Thomas Kukar

6.0k total citations
42 papers, 1.9k citations indexed

About

Thomas Kukar is a scholar working on Physiology, Molecular Biology and Neurology. According to data from OpenAlex, Thomas Kukar has authored 42 papers receiving a total of 1.9k indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Physiology, 18 papers in Molecular Biology and 16 papers in Neurology. Recurrent topics in Thomas Kukar's work include Alzheimer's disease research and treatments (18 papers), Amyotrophic Lateral Sclerosis Research (15 papers) and Cholinesterase and Neurodegenerative Diseases (11 papers). Thomas Kukar is often cited by papers focused on Alzheimer's disease research and treatments (18 papers), Amyotrophic Lateral Sclerosis Research (15 papers) and Cholinesterase and Neurodegenerative Diseases (11 papers). Thomas Kukar collaborates with scholars based in United States, Germany and China. Thomas Kukar's co-authors include Todd E. Golde, Qiudong Deng, Christopher J. Holler, Georgia Taylor, Thomas B. Ladd, Edward H. Koo, Paola Merino, Pritam Das, Wei Lian and Dennis W. Dickson and has published in prestigious journals such as Journal of Biological Chemistry, Nature Medicine and The Journal of Experimental Medicine.

In The Last Decade

Thomas Kukar

40 papers receiving 1.8k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Thomas Kukar United States 25 890 873 461 259 255 42 1.9k
Nathalie Brouwers Belgium 26 1.6k 1.7× 1.2k 1.4× 668 1.4× 255 1.0× 421 1.7× 46 2.6k
Rachel M. Bailey United States 18 575 0.6× 1.0k 1.2× 663 1.4× 149 0.6× 207 0.8× 29 1.9k
Xiaopin Ma United States 14 697 0.8× 1.4k 1.6× 355 0.8× 155 0.6× 237 0.9× 18 2.2k
Karen Jansen United States 15 703 0.8× 884 1.0× 147 0.3× 193 0.7× 165 0.6× 19 1.7k
Misaki Sekiguchi Japan 11 964 1.1× 531 0.6× 143 0.3× 262 1.0× 206 0.8× 19 1.4k
Ritchie Williamson United Kingdom 25 946 1.1× 1.1k 1.3× 155 0.3× 235 0.9× 204 0.8× 39 2.3k
Hayk Davtyan United States 26 1.3k 1.4× 708 0.8× 205 0.4× 258 1.0× 1.1k 4.1× 55 2.4k
Kazuchika Nishitsuji Japan 22 770 0.9× 795 0.9× 108 0.2× 166 0.6× 229 0.9× 60 1.6k
Mary Lou Previti United States 18 930 1.0× 409 0.5× 257 0.6× 118 0.5× 591 2.3× 27 1.5k
Maciej Łałowski Finland 25 792 0.9× 1.2k 1.4× 122 0.3× 105 0.4× 131 0.5× 68 2.0k

