Shu-Hui Yen

6.6k total citations · 2 hit papers
58 papers, 5.0k citations indexed

About

Shu-Hui Yen is a scholar working on Physiology, Neurology and Molecular Biology. According to data from OpenAlex, Shu-Hui Yen has authored 58 papers receiving a total of 5.0k indexed citations (citations by other indexed papers that have themselves been cited), including 43 papers in Physiology, 26 papers in Neurology and 22 papers in Molecular Biology. Recurrent topics in Shu-Hui Yen's work include Alzheimer's disease research and treatments (41 papers), Parkinson's Disease Mechanisms and Treatments (22 papers) and Neuroscience and Neuropharmacology Research (10 papers). Shu-Hui Yen is often cited by papers focused on Alzheimer's disease research and treatments (41 papers), Parkinson's Disease Mechanisms and Treatments (22 papers) and Neuroscience and Neuropharmacology Research (10 papers). Shu-Hui Yen collaborates with scholars based in United States, Japan and United Kingdom. Shu-Hui Yen's co-authors include Dennis W. Dickson, Peizhou Jiang, Jada Lewis, Peter Davies, Parimala Nacharaju, Li‐wen Ko, Daniel Sevlever, Michael Hutton, Wen-Lang Lin and Ágnes Kenessey and has published in prestigious journals such as Science, Journal of Biological Chemistry and Neuron.

In The Last Decade

Shu-Hui Yen

58 papers receiving 4.9k citations

Hit Papers

Neurofibrillary tangles, amyotrophy and progressive motor... 1992 2026 2003 2014 2000 1992 250 500 750 1000

Peers

Shu-Hui Yen
Shu‐Hui Yen United States
Nicholas M. Kanaan United States
Yasuji Matsuoka United States
Robin Barbour United States
Selina Wray United Kingdom
Urmi Sengupta United States
T Saitoh United States
Shu‐Hui Yen United States
Shu-Hui Yen
Citations per year, relative to Shu-Hui Yen Shu-Hui Yen (= 1×) peers Shu‐Hui Yen

Countries citing papers authored by Shu-Hui Yen

Since Specialization
Citations

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

Fields of papers citing papers by Shu-Hui Yen

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Shu-Hui Yen. 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 Shu-Hui Yen. The network helps show where Shu-Hui Yen may publish in the future.

Co-authorship network of co-authors of Shu-Hui Yen

This figure shows the co-authorship network connecting the top 25 collaborators of Shu-Hui Yen. A scholar is included among the top collaborators of Shu-Hui Yen 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 Shu-Hui Yen. Shu-Hui Yen 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.
Jiang, Peizhou, Ming Gan, Shu-Hui Yen, Pamela J. McLean, & Dennis W. Dickson. (2017). Impaired endo-lysosomal membrane integrity accelerates the seeding progression of α-synuclein aggregates. Scientific Reports. 7(1). 7690–7690. 78 indexed citations
2.
Jiang, Peizhou, Peng Huang, Shu-Hui Yen, Abba C. Zubair, & Dennis W. Dickson. (2016). Genetic modification of H2AX renders mesenchymal stromal cell–derived dopamine neurons more resistant to DNA damage and subsequent apoptosis. Cytotherapy. 18(12). 1483–1492. 7 indexed citations
3.
Jiang, Peizhou, Ming Gan, & Shu-Hui Yen. (2013). Dopamine prevents lipid peroxidation-induced accumulation of toxic α-synuclein oligomers by preserving autophagy-lysosomal function. Frontiers in Cellular Neuroscience. 7. 81–81. 17 indexed citations
4.
Jiang, Peizhou, Ming Gan, Abdul Shukkur Ebrahim, et al.. (2010). ER stress response plays an important role in aggregation of α-synuclein. Molecular Neurodegeneration. 5(1). 56–56. 93 indexed citations
5.
Zhang, Yong‐Jie, Tania F. Gendron, Ya-Fei Xu, et al.. (2010). Phosphorylation regulates proteasomal-mediated degradation and solubility of TAR DNA binding protein-43 C-terminal fragments. Molecular Neurodegeneration. 5(1). 33–33. 104 indexed citations
7.
Ko, Li‐wen, et al.. (2008). Aggregates Assembled From Overexpression of Wild-Type α-Synuclein are not Toxic to Human Neuronal Cells. Journal of Neuropathology & Experimental Neurology. 67(11). 1084–1096. 38 indexed citations
8.
Ko, Li‐wen, et al.. (2006). Cytosine β-D-arabinofuranoside used as a Paradigm Modifier to Increase Production of Tau Aggregates in a Cellular Model of Tauopathy. Neurochemical Research. 32(4-5). 823–832. 2 indexed citations
9.
Bhaskar, Kiran, Shu-Hui Yen, & Gloria Lee. (2005). Disease-related Modifications in Tau Affect the Interaction between Fyn and Tau. Journal of Biological Chemistry. 280(42). 35119–35125. 187 indexed citations
10.
Ko, Li‐wen, et al.. (2004). Recent advances in experimental modeling of the assembly of tau filaments. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1739(2-3). 125–139. 16 indexed citations
11.
Lin, Wen-Lang, Jada Lewis, Shu-Hui Yen, Michael Hutton, & Dennis W. Dickson. (2003). Ultrastructural neuronal pathology in transgenic mice expressing mutant (P301L) human tau. Journal of Neurocytology. 32(9). 1091–1105. 108 indexed citations
12.
Ishizawa, Takashi, Koichi Ishiguro, Eileen McGowan, et al.. (2003). Co-Localization of Glycogen Synthase Kinase-3 with Neurofibrillary Tangles and Granulovacuolar Degeneration in Transgenic Mice. American Journal Of Pathology. 163(3). 1057–1067. 77 indexed citations
13.
Grover, Andrew, Michael DeTure, Shu-Hui Yen, & Mike Hutton. (2002). Effects on splicing and protein function of three mutations in codon N296 of tau in vitro. Neuroscience Letters. 323(1). 33–36. 39 indexed citations
14.
Ko, Li‐wen, et al.. (2002). Cellular Models for Tau Filament Assembly. Journal of Molecular Neuroscience. 19(3). 309–316. 13 indexed citations
15.
DeTure, Michael, Li‐wen Ko, Colin Easson, & Shu-Hui Yen. (2002). tau Assembly in Inducible Transfectants Expressing Wild-Type or FTDP-17 tau. American Journal Of Pathology. 161(5). 1711–1722. 59 indexed citations
16.
Nacharaju, Parimala, et al.. (1999). Accelerated filament formation from tau protein with specific FTDP‐17 missense mutations. FEBS Letters. 447(2-3). 195–199. 237 indexed citations
17.
Sironi, Juan, et al.. (1998). Ser‐262 in human recombinant tau protein is a markedly more favorable site for phosphorylation by CaMKII than PKA or PhK. FEBS Letters. 436(3). 471–475. 68 indexed citations
18.
Ko, Li‐wen, Toshinari Odawara, & Shu-Hui Yen. (1997). Menadione-induced tau dephosphorylation in cultured human neuroblastoma cells. Brain Research. 760(1-2). 118–128. 24 indexed citations
19.
Ko, Li‐wen, et al.. (1996). Modulated induction of tau proteins in cultured human neuroblastoma cells. Brain Research. 707(2). 256–265. 7 indexed citations
20.
Ksiȩżak-Reding, Hanna & Shu-Hui Yen. (1991). Structural stability of paired helical filaments requires microtubule-binding domains of Tau: A model for self-association. Neuron. 6(5). 717–728. 117 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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