Deguo Du

2.4k total citations
45 papers, 2.0k citations indexed

About

Deguo Du is a scholar working on Molecular Biology, Physiology and Materials Chemistry. According to data from OpenAlex, Deguo Du has authored 45 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Molecular Biology, 22 papers in Physiology and 9 papers in Materials Chemistry. Recurrent topics in Deguo Du's work include Alzheimer's disease research and treatments (21 papers), Protein Structure and Dynamics (16 papers) and Enzyme Structure and Function (7 papers). Deguo Du is often cited by papers focused on Alzheimer's disease research and treatments (21 papers), Protein Structure and Dynamics (16 papers) and Enzyme Structure and Function (7 papers). Deguo Du collaborates with scholars based in United States, China and United Kingdom. Deguo Du's co-authors include Feng Gai, Jeffery W. Kelly, Cheng‐Yen Huang, Yongjin Zhu, Andrew Dillin, Ehud Cohen, Ewa P. Wojcikiewicz, Eliezer Masliah, Martin Holzenberger and Anthony Adame and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Angewandte Chemie International Edition.

In The Last Decade

Deguo Du

43 papers receiving 2.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Deguo Du United States 21 1.3k 544 456 232 221 45 2.0k
Edith B. Gralla United States 24 1.3k 1.0× 472 0.9× 165 0.4× 106 0.5× 204 0.9× 34 3.0k
Aleister J. Saunders United States 27 1.8k 1.3× 1.5k 2.7× 289 0.6× 63 0.3× 276 1.2× 52 3.3k
Francesco A. Aprile United Kingdom 24 2.0k 1.5× 1.4k 2.6× 278 0.6× 55 0.2× 341 1.5× 60 3.5k
Benedetta Mannini United Kingdom 22 1.3k 1.0× 1.2k 2.2× 191 0.4× 57 0.2× 287 1.3× 43 2.1k
Thomas R. Jahn United Kingdom 21 1.6k 1.2× 1.1k 2.1× 288 0.6× 51 0.2× 348 1.6× 31 2.2k
Brandon H. Toyama United States 11 2.0k 1.5× 788 1.4× 179 0.4× 111 0.5× 277 1.3× 12 2.4k
Carlos W. Bertoncini Argentina 30 1.9k 1.4× 2.0k 3.6× 525 1.2× 41 0.2× 395 1.8× 34 4.4k
Annalisa Relini Italy 36 2.7k 2.0× 1.9k 3.4× 357 0.8× 45 0.2× 417 1.9× 109 4.0k
Claudie Hooper United Kingdom 21 2.1k 1.5× 1.2k 2.2× 153 0.3× 48 0.2× 169 0.8× 41 3.5k
Mathew H. Horrocks United Kingdom 27 1.5k 1.1× 997 1.8× 209 0.5× 28 0.1× 289 1.3× 68 3.0k