Countries citing papers authored by Thomas Kukar

Since Specialization
Citations

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

Fields of papers citing papers by Thomas Kukar

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Thomas Kukar

This figure shows the co-authorship network connecting the top 25 collaborators of Thomas Kukar. A scholar is included among the top collaborators of Thomas Kukar 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 Thomas Kukar. Thomas Kukar 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.
Tadepalli, Anjaneyulu S., Nicholas T. Seyfried, Thomas Kukar, et al.. (2025). Reduction of sphingomyelinase activity associated with progranulin deficiency and frontotemporal dementia. Neurobiology of Disease. 213. 107024–107024.
2.
Johnson, Michelle A., Paola Merino, Pritha Bagchi, et al.. (2022). Proximity-based labeling reveals DNA damage–induced phosphorylation of fused in sarcoma (FUS) causes distinct changes in the FUS protein interactome. Journal of Biological Chemistry. 298(8). 102135–102135. 3 indexed citations
3.
Root, Jessica, et al.. (2021). Lysosome dysfunction as a cause of neurodegenerative diseases: Lessons from frontotemporal dementia and amyotrophic lateral sclerosis. Neurobiology of Disease. 154. 105360–105360. 132 indexed citations
4.
Holler, Christopher J., Georgia Taylor, Qiudong Deng, & Thomas Kukar. (2017). Intracellular Proteolysis of Progranulin Generates Stable, Lysosomal Granulins that Are Haploinsufficient in Patients with Frontotemporal Dementia Caused byGRNMutations. eNeuro. 4(4). ENEURO.0100–17.2017. 99 indexed citations
5.
Deng, Qiudong, Christopher J. Holler, Geraldine Taylor, et al.. (2014). FUS is Phosphorylated by DNA-PK and Accumulates in the Cytoplasm after DNA Damage. Journal of Neuroscience. 34(23). 7802–7813. 126 indexed citations
6.
Chen, Xi, Jianjun Chang, Qiudong Deng, et al.. (2013). Progranulin Does Not Bind Tumor Necrosis Factor (TNF) Receptors and Is Not a Direct Regulator of TNF-Dependent Signaling or Bioactivity in Immune or Neuronal Cells. Journal of Neuroscience. 33(21). 9202–9213. 74 indexed citations
7.
Das, Pritam, Christophe Verbeeck, Lisa M. Minter, et al.. (2012). Transient pharmacologic lowering of Aβ production prior to deposition results in sustained reduction of amyloid plaque pathology. Molecular Neurodegeneration. 7(1). 39–39. 25 indexed citations
8.
Verbeeck, Christophe, Qiudong Deng, Mariely DeJesus‐Hernandez, et al.. (2012). Expression of Fused in sarcoma mutations in mice recapitulates the neuropathology of FUS proteinopathies and provides insight into disease pathogenesis. Molecular Neurodegeneration. 7(1). 53–53. 52 indexed citations
9.
Sagi, Sarah A., Christian Lessard, Kellen D. Winden, et al.. (2011). Substrate Sequence Influences γ-Secretase Modulator Activity, Role of the Transmembrane Domain of the Amyloid Precursor Protein. Journal of Biological Chemistry. 286(46). 39794–39803. 30 indexed citations
10.
Kukar, Thomas, Thomas B. Ladd, Paul Robertson, et al.. (2011). Lysine 624 of the Amyloid Precursor Protein (APP) Is a Critical Determinant of Amyloid β Peptide Length. Journal of Biological Chemistry. 286(46). 39804–39812. 58 indexed citations
11.
Czirr, Eva, Barbara A. Cottrell, Stefanie Leuchtenberger, et al.. (2008). Independent Generation of Aβ42 and Aβ38 Peptide Species by γ-Secretase. Journal of Biological Chemistry. 283(25). 17049–17054. 64 indexed citations
12.
Kukar, Thomas & Todd E. Golde. (2008). Possible Mechanisms of Action of NSAIDs and Related Compounds that Modulate γ - Secretase Cleavage. Current Topics in Medicinal Chemistry. 8(1). 47–53. 36 indexed citations
13.
Kukar, Thomas, Jason L. Eriksen, V. Holloway, et al.. (2007). Chronic administration of R-flurbiprofen attenuates learning impairments in transgenic amyloid precursor protein mice. BMC Neuroscience. 8(1). 54–54. 102 indexed citations
14.
Leuchtenberger, Stefanie, Markus P. Kummer, Thomas Kukar, et al.. (2005). Inhibitors of Rho‐kinase modulate amyloid‐β (Aβ) secretion but lack selectivity for Aβ42. Journal of Neurochemistry. 96(2). 355–365. 26 indexed citations
15.
Kukar, Thomas, M. Paul Murphy, Jason L. Eriksen, et al.. (2005). Diverse compounds mimic Alzheimer disease–causing mutations by augmenting Aβ42 production. Nature Medicine. 11(5). 545–550. 228 indexed citations
16.
Lian, Wei, Thomas Kukar, L. Govindasamy, et al.. (2004). Crystallization and preliminary X-ray crystallographic studies on recombinant rat choline acetyltransferase. Acta Crystallographica Section D Biological Crystallography. 60(2). 374–375. 3 indexed citations
17.
Govindasamy, L., Wei Lian, Thomas Kukar, et al.. (2004). Structural insights and functional implications of choline acetyltransferase. Journal of Structural Biology. 148(2). 226–235. 28 indexed citations
18.
Wu, Donghai, L. Govindasamy, Wei Lian, et al.. (2003). Structure of Human Carnitine Acetyltransferase. Journal of Biological Chemistry. 278(15). 13159–13165. 66 indexed citations
19.
Kukar, Thomas, et al.. (2002). Protein Microarrays to Detect Protein–Protein Interactions Using Red and Green Fluorescent Proteins. Analytical Biochemistry. 306(1). 50–54. 64 indexed citations
20.
Lian, Wei, et al.. (2002). Crystallization and preliminary X-ray crystallographic studies on recombinant human carnitine acetyltransferase. Acta Crystallographica Section D Biological Crystallography. 58(7). 1193–1194. 8 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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