David C. Thorn

1.8k total citations
27 papers, 1.4k citations indexed

About

David C. Thorn is a scholar working on Molecular Biology, Food Science and Physiology. According to data from OpenAlex, David C. Thorn has authored 27 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 24 papers in Molecular Biology, 13 papers in Food Science and 9 papers in Physiology. Recurrent topics in David C. Thorn's work include Proteins in Food Systems (13 papers), Connexins and lens biology (9 papers) and Advanced Glycation End Products research (8 papers). David C. Thorn is often cited by papers focused on Proteins in Food Systems (13 papers), Connexins and lens biology (9 papers) and Advanced Glycation End Products research (8 papers). David C. Thorn collaborates with scholars based in Australia, United Kingdom and United States. David C. Thorn's co-authors include John A. Carver, Heath Ecroyd, Carl Holt, Agata Rekas, Mark R. Wilson, Margaret Sunde, Sarah Meehan, Christopher M. Dobson, Cait E. MacPhee and Sally L. Gras and has published in prestigious journals such as Journal of Biological Chemistry, Accounts of Chemical Research and Journal of Molecular Biology.

In The Last Decade

David C. Thorn

26 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
David C. Thorn Australia 17 831 658 245 161 146 27 1.4k
Peter Kötter Germany 36 3.7k 4.4× 537 0.8× 58 0.2× 365 2.3× 127 0.9× 67 4.2k
Karin B. Merck Netherlands 12 1.1k 1.4× 201 0.3× 217 0.9× 65 0.4× 205 1.4× 17 1.4k
Bertrand Daignan‐Fornier France 29 2.3k 2.7× 206 0.3× 60 0.2× 371 2.3× 128 0.9× 70 2.7k
Tiziana Lodi Italy 23 1.4k 1.7× 179 0.3× 36 0.1× 186 1.2× 69 0.5× 76 1.8k
Il‐Seon Park South Korea 26 1.1k 1.3× 80 0.1× 255 1.0× 63 0.4× 113 0.8× 57 1.7k
Andreas Hartig Austria 29 2.8k 3.4× 99 0.2× 168 0.7× 308 1.9× 126 0.9× 65 3.1k
Hideyuki Tomitori Japan 22 1.1k 1.3× 83 0.1× 83 0.3× 154 1.0× 51 0.3× 43 1.5k
Joanna Rytka Poland 24 1.8k 2.1× 117 0.2× 60 0.2× 236 1.5× 117 0.8× 77 2.0k
Reiko Urade Japan 27 1.0k 1.2× 148 0.2× 153 0.6× 398 2.5× 75 0.5× 61 2.1k
Hedvig von Bahr‐Lindström Sweden 22 779 0.9× 181 0.3× 90 0.4× 41 0.3× 115 0.8× 35 1.3k

Countries citing papers authored by David C. Thorn

Since Specialization
Citations

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

Fields of papers citing papers by David C. Thorn

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by David C. Thorn. 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 David C. Thorn. The network helps show where David C. Thorn may publish in the future.

