Steven G. Burston

3.0k total citations
37 papers, 2.5k citations indexed

About

Steven G. Burston is a scholar working on Molecular Biology, Materials Chemistry and Pharmacology. According to data from OpenAlex, Steven G. Burston has authored 37 papers receiving a total of 2.5k indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Molecular Biology, 23 papers in Materials Chemistry and 4 papers in Pharmacology. Recurrent topics in Steven G. Burston's work include Enzyme Structure and Function (23 papers), Protein Structure and Dynamics (22 papers) and Heat shock proteins research (21 papers). Steven G. Burston is often cited by papers focused on Enzyme Structure and Function (23 papers), Protein Structure and Dynamics (22 papers) and Heat shock proteins research (21 papers). Steven G. Burston collaborates with scholars based in United Kingdom, United States and France. Steven G. Burston's co-authors include Anthony R. Clarke, Wayne A. Fenton, Neil A. Ranson, Arthur L. Horwich, Hays S. Rye, Zhaohui Xu, Paul B. Sigler, Rosemary A. Staniforth, Tony Atkinson and J. John Holbrook and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Steven G. Burston

36 papers receiving 2.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Steven G. Burston United Kingdom 23 2.3k 1.4k 327 225 96 37 2.5k
Aaron K. Chamberlain United States 19 1.7k 0.7× 448 0.3× 249 0.8× 135 0.6× 94 1.0× 22 2.2k
Krystyna Furtak United States 13 1.7k 0.8× 835 0.6× 241 0.7× 268 1.2× 178 1.9× 16 2.0k
Ray Yu‐Ruei Wang United States 10 1.9k 0.9× 464 0.3× 194 0.6× 259 1.2× 209 2.2× 10 2.5k
Patricia L. Clark United States 30 2.1k 0.9× 505 0.4× 135 0.4× 197 0.9× 592 6.2× 68 2.7k
Michal Žółkiewski United States 24 1.6k 0.7× 482 0.3× 234 0.7× 367 1.6× 287 3.0× 67 2.1k
Joel R. Hoskins United States 32 2.9k 1.3× 833 0.6× 236 0.7× 534 2.4× 1.0k 10.5× 53 3.3k
Vincent Forge France 31 1.8k 0.8× 626 0.4× 148 0.5× 222 1.0× 208 2.2× 46 2.5k
Dagmar Klostermeier Germany 32 2.8k 1.2× 248 0.2× 175 0.5× 158 0.7× 176 1.8× 84 3.0k
Zhaohui Xu Canada 9 1.4k 0.6× 615 0.4× 168 0.5× 135 0.6× 163 1.7× 14 1.7k
Jannette Carey United States 31 2.5k 1.1× 476 0.3× 71 0.2× 148 0.7× 786 8.2× 87 2.9k

Countries citing papers authored by Steven G. Burston

Since Specialization
Citations

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

Fields of papers citing papers by Steven G. Burston

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Steven G. Burston. 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 Steven G. Burston. The network helps show where Steven G. Burston may publish in the future.