Countries citing papers authored by Deguo Du

Since Specialization
Citations

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

Fields of papers citing papers by Deguo Du

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Deguo Du

This figure shows the co-authorship network connecting the top 25 collaborators of Deguo Du. A scholar is included among the top collaborators of Deguo Du 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 Deguo Du. Deguo Du 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.
Du, Deguo, et al.. (2025). Inhibition of amyloid formation of prion fragment (106–128) by polyphenolic compounds. Biochimica et Biophysica Acta (BBA) - General Subjects. 1869(5). 130778–130778.
2.
Shen, Fengyun, et al.. (2023). Effect of phospholipid liposomes on prion fragment (106–128) amyloid formation. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1865(7). 184199–184199. 2 indexed citations
3.
Du, Deguo, et al.. (2022). Mucin-Type O-Glycosylation Proximal to β-Secretase Cleavage Site Affects APP Processing and Aggregation Fate. Frontiers in Chemistry. 10. 859822–859822. 5 indexed citations
4.
Shen, Fengyun, et al.. (2022). Effects of zinc and carnosine on aggregation kinetics of Amyloid-β40 peptide. Biochemistry and Biophysics Reports. 32. 101333–101333. 6 indexed citations
5.
Shen, Fengyun, et al.. (2022). Therapeutic strategies for tauopathies and drug repurposing as a potential approach. Biochemical Pharmacology. 198. 114979–114979. 10 indexed citations
6.
Oyola, Rolando, et al.. (2014). Aggregation Gatekeeper and Controlled Assembly of Trpzip β-Hairpins. Biochemistry. 53(7). 1146–1154. 15 indexed citations
7.
Ojha, Bimlesh, Haiyang Liu, Samrat Dutta, et al.. (2013). Poly(4-styrenesulfonate) as an Inhibitor of Aβ40 Amyloid Fibril Formation. The Journal of Physical Chemistry B. 117(45). 13975–13984. 15 indexed citations
8.
Du, Deguo, Haiyang Liu, & Bimlesh Ojha. (2013). Study Protein Folding and Aggregation Using Nonnatural Amino Acid p-Cyanophenylalanine as a Sensitive Optical Probe. Methods in molecular biology. 1081. 77–89. 2 indexed citations
9.
Holmberg, M., Eva Teuling, Moisés Garcı́a-Arencibia, et al.. (2010). A30 Identification of MOAG-4/SERF as a regulator of age related proteotoxicity. Journal of Neurology Neurosurgery & Psychiatry. 81(Suppl 1). A10.1–A10. 1 indexed citations
10.
Ham, Tjakko J. van, M. Holmberg, Annemieke T. van der Goot, et al.. (2010). Identification of MOAG-4/SERF as a Regulator of Age-Related Proteotoxicity. Cell. 142(4). 601–612. 101 indexed citations
11.
Cohen, Ehud, Johan F. Paulsson, Pablo Blinder, et al.. (2009). Reduced IGF-1 Signaling Delays Age-Associated Proteotoxicity in Mice. Cell. 139(6). 1157–1169. 402 indexed citations
12.
Cohen, Ehud, et al.. (2009). Temporal requirements of insulin/IGF‐1 signaling for proteotoxicity protection. Aging Cell. 9(2). 126–134. 65 indexed citations
13.
Wang, Ting, Zheng Zhou, Michelle R. Bunagan, et al.. (2007). Probing the folding intermediate of Rd‐apocyt b562 by protein engineering and infrared T‐jump. Protein Science. 16(6). 1176–1183. 8 indexed citations
14.
Du, Deguo, Michelle R. Bunagan, & Feng Gai. (2007). The Effect of Charge-Charge Interactions on the Kinetics of α-Helix Formation. Biophysical Journal. 93(11). 4076–4082. 16 indexed citations
15.
Gai, Feng, Deguo Du, & Yao Xu. (2006). Infrared Temperature-Jump Study of the Folding Dynamics of α-Helices and β-Hairpins. Humana Press eBooks. 350. 1–20. 5 indexed citations
16.
Snow, Christopher D., Linlin Qiu, Deguo Du, et al.. (2004). Trp zipper folding kinetics by molecular dynamics and temperature-jump spectroscopy. Proceedings of the National Academy of Sciences. 101(12). 4077–4082. 164 indexed citations
17.
Du, Deguo, Yongjin Zhu, Cheng‐Yen Huang, & Feng Gai. (2004). Understanding the key factors that control the rate of β-hairpin folding. Proceedings of the National Academy of Sciences. 101(45). 15915–15920. 180 indexed citations
18.
Wang, Ting, Yao Xu, Deguo Du, & Feng Gai. (2004). Determining β‐sheet stability by Fourier transform infrared difference spectra. Biopolymers. 75(2). 163–172. 33 indexed citations
19.
20.
Du, Deguo, Shuqing Sun, Qun Zhou, Liang Xu, & Xu Yang. (2000). [Quantitative analysis of rutin and vitamin C by NIR FTIR].. PubMed. 20(4). 474–6. 6 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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