9×	343 0.2×	217	13.8k
Haopeng Sun China	42	1.9k 0.4×	3.1k 0.8×	1.3k 0.5×	529 0.3×	365 0.3×	268	6.8k
Hai‐Bin Luo China	38	1.2k 0.3×	3.4k 0.8×	752 0.3×	758 0.4×	875 0.6×	217	6.9k

Countries citing papers authored by Terrone L. Rosenberry

Since Specialization

Citations

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

Fields of papers citing papers by Terrone L. Rosenberry

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Terrone L. Rosenberry

This figure shows the co-authorship network connecting the top 25 collaborators of Terrone L. Rosenberry. A scholar is included among the top collaborators of Terrone L. Rosenberry 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 Terrone L. Rosenberry. Terrone L. Rosenberry is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Prasad, Ramesh, Yuan Gao, Jens O. Watzlawik, et al.. (2023). A common pathway for detergent-assisted oligomerization of Aβ42. Communications Biology. 6(1). 1184–1184. 5 indexed citations

Suire, Caitlin N., Samer O. Abdul‐Hay, Dongcheul Kang, et al.. (2020). Cathepsin D regulates cerebral Aβ42/40 ratios via differential degradation of Aβ42 and Aβ40. Alzheimer s Research & Therapy. 12(1). 80–80. 50 indexed citations

Rosenberry, Terrone L. & Jonah Cheung. (2019). Rate-limiting step in the decarbamoylation of acetylcholinesterases with large carbamoyl groups. Chemico-Biological Interactions. 308. 392–395. 1 indexed citations

Venkatasubban, Kunisi S., et al.. (2018). Decarbamoylation of acetylcholinesterases is markedly slowed as carbamoyl groups increase in size. Archives of Biochemistry and Biophysics. 655. 67–74. 12 indexed citations

Zimmerman, Maxwell I., et al.. (2015). Antiparallel β-Sheet Structure within the C-Terminal Region of 42-Residue Alzheimer's Amyloid-β Peptides When They Form 150-kDa Oligomers. Journal of Molecular Biology. 427(13). 2319–2328. 61 indexed citations

Maharvi, Ghulam M., et al.. (2012). Hydrolysis of low concentrations of the acetylthiocholine analogs acetyl(homo)thiocholine and acetyl(nor)thiocholine by acetylcholinesterase may be limited by selective gating at the enzyme peripheral site. Chemico-Biological Interactions. 203(1). 38–43. 8 indexed citations

Tay, William M., et al.. (2012). A Mass Spectrometric Approach for Characterization of Amyloid-β Aggregates and Identification of Their Post-Translational Modifications. Biochemistry. 51(18). 3759–3766. 10 indexed citations

Wildman, Scott A., et al.. (2011). Drug‐like Leads for Steric Discrimination between Substrate and Inhibitors of Human Acetylcholinesterase. Chemical Biology & Drug Design. 78(4). 495–504. 22 indexed citations

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

10.

Berger, Zdenek, Hanno M. Roder, Amanda Hanna, et al.. (2007). Accumulation of Pathological Tau Species and Memory Loss in a Conditional Model of Tauopathy. Journal of Neuroscience. 27(14). 3650–3662. 387 indexed citations

11.

Levites, Yona, Lisa Smithson, Robert Price, et al.. (2006). Insights into the mechanisms of action of anti‐Aβ antibodies in Alzheimer's disease mouse models. The FASEB Journal. 20(14). 2576–2578. 93 indexed citations

12.

Nichols, Michael R., et al.. (2004). Amyloid-β Protofibrils Differ from Amyloid-β Aggregates Induced in Dilute Hexafluoroisopropanol in Stability and Morphology. Journal of Biological Chemistry. 280(4). 2471–2480. 100 indexed citations

13.

Dunlap, Mark E., Steve Bibevski, Terrone L. Rosenberry, & Paul Ernsberger. (2003). Mechanisms of altered vagal control in heart failure: influence of muscarinic receptors and acetylcholinesterase activity. American Journal of Physiology-Heart and Circulatory Physiology. 285(4). H1632–H1640. 51 indexed citations

14.

Rosenberry, Terrone L.. (1996). A fat lot of good. Trends in Cell Biology. 6(11). 445–446. 1 indexed citations

15.

Wongkajornsilp, Adisak & Terrone L. Rosenberry. (1995). Uptake of Exogenous sn-1-Acyl-2- lyso-phosphatidylinositol into HeLa S3 Cells. Journal of Biological Chemistry. 270(16). 9147–9153. 11 indexed citations

16.

Güther, Maria Lucia S., et al.. (1994). The Detection of Phospholipase-Resistant and -Sensitive Glycosyl-phosphatidylinositol Membrane Anchors by Western Blotting. Analytical Biochemistry. 219(2). 249–255. 27 indexed citations

17.

Breton, Catherine Braun, et al.. (1990). Glycolipid anchorage of plasmodium falciparum surface antigens. Research in Immunology. 141(7). 743–755. 31 indexed citations

18.

Rosenberry, Terrone L., et al.. (1982). [13] Acetylcholinesterase. Methods in enzymology on CD-ROM/Methods in enzymology. 82 Pt A. 325–339. 27 indexed citations

19.

Rosenberry, Terrone L., et al.. (1977). Catalysis by acetylcholinesterase. Acceleration of the hydrolysis of neutral acetic acid esters by certain aromatic cations.. Journal of Biological Chemistry. 252(20). 7200–7206. 27 indexed citations

20.

Rosenberry, Terrone L. & Sidney A. Bernhard. (1971). Catalysis by acetylcholinesterase. I. Fluorescent titration with a carbamoylating agent. Biochemistry. 10(22). 4114–4120. 82 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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