Co-authorship network of co-authors of David C. Thorn

This figure shows the co-authorship network connecting the top 25 collaborators of David C. Thorn. A scholar is included among the top collaborators of David C. Thorn 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 David C. Thorn. David C. Thorn 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.
Thorn, David C., et al.. (2025). The Eye Lens Protein, γS Crystallin, Undergoes Glutathionylation-Induced Disulfide Bonding Between Cysteines 22 and 26. Biomolecules. 15(3). 402–402. 1 indexed citations
2.
Shu, Daisy Y., Suman Chaudhary, Kin‐Sang Cho, et al.. (2023). Role of Oxidative Stress in Ocular Diseases: A Balancing Act. Metabolites. 13(2). 187–187. 63 indexed citations
3.
Kumar, Manjeet, Crystall M. D. Swarbrick, David C. Thorn, et al.. (2023). Amyloid fibril formation, structure and domain swapping of acyl‐coenzyme A thioesterase‐7. FEBS Journal. 290(16). 4057–4073. 3 indexed citations
4.
Serebryany, Eugene, Sourav Chowdhury, David C. Thorn, et al.. (2022). A native chemical chaperone in the human eye lens. eLife. 11. 16 indexed citations
5.
Sunde, Margaret, et al.. (2022). Amyloid fibril formation by αS1- and β-casein implies that fibril formation is a general property of casein proteins. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1870(11-12). 140854–140854. 9 indexed citations
6.
Serebryany, Eugene, David C. Thorn, & Liliana Quintanar. (2021). Redox chemistry of lens crystallins: A system of cysteines. Experimental Eye Research. 211. 108707–108707. 17 indexed citations
7.
Williams, Danielle M., David C. Thorn, Christopher M. Dobson, et al.. (2021). The Amyloid Fibril-Forming β-Sheet Regions of Amyloid β and α-Synuclein Preferentially Interact with the Molecular Chaperone 14-3-3ζ. Molecules. 26(20). 6120–6120. 11 indexed citations
8.
Rekas, Agata, et al.. (2020). The Aggregation of αB-Crystallin under Crowding Conditions Is Prevented by αA-Crystallin: Implications for α-Crystallin Stability and Lens Transparency. Journal of Molecular Biology. 432(20). 5593–5613. 11 indexed citations
9.
Thorn, David C., Tomas Koudelka, Peter Hoffmann, et al.. (2020). Native disulphide-linked dimers facilitate amyloid fibril formation by bovine milk αS2-casein. Biophysical Chemistry. 270. 106530–106530. 13 indexed citations
10.
Carver, John A., Heath Ecroyd, Roger J.W. Truscott, David C. Thorn, & Carl Holt. (2018). Proteostasis and the Regulation of Intra- and Extracellular Protein Aggregation by ATP-Independent Molecular Chaperones: Lens α-Crystallins and Milk Caseins. Accounts of Chemical Research. 51(3). 745–752. 43 indexed citations
11.
Thorn, David C., et al.. (2018). The Structure and Stability of the Disulfide-Linked γS-Crystallin Dimer Provide Insight into Oxidation Products Associated with Lens Cataract Formation. Journal of Molecular Biology. 431(3). 483–497. 29 indexed citations
12.
Kumar, Manjeet, Yuning Hong, David C. Thorn, Heath Ecroyd, & John A. Carver. (2017). Monitoring Early-Stage Protein Aggregation by an Aggregation-Induced Emission Fluorogen. Analytical Chemistry. 89(17). 9322–9329. 65 indexed citations
13.
Liu, Jihua, John A. Carver, & David C. Thorn. (2014). Amyloid fibril by β-casein and its influence factor. Gaodeng xuexiao huaxue xuebao. 35(5). 976. 1 indexed citations
14.
Ecroyd, Heath, Megan Garvey, David C. Thorn, Juliet A. Gerrard, & John A. Carver. (2013). Amyloid Fibrils from Readily Available Sources: Milk Casein and Lens Crystallin Proteins. Methods in molecular biology. 996. 103–117. 4 indexed citations
15.
Holt, Carl, John A. Carver, Heath Ecroyd, & David C. Thorn. (2013). Invited review: Caseins and the casein micelle: Their biological functions, structures, and behavior in foods. Journal of Dairy Science. 96(10). 6127–6146. 342 indexed citations
16.
Treweek, Teresa M., David C. Thorn, William E. Price, & John A. Carver. (2011). The chaperone action of bovine milk αS1- and αS2-caseins and their associated form αS-casein. Archives of Biochemistry and Biophysics. 510(1). 42–52. 53 indexed citations
17.
Thorn, David C., Heath Ecroyd, & John A. Carver. (2009). The two-faced nature of milk casein proteins: amyloid fibril formation and chaperone-like activity. Australian Journal of Dairy Technology. 64(1). 34–40. 21 indexed citations
18.
Ecroyd, Heath, Tomas Koudelka, David C. Thorn, et al.. (2008). Dissociation from the Oligomeric State Is the Rate-limiting Step in Fibril Formation by κ-Casein. Journal of Biological Chemistry. 283(14). 9012–9022. 69 indexed citations
19.
Rekas, Agata, Lucy Jankova, David C. Thorn, Roberto Cappai, & John A. Carver. (2007). Monitoring the prevention of amyloid fibril formation by α‐crystallin. FEBS Journal. 274(24). 6290–6304. 64 indexed citations
20.
Carver, John A., Agata Rekas, David C. Thorn, & Mark R. Wilson. (2003). Small Heat‐shock Proteins and Clusterin: Intra‐ and Extracellular Molecular Chaperones with a Common Mechanism of Action and Function?. IUBMB Life. 55(12). 661–668. 163 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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