Hilda H. Slunt

9.9k total citations · 4 hit papers
39 papers, 8.0k citations indexed

About

Hilda H. Slunt is a scholar working on Molecular Biology, Physiology and Cellular and Molecular Neuroscience. According to data from OpenAlex, Hilda H. Slunt has authored 39 papers receiving a total of 8.0k indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Molecular Biology, 24 papers in Physiology and 11 papers in Cellular and Molecular Neuroscience. Recurrent topics in Hilda H. Slunt's work include Alzheimer's disease research and treatments (23 papers), Prion Diseases and Protein Misfolding (11 papers) and Genetic Neurodegenerative Diseases (5 papers). Hilda H. Slunt is often cited by papers focused on Alzheimer's disease research and treatments (23 papers), Prion Diseases and Protein Misfolding (11 papers) and Genetic Neurodegenerative Diseases (5 papers). Hilda H. Slunt collaborates with scholars based in United States, Japan and France. Hilda H. Slunt's co-authors include David Borchelt, Sangram S. Sisodia, Donald L. Price, Neal G. Copeland, Nancy A. Jenkins, Gopal Thinakaran, Michael K. Lee, Joanna L. Jankowsky, Tamara Ratovitski and Sam Gandy and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Hilda H. Slunt

39 papers receiving 7.9k citations

Hit Papers

Familial Alzheimer's Disease–Linked Presenilin 1 Variants... 1995 2026 2005 2015 1996 1996 2001 1995 400 800 1.2k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Hilda H. Slunt United States 31 5.5k 3.9k 2.3k 1.5k 1.1k 39 8.0k
Stephen D. Schmidt United States 30 5.6k 1.0× 2.8k 0.7× 1.2k 0.5× 1.3k 0.9× 1.1k 1.0× 38 7.4k
Lisa McConlogue United States 31 6.0k 1.1× 3.6k 0.9× 2.2k 1.0× 1.7k 1.1× 803 0.7× 41 8.2k
Nikolaos K. Robakis United States 51 4.3k 0.8× 4.1k 1.0× 1.6k 0.7× 1.1k 0.7× 1.1k 0.9× 133 7.3k
Steven L. Wagner United States 37 4.4k 0.8× 3.7k 0.9× 1.9k 0.8× 879 0.6× 689 0.6× 78 8.4k
Albert Y. Hung United States 24 4.7k 0.9× 3.6k 0.9× 1.4k 0.6× 1.3k 0.9× 1.0k 0.9× 35 6.8k
Chris Eckman United States 11 6.7k 1.2× 3.0k 0.8× 2.2k 1.0× 1.8k 1.2× 432 0.4× 13 8.0k
Christopher Janus United States 30 4.3k 0.8× 2.4k 0.6× 2.4k 1.0× 1.1k 0.7× 551 0.5× 53 6.9k
Wilma Wasco United States 32 4.2k 0.8× 3.3k 0.8× 1.5k 0.7× 1.1k 0.7× 892 0.8× 59 6.0k
Gopal Thinakaran United States 57 8.9k 1.6× 6.0k 1.5× 2.5k 1.1× 2.2k 1.4× 3.0k 2.6× 121 12.1k
Anne M. Cataldo United States 45 5.2k 0.9× 3.8k 1.0× 1.7k 0.7× 852 0.6× 2.8k 2.5× 66 9.3k

Countries citing papers authored by Hilda H. Slunt

Since Specialization
Citations

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

Fields of papers citing papers by Hilda H. Slunt

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Hilda H. Slunt. 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 Hilda H. Slunt. The network helps show where Hilda H. Slunt may publish in the future.