Co-authorship network of co-authors of Steven G. Burston

This figure shows the co-authorship network connecting the top 25 collaborators of Steven G. Burston. A scholar is included among the top collaborators of Steven G. Burston 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 Steven G. Burston. Steven G. Burston 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.
Andreeva, Antonina, et al.. (2025). A global survey of intramolecular isopeptide bonds. Protein Science. 34(12). e70342–e70342. 1 indexed citations
2.
Kaschani, Farnusch, Markus Kaiser, Christine Beuck, et al.. (2024). High resolution analysis of proteolytic substrate processing. Journal of Biological Chemistry. 300(11). 107812–107812.
3.
Back, Catherine R., Li‐Chen Han, Nicholas R. Lees, et al.. (2024). Delineation of the complete reaction cycle of a natural Diels–Alderase. Chemical Science. 15(29). 11572–11583. 2 indexed citations
4.
Lafita, Aleix, Vivian Monzon, Catherine R. Back, et al.. (2023). Domain shuffling of a highly mutable ligand‐binding fold drives adhesin generation across the bacterial kingdom. Proteins Structure Function and Bioinformatics. 91(8). 1007–1020. 2 indexed citations
5.
Morgan, Eric R., et al.. (2011). A survey of helminth control practices on sheep farms in Great Britain and Ireland. The Veterinary Journal. 192(3). 390–397. 56 indexed citations
6.
Evans, Simon, Christopher Williams, Christopher J. Arthur, et al.. (2008). An ACP Structural Switch: Conformational Differences between the Apo and Holo Forms of the Actinorhodin Polyketide Synthase Acyl Carrier Protein. ChemBioChem. 9(15). 2424–2432. 37 indexed citations
7.
Cliff, Matthew J., et al.. (2006). Elucidation of Steps in the Capture of a Protein Substrate for Efficient Encapsulation by GroE. Journal of Biological Chemistry. 281(30). 21266–21275. 35 indexed citations
8.
Krzewska, Joanna, Motomasa Tanaka, Steven G. Burston, & Ronald Melki. (2006). Biochemical and Functional Analysis of the Assembly of Full-length Sup35p and Its Prion-forming Domain. Journal of Biological Chemistry. 282(3). 1679–1686. 45 indexed citations
9.
Clarke, Anthony R., et al.. (2004). Identification of a Major Inter-ring Coupling Step in the GroEL Reaction Cycle. Journal of Biological Chemistry. 279(37). 38111–38117. 5 indexed citations
10.
Cliff, Matthew J., Neil M. Kad, Peter A. Lund, et al.. (1999). A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL 1 1Edited by A. R. Fersht. Journal of Molecular Biology. 293(3). 667–684. 63 indexed citations
11.
Burston, Steven G., et al.. (1999). Molecular chaperones and folding catalysts. 1 indexed citations
12.
Sigler, Paul B., Zhaohui Xu, Hays S. Rye, et al.. (1998). STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING. Annual Review of Biochemistry. 67(1). 581–608. 466 indexed citations
13.
Horwich, Arthur L., Steven G. Burston, Hays S. Rye, Jonathan S. Weissman, & Wayne A. Fenton. (1998). [11] Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL. Methods in enzymology on CD-ROM/Methods in enzymology. 290. 141–146. 22 indexed citations
14.
Rye, Hays S., Steven G. Burston, Wayne A. Fenton, et al.. (1997). Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature. 388(6644). 792–798. 338 indexed citations
15.
Burston, Steven G., et al.. (1996). Release of both native and non-native proteins from a cis-only GroEL ternary complex. Nature. 383(6595). 96–99. 83 indexed citations
16.
Parker, MJ, et al.. (1995). Characterisation of the structural and energetic properties of the intermediates on the folding pathways of PGK from Bacillus stearothermophilus. 8. 22–22. 1 indexed citations
17.
Ranson, Neil A., et al.. (1995). Chaperonins can Catalyse the Reversal of Early Aggregation Steps when a Protein Misfolds. Journal of Molecular Biology. 250(5). 581–586. 116 indexed citations
18.
Chen, Shaoxia, Alan M. Roseman, Stephen P. Wood, et al.. (1994). Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy. Nature. 371(6494). 261–264. 284 indexed citations
19.
Jackson, Graham S., Rosemary A. Staniforth, David Halsall, et al.. (1993). Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: Implications for the mechanism of assisted protein folding. Biochemistry. 32(10). 2554–2563. 234 indexed citations
20.
Staniforth, Rosemary A., Steven G. Burston, Corinne J. Smith, et al.. (1993). The energetics and cooperativity of protein folding: a simple experimental analysis based upon the solvation of internal residues. Biochemistry. 32(15). 3842–3851. 55 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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