Jeff Kuret

13.5k total citations
104 papers, 6.4k citations indexed

About

Jeff Kuret is a scholar working on Molecular Biology, Physiology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Jeff Kuret has authored 104 papers receiving a total of 6.4k indexed citations (citations by other indexed papers that have themselves been cited), including 65 papers in Molecular Biology, 65 papers in Physiology and 17 papers in Cellular and Molecular Neuroscience. Recurrent topics in Jeff Kuret's work include Alzheimer's disease research and treatments (64 papers), Prion Diseases and Protein Misfolding (18 papers) and Neuroscience and Neuropharmacology Research (15 papers). Jeff Kuret is often cited by papers focused on Alzheimer's disease research and treatments (64 papers), Prion Diseases and Protein Misfolding (18 papers) and Neuroscience and Neuropharmacology Research (15 papers). Jeff Kuret collaborates with scholars based in United States, United Kingdom and Canada. Jeff Kuret's co-authors include Mihaela Necula, Lester I. Binder, Carmen N. Chirita, Haishan Yin, Gilles Carmel, Howard Schulman, Erin E. Congdon, T. Chris Gamblin, Michelle E. King and Anthony J. DeMaggio and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Jeff Kuret

102 papers receiving 6.3k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Jeff Kuret United States	50	3.7k	3.7k	1.3k	1.1k	888	104	6.4k
Saskia Milton United States	21	4.3k 1.2×	5.5k 1.5×	1.0k 0.8×	623 0.6×	968 1.1×	34	7.5k
Lars O. Tjernberg Sweden	34	3.5k 0.9×	4.3k 1.2×	722 0.6×	643 0.6×	1.0k 1.2×	107	6.3k
Paolo Paganetti Switzerland	37	4.1k 1.1×	3.1k 0.8×	2.1k 1.6×	1.3k 1.2×	761 0.9×	90	7.1k
Kurt R. Brunden United States	44	3.3k 0.9×	4.3k 1.2×	1.8k 1.4×	932 0.8×	1.2k 1.3×	115	8.7k
Nikolaos K. Robakis United States	51	4.1k 1.1×	4.3k 1.2×	1.6k 1.3×	1.1k 1.0×	1.1k 1.3×	133	7.3k
Jan Näslund Sweden	30	3.4k 0.9×	5.4k 1.5×	1.0k 0.8×	532 0.5×	1.4k 1.5×	51	7.0k
Beth L. Ostaszewski United States	33	4.4k 1.2×	6.6k 1.8×	1.5k 1.2×	1.4k 1.3×	1.9k 2.1×	40	8.8k
H. M. Wiśniewski United States	29	4.3k 1.1×	4.9k 1.3×	1.5k 1.1×	1.1k 1.0×	947 1.1×	78	7.6k
Joseph F. Poduslo United States	51	2.6k 0.7×	2.9k 0.8×	1.7k 1.4×	450 0.4×	427 0.5×	123	6.7k
Malcolm A. Leissring United States	36	2.4k 0.6×	3.1k 0.8×	1.1k 0.9×	827 0.7×	881 1.0×	65	5.0k

Countries citing papers authored by Jeff Kuret

Since Specialization

Citations

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

Fields of papers citing papers by Jeff Kuret

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jeff Kuret

This figure shows the co-authorship network connecting the top 25 collaborators of Jeff Kuret. A scholar is included among the top collaborators of Jeff Kuret 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 Jeff Kuret. Jeff Kuret 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

Kuret, Jeff, et al.. (2024). Quantification of Methylation and Phosphorylation Stoichiometry. Methods in molecular biology. 2754. 221–235.

Headley, Colwyn A., Yongbin Han, Jay L. Zweíer, et al.. (2019). Membrane-specific spin trap, 5-dodecylcarbamoyl-5-N-dodecylacetamide-1-pyroline-N-oxide (diC₁₂PO): theoretical, bioorthogonal fluorescence imaging and EPR studies. Organic & Biomolecular Chemistry. 17(33). 7694–7705. 5 indexed citations

Bundschuh, Ralf, et al.. (2019). The role of annealing and fragmentation in human tau aggregation dynamics. Journal of Biological Chemistry. 294(13). 4728–4737. 18 indexed citations

Cocuron, Jean‐Christophe, et al.. (2018). A liquid chromatography tandem mass spectroscopy approach for quantification of protein methylation stoichiometry. Analytical Biochemistry. 545. 72–77. 3 indexed citations

