Thomas E. Creighton

17.5k total citations · 4 hit papers
141 papers, 14.6k citations indexed

About

Thomas E. Creighton is a scholar working on Molecular Biology, Cell Biology and Materials Chemistry. According to data from OpenAlex, Thomas E. Creighton has authored 141 papers receiving a total of 14.6k indexed citations (citations by other indexed papers that have themselves been cited), including 115 papers in Molecular Biology, 58 papers in Cell Biology and 44 papers in Materials Chemistry. Recurrent topics in Thomas E. Creighton's work include Protein Structure and Dynamics (68 papers), Enzyme Structure and Function (44 papers) and Biochemical and Structural Characterization (28 papers). Thomas E. Creighton is often cited by papers focused on Protein Structure and Dynamics (68 papers), Enzyme Structure and Function (44 papers) and Biochemical and Structural Characterization (28 papers). Thomas E. Creighton collaborates with scholars based in United Kingdom, Germany and United States. Thomas E. Creighton's co-authors include Nigel J. Darby, David P. Goldenberg, Johan Kemmink, André Zapun, Jonathan J. Ewbank, Tanja Kortemme, Charles Yanofsky, Carlo P. M. van Mierlo, Robert B. Freedman and Jeffrey W. Nelson and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Thomas E. Creighton

140 papers receiving 13.8k citations

Hit Papers

Proteins: Structures and ... 1979 2026 1994 2010 1986 1992 1979 1987 500 1000 1.5k 2.0k

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Thomas E. Creighton 12.0k 4.4k 3.8k 1.2k 973 141 14.6k
Rainer Jaenicke 13.0k 1.1× 6.1k 1.4× 2.5k 0.7× 942 0.8× 1.1k 1.2× 312 15.9k
Christian B. Anfinsen 15.8k 1.3× 4.5k 1.0× 2.8k 0.7× 1.7k 1.5× 1.5k 1.6× 176 20.5k
Guy Dodson 10.4k 0.9× 2.5k 0.6× 1.8k 0.5× 1.2k 1.1× 1.0k 1.0× 159 13.4k
Yuji Goto 15.7k 1.3× 4.2k 1.0× 1.9k 0.5× 1.7k 1.5× 1.3k 1.4× 377 21.7k
Cyrus Chothia 21.0k 1.7× 6.7k 1.5× 2.5k 0.7× 1.8k 1.5× 1.4k 1.5× 116 25.4k
P. Kraulis 12.1k 1.0× 4.2k 0.9× 1.6k 0.4× 678 0.6× 1.5k 1.6× 18 16.1k
Joël Janin 14.3k 1.2× 6.0k 1.4× 1.2k 0.3× 1.0k 0.9× 950 1.0× 166 17.1k
G.N. Phillips 11.3k 0.9× 3.1k 0.7× 5.1k 1.3× 1.1k 0.9× 622 0.6× 300 16.5k
C. Nick Pace 15.7k 1.3× 6.1k 1.4× 1.8k 0.5× 1.8k 1.5× 1.4k 1.4× 202 21.1k
Frederic M. Richards 11.1k 0.9× 4.8k 1.1× 1.5k 0.4× 1.8k 1.6× 603 0.6× 106 14.2k

Countries citing papers authored by Thomas E. Creighton

Since Specialization
Citations

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

Fields of papers citing papers by Thomas E. Creighton

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Thomas E. Creighton. 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 Thomas E. Creighton. The network helps show where Thomas E. Creighton may publish in the future.

