Alan R. Fersht

31.8k total citations · 8 hit papers
264 papers, 26.6k citations indexed

About

Alan R. Fersht is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, Alan R. Fersht has authored 264 papers receiving a total of 26.6k indexed citations (citations by other indexed papers that have themselves been cited), including 245 papers in Molecular Biology, 137 papers in Materials Chemistry and 38 papers in Spectroscopy. Recurrent topics in Alan R. Fersht's work include Protein Structure and Dynamics (160 papers), Enzyme Structure and Function (137 papers) and RNA and protein synthesis mechanisms (61 papers). Alan R. Fersht is often cited by papers focused on Protein Structure and Dynamics (160 papers), Enzyme Structure and Function (137 papers) and RNA and protein synthesis mechanisms (61 papers). Alan R. Fersht collaborates with scholars based in United Kingdom, United States and Germany. Alan R. Fersht's co-authors include Valerie Daggett, Andreas Matouschek, Gideon Schreiber, Luís Serrano, Greg Winter, Luis Serrano, Anthony J. Wilkinson, James T. Kellis, Laura S. Itzhaki and C. Mark Johnson and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Alan R. Fersht

263 papers receiving 25.5k citations

Hit Papers

Hydrogen bonding and biological specificity analysed by p... 1982 2026 1996 2011 1985 1992 1995 1989 1984 250 500 750
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. Hydrogen bonding and biological specificity analysed by protein engineering
    1985 887 citations Alan R. Fersht et al. Nature profile →
  2. The folding of an enzyme
    1992 811 citations Alan R. Fersht, Andreas Matouschek et al. Journal of Molecular Biology profile →
  3. The Structure of the Transition State for Folding of Chymotrypsin Inhibitor 2 Analysed by Protein Engineering Methods: Evidence for a Nucleation-condensation Mechanism for Protein Folding
    1995 631 citations Alan R. Fersht et al. Journal of Molecular Biology profile →
  4. Mapping the transition state and pathway of protein folding by protein engineering
    1989 610 citations Andreas Matouschek, James T. Kellis et al. Nature profile →
  5. The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)
    1984 511 citations Alan R. Fersht et al. profile →
  6. The p53 Pathway: Origins, Inactivation in Cancer, and Emerging Therapeutic Approaches
    2016 477 citations Andreas C. Joerger, Alan R. Fersht profile →
  7. Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding
    1982 285 citations Alan R. Fersht et al. Nature profile →
  8. Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation
    1983 237 citations Alan R. Fersht et al. Biochemistry profile →

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Alan R. Fersht United Kingdom 87 23.6k 10.8k 2.9k 2.8k 2.1k 264 26.6k
H. Jane Dyson United States 94 31.4k 1.3× 10.1k 0.9× 4.4k 1.5× 4.4k 1.6× 2.5k 1.2× 305 37.3k
Robert L. Baldwin United States 93 24.9k 1.1× 9.4k 0.9× 4.1k 1.4× 3.0k 1.1× 1.4k 0.7× 261 29.7k
C. Nick Pace United States 60 15.7k 0.7× 6.1k 0.6× 1.8k 0.6× 1.8k 0.7× 1.4k 0.7× 202 21.1k
Stephan Grzesiek Switzerland 66 22.5k 1.0× 6.0k 0.6× 6.0k 2.1× 2.6k 1.0× 2.2k 1.0× 171 29.5k
John L. Markley United States 72 20.1k 0.9× 5.2k 0.5× 4.9k 1.7× 1.9k 0.7× 1.4k 0.7× 507 27.9k
Sheena E. Radford United Kingdom 84 18.7k 0.8× 6.2k 0.6× 3.1k 1.1× 2.4k 0.9× 1.7k 0.8× 355 25.2k
Frank Delaglio United States 30 19.3k 0.8× 4.7k 0.4× 4.2k 1.5× 2.3k 0.8× 2.0k 1.0× 61 24.8k
Florante A. Quiocho United States 72 13.6k 0.6× 4.8k 0.4× 2.1k 0.7× 2.3k 0.8× 2.3k 1.1× 205 19.1k
J. Deisenhofer United States 72 19.4k 0.8× 4.4k 0.4× 1.1k 0.4× 2.2k 0.8× 2.3k 1.1× 134 27.5k
Cyrus Chothia United Kingdom 70 21.0k 0.9× 6.7k 0.6× 1.8k 0.6× 2.5k 0.9× 1.4k 0.7× 116 25.4k

Countries citing papers authored by Alan R. Fersht

Since Specialization
Citations

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

Fields of papers citing papers by Alan R. Fersht

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Alan R. Fersht. 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 Alan R. Fersht. The network helps show where Alan R. Fersht may publish in the future.

