Paul T. Wingfield

21.2k total citations · 4 hit papers
238 papers, 16.5k citations indexed

About

Paul T. Wingfield is a scholar working on Molecular Biology, Virology and Infectious Diseases. According to data from OpenAlex, Paul T. Wingfield has authored 238 papers receiving a total of 16.5k indexed citations (citations by other indexed papers that have themselves been cited), including 146 papers in Molecular Biology, 54 papers in Virology and 46 papers in Infectious Diseases. Recurrent topics in Paul T. Wingfield's work include HIV Research and Treatment (54 papers), Protein Structure and Dynamics (44 papers) and HIV/AIDS drug development and treatment (41 papers). Paul T. Wingfield is often cited by papers focused on HIV Research and Treatment (54 papers), Protein Structure and Dynamics (44 papers) and HIV/AIDS drug development and treatment (41 papers). Paul T. Wingfield collaborates with scholars based in United States, Switzerland and United Kingdom. Paul T. Wingfield's co-authors include Stephen J. Stahl, Angela M. Gronenborn, G. Marius Clore, Ad Bax, Alasdair C. Steven, Joshua D. Kaufman, Ira Palmer, Paul C. Driscoll, Stephan Grzesiek and Adam Zlotnick and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Paul T. Wingfield

235 papers receiving 16.1k citations

Hit Papers

Overcoming the overlap problem in the assignment of proto... 1989 2026 2001 2013 1989 1991 1993 2014 200 400 600

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Paul T. Wingfield United States 67 9.8k 2.6k 2.5k 2.3k 2.3k 238 16.5k
Peter S. Kim United States 75 17.7k 1.8× 5.6k 2.2× 2.8k 1.1× 3.0k 1.3× 4.5k 2.0× 176 26.9k
Charles S. Craik United States 76 10.6k 1.1× 1.2k 0.5× 2.2k 0.9× 2.0k 0.9× 2.3k 1.0× 344 19.6k
Alexander Wlodawer United States 71 12.7k 1.3× 3.6k 1.4× 1.5k 0.6× 915 0.4× 4.0k 1.8× 371 19.0k
Stephen B. H. Kent United States 77 22.2k 2.3× 2.0k 0.8× 1.6k 0.6× 1.7k 0.7× 2.3k 1.0× 261 29.0k
David R. Davies United States 62 14.0k 1.4× 1.6k 0.6× 3.7k 1.5× 1.1k 0.5× 2.0k 0.9× 146 20.1k
Jacob V. Maizel United States 54 9.7k 1.0× 1.3k 0.5× 1.5k 0.6× 1.3k 0.6× 2.3k 1.0× 171 15.4k
Martin Billeter Switzerland 71 13.3k 1.4× 609 0.2× 1.4k 0.6× 4.7k 2.0× 2.4k 1.1× 190 20.2k
Wayne A. Hendrickson United States 89 20.0k 2.0× 6.1k 2.3× 6.5k 2.6× 1.5k 0.6× 3.5k 1.5× 300 32.6k
David I. Stuart United Kingdom 102 15.5k 1.6× 3.8k 1.4× 5.9k 2.4× 3.9k 1.7× 7.4k 3.3× 459 38.7k
Christopher P. Hill United States 61 10.0k 1.0× 3.0k 1.2× 1.4k 0.6× 1.7k 0.8× 1.7k 0.8× 138 13.3k

Countries citing papers authored by Paul T. Wingfield

Since Specialization
Citations

This map shows the geographic impact of Paul T. Wingfield'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 Paul T. Wingfield with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Paul T. Wingfield more than expected).

Fields of papers citing papers by Paul T. Wingfield

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Paul T. Wingfield. 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 Paul T. Wingfield. The network helps show where Paul T. Wingfield may publish in the future.

