Lynne Regan

11.6k total citations
173 papers, 9.2k citations indexed

About

Lynne Regan is a scholar working on Molecular Biology, Materials Chemistry and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, Lynne Regan has authored 173 papers receiving a total of 9.2k indexed citations (citations by other indexed papers that have themselves been cited), including 150 papers in Molecular Biology, 60 papers in Materials Chemistry and 22 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in Lynne Regan's work include Protein Structure and Dynamics (86 papers), RNA and protein synthesis mechanisms (59 papers) and Enzyme Structure and Function (56 papers). Lynne Regan is often cited by papers focused on Protein Structure and Dynamics (86 papers), RNA and protein synthesis mechanisms (59 papers) and Enzyme Structure and Function (56 papers). Lynne Regan collaborates with scholars based in United States, United Kingdom and Israel. Lynne Regan's co-authors include Catherine K. Smith, Aitziber L. Cortajarena, William F. DeGrado, Indraneel Ghosh, Andrew D. Hamilton, Thomas J. Magliery, Ewan R.G. Main, Roberto Valverde, Jane S. Merkel and S. G. J. Mochrie and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Lynne Regan

172 papers receiving 9.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Lynne Regan United States 52 7.7k 2.3k 867 735 680 173 9.2k
Duilio Cascio United States 55 8.0k 1.0× 2.0k 0.9× 705 0.8× 917 1.2× 378 0.6× 156 10.8k
Petr V. Konarev Russia 39 7.0k 0.9× 2.8k 1.2× 894 1.0× 1.0k 1.4× 335 0.5× 183 10.6k
J. Martin Scholtz United States 45 8.5k 1.1× 3.0k 1.3× 748 0.9× 619 0.8× 515 0.8× 91 10.9k
Tom Alber United States 62 10.3k 1.3× 3.0k 1.3× 1.2k 1.4× 1.2k 1.6× 575 0.8× 131 13.1k
Tamir Gonen United States 52 7.2k 0.9× 2.8k 1.2× 1.2k 1.4× 607 0.8× 429 0.6× 148 10.8k
Tanja Kortemme United States 55 9.1k 1.2× 2.6k 1.1× 768 0.9× 662 0.9× 1.1k 1.7× 100 11.0k
Masahiro Shirakawa Japan 56 6.8k 0.9× 2.2k 1.0× 674 0.8× 1.0k 1.4× 490 0.7× 205 9.7k
Maxim V. Petoukhov Germany 33 6.8k 0.9× 3.0k 1.3× 856 1.0× 951 1.3× 334 0.5× 86 9.5k
Daniel Franke Germany 28 4.8k 0.6× 3.1k 1.4× 637 0.7× 652 0.9× 352 0.5× 51 8.5k
James D. Lear United States 48 6.1k 0.8× 848 0.4× 905 1.0× 390 0.5× 432 0.6× 87 7.8k

Countries citing papers authored by Lynne Regan

Since Specialization
Citations

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

Fields of papers citing papers by Lynne Regan

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Lynne Regan

This figure shows the co-authorship network connecting the top 25 collaborators of Lynne Regan. A scholar is included among the top collaborators of Lynne Regan 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 Lynne Regan. Lynne Regan 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.
Kitchen, Philip, et al.. (2025). Engineering Protein–Peptide Interfaces via Combinatorial Mutagenesis and Mass Photometric Screening. Biomolecules. 15(8). 1183–1183.
2.
Laohakunakorn, Nadanai, et al.. (2025). Cell-Free Protein Synthesis as a Method to Rapidly Screen Machine Learning-Generated Protease Variants. ACS Synthetic Biology. 14(5). 1710–1718. 2 indexed citations
3.
Regan, Lynne, et al.. (2023). Modulating the Viscoelastic Properties of Covalently Crosslinked Protein Hydrogels. Gels. 9(6). 481–481. 2 indexed citations
4.
Rawlings, Andrea E., Daniel T. Peters, Fiona Whelan, et al.. (2020). Rational Design and Self-Assembly of Coiled-Coil Linked SasG Protein Fibrils. ACS Synthetic Biology. 9(7). 1599–1607. 4 indexed citations
5.
Regan, Lynne, et al.. (2018). Comparing side chain packing in soluble proteins, protein‐protein interfaces, and transmembrane proteins. Proteins Structure Function and Bioinformatics. 86(5). 581–591. 7 indexed citations
6.
Regan, Lynne, et al.. (2016). Random close packing in protein cores. Physical review. E. 93(3). 32415–32415. 18 indexed citations
7.
Kamenetska, Maria, et al.. (2014). Routes to DNA Accessibility: Alternative Pathways for Nucleosome Unwinding. Biophysical Journal. 107(2). 384–392. 7 indexed citations
8.
O’Hern, Corey S., et al.. (2013). The power of hard-sphere models for proteins: Understanding side-chain conformations and predicting thermodynamic stability. Bulletin of the American Physical Society. 2013. 1 indexed citations
9.
O’Hern, Corey S., et al.. (2013). New Insights into the Interdependence between Amino Acid Stereochemistry and Protein Structure. Biophysical Journal. 105(10). 2403–2411. 13 indexed citations
10.
Kundrat, Lenka, et al.. (2009). A structural model for the HAT domain of Utp6 incorporating bioinformatics and genetics. Protein Engineering Design and Selection. 22(7). 431–439. 10 indexed citations
11.
Valverde, Roberto, Irina Pozdnyakova, Tommi Kajander, Janani Venkatraman, & Lynne Regan. (2007). Fragile X Mental Retardation Syndrome: Structure of the KH1-KH2 Domains of Fragile X Mental Retardation Protein. Structure. 15(9). 1090–1098. 55 indexed citations
12.
Pozdnyakova, Irina & Lynne Regan. (2005). New insights into Fragile X syndrome. FEBS Journal. 272(3). 872–878. 15 indexed citations
13.
Cortajarena, Aitziber L., Tommi Kajander, Weihong Pan, Melanie J. Cocco, & Lynne Regan. (2004). Protein design to understand peptide ligand recognition by tetratricopeptide repeat proteins. Protein Engineering Design and Selection. 17(4). 399–409. 63 indexed citations
14.
Magliery, Thomas J. & Lynne Regan. (2004). Library approaches to biophysical problems. European Journal of Biochemistry. 271(9). 1593–1594. 1 indexed citations
15.
Merkel, Jane S. & Lynne Regan. (2000). Modulating Protein Folding Rates in Vivo and in Vitro by Side-chain Interactions between the Parallel β Strands of Green Fluorescent Protein. Journal of Biological Chemistry. 275(38). 29200–29206. 26 indexed citations
16.
Merkel, Jane S., Julian M. Sturtevant, & Lynne Regan. (1999). Sidechain interactions in parallel β sheets: the energetics of cross-strand pairings. Structure. 7(11). 1333–1343. 88 indexed citations
17.
Anderson, Karen S., et al.. (1999). Using loop length variants to dissect the folding pathway of a four-helix-bundle protein. Journal of Molecular Biology. 286(1). 257–265. 47 indexed citations
18.
Merkel, Jane S. & Lynne Regan. (1998). Aromatic rescue of glycine in β sheets. PubMed. 3(6). 449–456. 67 indexed citations
19.
Munson, Mary, Karen S. Anderson, & Lynne Regan. (1997). Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude. PubMed. 2(1). 77–87. 51 indexed citations
20.
Regan, Lynne, Luis Serrano, Andrej Săli, Amnon Horovitz, & Charles B. Wilson. (1997). Paper alert. 2(6). R105–R108. 1 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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