Kuret, Jeff, et al.. (2016). Detection and Quantification Methods for Fibrillar Products of In Vitro Tau Aggregation Assays. Methods in molecular biology. 1523. 101–111. 9 indexed citations

Jensen, Jordan, Katryna Cisek, Nicolette S. Honson, & Jeff Kuret. (2011). Ligand polarizability contributes to tau fibril binding affinity. Bioorganic & Medicinal Chemistry. 19(17). 5147–5154. 15 indexed citations

Murale, Dhiraj P., et al.. (2011). Structure–activity relationship of cyclic thiacarbocyanine tau aggregation inhibitors. Bioorganic & Medicinal Chemistry Letters. 21(11). 3273–3276. 7 indexed citations

Jensen, Jordan, et al.. (2010). Imaging as a Strategy for Premortem Diagnosis and Staging of Tauopathies. Current Alzheimer Research. 7(3). 230–234. 10 indexed citations

Duff, Karen, Jeff Kuret, & Erin E. Congdon. (2010). Disaggregation of Tau as a Therapeutic Approach to Tauopathies. Current Alzheimer Research. 7(3). 235–240. 15 indexed citations

10.

Chang, Edward S., Sohee Kim, Haishan Yin, Haikady N. Nagaraja, & Jeff Kuret. (2008). Pathogenic missense MAPT mutations differentially modulate tau aggregation propensity at nucleation and extension steps. Journal of Neurochemistry. 107(4). 1113–1123. 45 indexed citations

11.

Honson, Nicolette S., Ronald L. Johnson, Wenwei Huang, et al.. (2007). Differentiating Alzheimer disease-associated aggregates with small molecules. Neurobiology of Disease. 28(3). 251–260. 69 indexed citations

12.

Necula, Mihaela & Jeff Kuret. (2005). Site‐specific pseudophosphorylation modulates the rate of tau filament dissociation. FEBS Letters. 579(6). 1453–1457. 32 indexed citations

13.

Mashhoon, Neda, Gilles Carmel, J. W. Pflugrath, & Jeff Kuret. (2001). Structure of the Unliganded cAMP-Dependent Protein Kinase Catalytic Subunit from Saccharomyces cerevisiae. Archives of Biochemistry and Biophysics. 387(1). 11–19. 12 indexed citations

14.

Schwab, Claudia, Anthony J. DeMaggio, Nupur Ghoshal, et al.. (2000). Casein kinase 1 delta is associated with pathological accumulation of tau in several neurodegenerative diseases. Neurobiology of Aging. 21(4). 503–510. 130 indexed citations

15.

Mashhoon, Neda, Anthony J. DeMaggio, Valentina Tereshko, et al.. (2000). Crystal Structure of a Conformation-selective Casein Kinase-1 Inhibitor. Journal of Biological Chemistry. 275(26). 20052–20060. 126 indexed citations

16.

Kuret, Jeff, et al.. (1997). Casein Kinase 1 Is Tightly Associated with Paired‐Helical Filaments Isolated from Alzheimer's Disease Brain. Journal of Neurochemistry. 69(6). 2506–2515. 77 indexed citations

17.

Wang, Xiangmin, Merl F. Hoekstra, Anthony J. DeMaggio, et al.. (1996). Prenylated Isoforms of Yeast Casein Kinase I, Including the Novel Yck3p, Suppress the gcs1 Blockage of Cell Proliferation from Stationary Phase. Molecular and Cellular Biology. 16(10). 5375–5385. 81 indexed citations

18.

Ebert, Matthias P., et al.. (1994). Molecular Cloning and Sequence Analysis of Two Novel Fission Yeast Casein Kinase-1 Isoforms. Biochemical and Biophysical Research Communications. 203(1). 231–236. 24 indexed citations

19.

Hoekstra, Merl F., Namrita Dhillon, Gilles Carmel, et al.. (1994). Budding and fission yeast casein kinase I isoforms have dual-specificity protein kinase activity.. Molecular Biology of the Cell. 5(8). 877–886. 58 indexed citations

20.

Vančura, Aleš, et al.. (1992). Two genes in Saccharomyces cerevisiae encode a membrane-bound form of casein kinase-1.. Molecular Biology of the Cell. 3(3). 275–286. 85 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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