Co-authorship network of co-authors of Paul T. Wingfield

This figure shows the co-authorship network connecting the top 25 collaborators of Paul T. Wingfield. A scholar is included among the top collaborators of Paul T. Wingfield 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 Paul T. Wingfield. Paul T. Wingfield 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.
Bhandari, Yuba R., Ping Yu, William F. Heinz, et al.. (2024). Determining structures of RNA conformers using AFM and deep neural networks. Nature. 637(8048). 1234–1243. 12 indexed citations
2.
Eren, Elif, Norman R. Watts, James F. Conway, & Paul T. Wingfield. (2024). Myxococcus xanthus encapsulin cargo protein EncD is a flavin-binding protein with ferric reductase activity. Proceedings of the National Academy of Sciences. 121(21). e2400426121–e2400426121. 4 indexed citations
3.
Eren, Elif, et al.. (2024). Encapsulated Ferritin-like Proteins: A Structural Perspective. Biomolecules. 14(6). 624–624. 4 indexed citations
4.
Watts, Norman R., Elif Eren, Ira Palmer, et al.. (2023). The ribosome-inactivating proteins MAP30 and Momordin inhibit SARS-CoV-2. PLoS ONE. 18(6). e0286370–e0286370. 3 indexed citations
5.
Dambuza, Ivy M., Chang He, Jin Kyeong Choi, et al.. (2017). IL-12p35 induces expansion of IL-10 and IL-35-expressing regulatory B cells and ameliorates autoimmune disease. Nature Communications. 8(1). 719–719. 145 indexed citations
6.
Wingfield, Paul T., et al.. (2016). An Investigation of Patient Preferences for Music Played Before Electroconvulsive Therapy. Journal of Ect. 32(3). 192–196. 3 indexed citations
7.
Lin, Xiaoyan, Soojay Banerjee, Joshua D. Kaufman, et al.. (2014). Z-disc-associated, Alternatively Spliced, PDZ Motif-containing Protein (ZASP) Mutations in the Actin-binding Domain Cause Disruption of Skeletal Muscle Actin Filaments in Myofibrillar Myopathy. Journal of Biological Chemistry. 289(19). 13615–13626. 40 indexed citations
8.
Watts, Norman R., Giovanni Cardone, Naiqian Cheng, et al.. (2008). Non-canonical Binding of an Antibody Resembling a Naïve B Cell Receptor Immunoglobulin to Hepatitis B Virus Capsids. Journal of Molecular Biology. 379(5). 1119–1129. 17 indexed citations
9.
Jaroniec, Christopher P., Joshua D. Kaufman, Stephen J. Stahl, et al.. (2005). Structure and Dynamics of Micelle-Associated Human Immunodeficiency Virus gp41 Fusion Domain ,. Biochemistry. 44(49). 16167–16180. 113 indexed citations
10.
Hejtmancik, J. Fielding, Paul T. Wingfield, & Yuri V. Sergeev. (2004). β-Crystallin association. Experimental Eye Research. 79(3). 377–383. 51 indexed citations
11.
Rubin, Jeffrey S., Regina M. Day, Neşe Atabey, et al.. (2001). Dissociation of Heparan Sulfate and Receptor Binding Domains of Hepatocyte Growth Factor Reveals That Heparan Sulfate-c-Met Interaction Facilitates Signaling. Journal of Biological Chemistry. 276(35). 32977–32983. 86 indexed citations
12.
Yang, Zhongning, Timothy C. Mueser, Joshua D. Kaufman, et al.. (1999). The Crystal Structure of the SIV gp41 Ectodomain at 1.47 Å Resolution. Journal of Structural Biology. 126(2). 131–144. 109 indexed citations
13.
Kaufman, Joshua D., Stephen J. Stahl, Paul T. Wingfield, et al.. (1998). The solution structure of the N-terminal domain of hepatocyte growth factor reveals a potential heparin-binding site. Structure. 6(1). 109–116. 47 indexed citations
14.
Sakata, Hiromi, Stephen J. Stahl, William G. Taylor, et al.. (1997). Heparin Binding and Oligomerization of Hepatocyte Growth Factor/Scatter Factor Isoforms. Journal of Biological Chemistry. 272(14). 9457–9463. 117 indexed citations
15.
Wingfield, Paul T., Stephen J. Stahl, Robert W. Williams, & Alasdair C. Steven. (1995). Hepatitis Core Antigen Produced in Escherichia coli: Subunit Composition, Conformation Analysis, and in Vitro Capsid Assembly. Biochemistry. 34(15). 4919–4932. 204 indexed citations
16.
Fankhauser, Christian, Elisa Izaurralde, Yasuhisa Adachi, Paul T. Wingfield, & Ulrich K. Laemmli. (1991). Specific Complex of Human Immunodeficiency Virus Type 1 Rev and Nucleolar B23 Proteins: Dissociation by the Rev Response Element. Molecular and Cellular Biology. 11(5). 2567–2575. 80 indexed citations
17.
Forman‐Kay, Julie D., et al.. (1990). Studies on the solution conformation of human thioredoxin using heteronuclear nitrogen-15-proton nuclear magnetic resonance spectroscopy. Biochemistry. 29(6). 1566–1572. 72 indexed citations
18.
Movva, N. Rao, Dominique Semon, Eric Kawashima, et al.. (1990). Cloning and nucleotide sequence of the Salmonella typhimurium pepM gene. Molecular and General Genetics MGG. 223(2). 345–348. 15 indexed citations
19.
Forman‐Kay, Julie D., G. Marius Clore, Paul C. Driscoll, et al.. (1989). A proton nuclear magnetic resonance assignment and secondary structure determination of recombinant human thioredoxin. Biochemistry. 28(17). 7088–7097. 19 indexed citations
20.
Wingfield, Paul T., Robert J. Mattaliano, H. Robson MacDonald, et al.. (1987). Recombinant-derived interleukin-1α stabilized against specific deamidation. Protein Engineering Design and Selection. 1(5). 413–417. 30 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