Co-authorship network of co-authors of Alan R. Fersht

This figure shows the co-authorship network connecting the top 25 collaborators of Alan R. Fersht. A scholar is included among the top collaborators of Alan R. Fersht 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 Alan R. Fersht. Alan R. Fersht 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.
Leith, Jason S., Anahita Tafvizi, Fang Huang, et al.. (2012). Sequence-dependent sliding kinetics of p53. Research Online (University of Wollongong). 2012. 1 indexed citations
2.
Korzhnev, Dmitry M., et al.. (2010). A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution. Science. 329(5997). 1312–1316. 244 indexed citations
3.
Brandt, Tobias, et al.. (2010). Molecular basis of S100 proteins interacting with the p53 homologs p63 and p73. Oncogene. 29(14). 2024–2035. 46 indexed citations
4.
Basse, Nicolas, Joel L. Kaar, Giovanni Settanni, et al.. (2010). Toward the Rational Design of p53-Stabilizing Drugs: Probing the Surface of the Oncogenic Y220C Mutant. Chemistry & Biology. 17(1). 46–56. 93 indexed citations
5.
Fernández‐Fernández, María Rosario, Trevor J. Rutherford, & Alan R. Fersht. (2008). Members of the S100 family bind p53 in two distinct ways. Protein Science. 17(10). 1663–1670. 73 indexed citations
6.
Sato, Satoshi, Tomasz L. Religa, & Alan R. Fersht. (2006). Φ-Analysis of the Folding of the B Domain of Protein A Using Multiple Optical Probes. Journal of Molecular Biology. 360(4). 850–864. 49 indexed citations
7.
White, George, Stefano Gianni, J. Günter Grossmann, et al.. (2005). Simulation and Experiment Conspire to Reveal Cryptic Intermediates and a Slide from the Nucleation-condensation to Framework Mechanism of Folding. Journal of Molecular Biology. 350(4). 757–775. 60 indexed citations
8.
Religa, Tomasz L., Joseph S. Markson, Ugo Mayor, Stefan M.V. Freund, & Alan R. Fersht. (2005). Solution structure of a protein denatured state and folding intermediate. Nature. 437(7061). 1053–1056. 203 indexed citations
9.
Fersht, Alan R.. (2002). On the simulation of protein folding by short time scale molecular dynamics and distributed computing. Proceedings of the National Academy of Sciences. 99(22). 14122–14125. 66 indexed citations
10.
Fersht, Alan R. & Fred E. Cohen. (1996). Folding & Design: introduction to a new journal. PubMed. 1(1). i–i.
11.
Clarke, Jane & Alan R. Fersht. (1996). An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway. PubMed. 1(4). 243–254. 92 indexed citations
12.
First, Eric A. & Alan R. Fersht. (1995). Analysis of the Role of the KMSKS Loop in the Catalytic Mechanism of the Tyrosyl-tRNA Synthetase Using Multimutant Cycles. Biochemistry. 34(15). 5030–5043. 56 indexed citations
13.
Fersht, Alan R., Sophie Jackson, & Luís Serrano. (1993). Protein stability: experimental data from protein engineering. Philosophical Transactions of the Royal Society of London Series A Physical and Engineering Sciences. 345(1674). 141–151. 12 indexed citations
14.
Meiering, Elizabeth M., Luis Serrano, & Alan R. Fersht. (1992). Effect of active site residues in barnase on activity and stability. Journal of Molecular Biology. 225(3). 585–589. 203 indexed citations
15.
Serrano, Luís, et al.. (1992). The folding of an enzyme. Journal of Molecular Biology. 224(3). 783–804. 333 indexed citations
16.
Matouschek, Andreas & Alan R. Fersht. (1991). [6] Protein engineering in analysis of protein folding pathways and stability. Methods in enzymology on CD-ROM/Methods in enzymology. 202. 82–112. 80 indexed citations
17.
Fersht, Alan R., Andreas Matouschek, Mark Bycroft, James T. Kellis, & Luis Serrano. (1991). Physical-organic molecular biology: pathway and stability of protein folding. Pure and Applied Chemistry. 63(2). 187–194. 8 indexed citations
18.
Fersht, Alan R., Robin J. Leatherbarrow, & Timothy N. C. Wells. (1986). Structure and activity of the tyrosy1-tRNA synthetase: the hydrogen bond in catalysis and specificity. Philosophical Transactions of the Royal Society of London Series A Mathematical and Physical Sciences. 317(1540). 305–320. 15 indexed citations
19.
Fersht, Alan R., Robin J. Leatherbarrow, & Timothy N. C. Wells. (1986). Binding energy and catalysis: a lesson from protein engineering of the tyrosyl-tRNA synthetase. Trends in Biochemical Sciences. 11(8). 321–325. 63 indexed citations
20.
Fersht, Alan R. & William P. Jencks. (1970). Reactions of nucleophilic reagents with acylating agents of extreme reactivity and unreactivity. Correlation of .beta. values for attacking and leaving group variation. Journal of the American Chemical Society. 92(18). 5442–5452. 53 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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