Co-authorship network of co-authors of Hilda H. Slunt

This figure shows the co-authorship network connecting the top 25 collaborators of Hilda H. Slunt. A scholar is included among the top collaborators of Hilda H. Slunt 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 Hilda H. Slunt. Hilda H. Slunt 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.
Gary, Devin S., et al.. (2007). Investigation of RNA interference to suppress expression of full-length and fragment human huntingtin. NeuroMolecular Medicine. 9(2). 145–155. 3 indexed citations
2.
Jankowsky, Joanna L., Hilda H. Slunt, Victoria Gonzales, et al.. (2005). Persistent Amyloidosis following Suppression of Aβ Production in a Transgenic Model of Alzheimer Disease. PLoS Medicine. 2(12). e355–e355. 177 indexed citations
3.
Wang, Jiou, Guilian Xu, Hilda H. Slunt, et al.. (2005). Coincident thresholds of mutant protein for paralytic disease and protein aggregation caused by restrictively expressed superoxide dismutase cDNA. Neurobiology of Disease. 20(3). 943–952. 91 indexed citations
4.
Jankowsky, Joanna L., Hilda H. Slunt, Victoria Gonzales, et al.. (2004). APP processing and amyloid deposition in mice haplo-insufficient for presenilin 1. Neurobiology of Aging. 25(7). 885–892. 136 indexed citations
5.
Schilling, Gabriele, Alena Savonenko, Alexandra M. Klevytska, et al.. (2004). Nuclear-targeting of mutant huntingtin fragments produces Huntington's disease-like phenotypes in transgenic mice. Human Molecular Genetics. 13(15). 1599–1610. 78 indexed citations
6.
Kratz, John, Duncan Stearns, David L. Huso, et al.. (2002). Expression of stabilized β-catenin in differentiated neurons of transgenic mice does not result in tumor formation. BMC Cancer. 2(1). 33–33. 19 indexed citations
7.
Borchelt, David, Michael K. Lee, Victoria Gonzales, et al.. (2002). Accumulation of proteolytic fragments of mutant presenilin 1 and accelerated amyloid deposition are co-regulated in transgenic mice. Neurobiology of Aging. 23(2). 171–177. 16 indexed citations
8.
Jankowsky, Joanna L., Hilda H. Slunt, Tamara Ratovitski, et al.. (2001). Co-expression of multiple transgenes in mouse CNS: a comparison of strategies. Biomolecular Engineering. 17(6). 157–165. 680 indexed citations breakdown →
9.
Schilling, Gabriele, Jonathan Wood, Kui Duan, et al.. (1999). Nuclear Accumulation of Truncated Atrophin-1 Fragments in a Transgenic Mouse Model of DRPLA. Neuron. 24(1). 275–286. 143 indexed citations
10.
Buxbaum, Joseph D., Gopal Thinakaran, Vassilis E. Koliatsos, et al.. (1998). Alzheimer Amyloid Protein Precursor in the Rat Hippocampus: Transport and Processing through the Perforant Path. Journal of Neuroscience. 18(23). 9629–9637. 212 indexed citations
11.
Thinakaran, Gopal, Tamara Ratovitski, Hilda H. Slunt, et al.. (1997). Evidence That Levels of Presenilins (PS1 and PS2) Are Coordinately Regulated by Competition for Limiting Cellular Factors. Journal of Biological Chemistry. 272(45). 28415–28422. 275 indexed citations
12.
Ratovitski, Tamara, Hilda H. Slunt, Gopal Thinakaran, et al.. (1997). Endoproteolytic Processing and Stabilization of Wild-type and Mutant Presenilin. Journal of Biological Chemistry. 272(39). 24536–24541. 177 indexed citations
13.
Sisodia, Sangram S., Gopal Thinakaran, Hilda H. Slunt, et al.. (1996). Studies on the Metabolism and Biological Function of APLP2a. Annals of the New York Academy of Sciences. 777(1). 77–81. 10 indexed citations
14.
Lee, Michael K., Hilda H. Slunt, Lee J. Martin, et al.. (1996). Expression of Presenilin 1 and 2 (PS1 and PS2) in Human and Murine Tissues. Journal of Neuroscience. 16(23). 7513–7525. 244 indexed citations
15.
Zheng, Hui, Minghao Jiang, Myrna E. Trumbauer, et al.. (1996). Mice Deficient for the Amyloid Precursor Protein Gene. Annals of the New York Academy of Sciences. 777(1). 421–426. 61 indexed citations
16.
Borchelt, David, Gopal Thinakaran, Christopher B. Eckman, et al.. (1996). Familial Alzheimer's Disease–Linked Presenilin 1 Variants Elevate Aβ1–42/1–40 Ratio In Vitro and In Vivo. Neuron. 17(5). 1005–1013. 1224 indexed citations breakdown →
17.
Thinakaran, Gopal, Hilda H. Slunt, & Sangram S. Sisodia. (1995). Novel Regulation of Chondroitin Sulfate Glycosaminoglycan Modification of Amyloid Precursor Protein and Its Homologue, APLP2. Journal of Biological Chemistry. 270(28). 16522–16525. 42 indexed citations
18.
Lo, Acy, Gopal Thinakaran, Hilda H. Slunt, & Sangram S. Sisodia. (1995). Metabolism of the Amyloid Precursor-like Protein 2 in MDCK Cells.. Journal of Biological Chemistry. 270(21). 12641–12645. 28 indexed citations
19.
Zheng, Hui, Minghao Jiang, Myrna E. Trumbauer, et al.. (1995). β-amyloid precursor protein-deficient mice show reactive gliosis and decreased locomotor activity. Cell. 81(4). 525–531. 566 indexed citations breakdown →
20.
Lamb, Bruce T., Sangram S. Sisodia, Ann M. Lawler, et al.. (1993). Introduction and expression of the 400 kilobase precursor amyloid protein gene in transgenic mice. Nature Genetics. 5(1). 22–30. 229 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.

Explore authors with similar magnitude of impact

Rankless by CCL
2026