Co-authorship network of co-authors of Thomas E. Creighton

This figure shows the co-authorship network connecting the top 25 collaborators of Thomas E. Creighton. A scholar is included among the top collaborators of Thomas E. Creighton 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 Thomas E. Creighton. Thomas E. Creighton 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.
Creighton, Thomas E.. (1997). Protein folding: Does diffusion determine the folding rate?. Current Biology. 7(6). R380–R383. 16 indexed citations
2.
Creighton, Thomas E.. (1997). How important is the molten globule for correct protein folding?. Trends in Biochemical Sciences. 22(1). 6–10. 80 indexed citations
3.
Kortemme, Tanja, Michelle Hollecker, Johan Kemmink, & Thomas E. Creighton. (1996). Comparison of the (30-51, 14-38) Two-disulphide Folding Intermediates of the Homologous Proteins Dendrotoxin K and Bovine Pancreatic Trypsin Inhibitor by Two-dimensional1H Nuclear Magnetic Resonance. Journal of Molecular Biology. 257(1). 188–198. 8 indexed citations
4.
Creighton, Thomas E.. (1995). Disulphide-coupled protein folding pathways. Philosophical Transactions of the Royal Society B Biological Sciences. 348(1323). 5–10. 22 indexed citations
5.
Darby, Nigel J. & Thomas E. Creighton. (1995). Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase. Biochemistry. 34(51). 16770–16780. 106 indexed citations
6.
Zapun, André, Dominique Missiakas, Satish Raina, & Thomas E. Creighton. (1995). Structural and Functional Characterization of DsbC, a Protein Involved in Disulfide Bond Formation in Escherichia coli. Biochemistry. 34(15). 5075–5089. 214 indexed citations
7.
Goldenberg, David P. & Thomas E. Creighton. (1994). Phage Tailspike Protein: A fishy tale of protein folding. Current Biology. 4(11). 1026–1029. 6 indexed citations
8.
Creighton, Thomas E. & David Shortle. (1994). Electrophoretic Characterization of the Denatured States of Staphylococcal Nuclease. Journal of Molecular Biology. 242(5). 670–682. 28 indexed citations
9.
Creighton, Thomas E. & Robert B. Freedman. (1993). Protein-structure - a model catalyst of protein disulfide bond formation. Kent Academic Repository (University of Kent). 1 indexed citations
10.
Ewbank, Jonathan J. & Thomas E. Creighton. (1992). Protein folding by stages. Current Biology. 2(7). 347–349. 10 indexed citations
11.
Darby, Nigel J., et al.. (1992). Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor. Journal of Molecular Biology. 224(4). 905–911. 28 indexed citations
12.
Creighton, Thomas E. & Peter S. Kim. (1991). Folding and binding. Current Opinion in Structural Biology. 1(1). 3–4. 14 indexed citations
13.
Darby, Nigel J., Carlo P. M. van Mierlo, & Thomas E. Creighton. (1991). The 5–55 single‐disulphide intermediate in folding of bovine pancreatic trypsin inhibitor. FEBS Letters. 279(1). 61–64. 34 indexed citations
14.
Creighton, Thomas E.. (1991). Characterizing intermediates in protein folding. Current Biology. 1(1). 8–10. 26 indexed citations
15.
Mierlo, Carlo P. M. van, Nigel J. Darby, David Neuhaus, & Thomas E. Creighton. (1991). (14–38, 30–51) Double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: A two-dimensional 1H nuclear magnetic resonance study. Journal of Molecular Biology. 222(2). 353–371. 63 indexed citations
16.
States, David J., Thomas E. Creighton, Christopher M. Dobson, & Martin Karplus. (1987). Conformations of intermediates in the folding of the pancreatic trypsin inhibitor. Journal of Molecular Biology. 195(3). 731–739. 85 indexed citations
17.
Creighton, Thomas E.. (1986). [5]Disulfide bonds as probes of protein folding pathways. Methods in enzymology on CD-ROM/Methods in enzymology. 131. 83–106. 181 indexed citations
18.
Creighton, Thomas E.. (1984). Disulfide bond formation in proteins. Methods in enzymology on CD-ROM/Methods in enzymology. 107. 305–329. 165 indexed citations
19.
Creighton, Thomas E.. (1983). Proteins : structures and molecular principles. 305 indexed citations
20.
Creighton, Thomas E.. (1979). Experimental studies of protein folding and unfolding. Progress in Biophysics and Molecular Biology. 33(3). 231–297. 462 indexed citations breakdown →

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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