Philip A. Evans

4.2k total citations · 1 hit paper
35 papers, 3.7k citations indexed

About

Philip A. Evans is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, Philip A. Evans has authored 35 papers receiving a total of 3.7k indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Molecular Biology, 20 papers in Materials Chemistry and 7 papers in Spectroscopy. Recurrent topics in Philip A. Evans's work include Protein Structure and Dynamics (25 papers), Enzyme Structure and Function (20 papers) and Glycosylation and Glycoproteins Research (8 papers). Philip A. Evans is often cited by papers focused on Protein Structure and Dynamics (25 papers), Enzyme Structure and Function (20 papers) and Glycosylation and Glycoproteins Research (8 papers). Philip A. Evans collaborates with scholars based in United Kingdom, United States and South Sudan. Philip A. Evans's co-authors include Sheena E. Radford, Christopher M. Dobson, Jean Baum, Christopher M. Dobson, Brent Holmes, Robert O. Fox, Derek N. Woolfson, Roger A. Kautz, Maureen Pitkeathly and Dudley H. Williams and has published in prestigious journals such as Nature, SHILAP Revista de lepidopterología and Journal of Molecular Biology.

In The Last Decade

Philip A. Evans

35 papers receiving 3.6k citations

Hit Papers

The folding of hen lysozy... 1992 2026 2003 2014 1992 200 400 600

Author Peers

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

Author Last Decade Papers Cites
Philip A. Evans 3.2k 2.0k 517 387 382 35 3.7k
Katsuhide Yutani 3.8k 1.2× 2.1k 1.1× 279 0.5× 263 0.7× 370 1.0× 154 4.5k
Rudolf Gilmanshin 2.6k 0.8× 1.2k 0.6× 469 0.9× 389 1.0× 390 1.0× 26 3.5k
Gennady V. Semisotnov 3.0k 1.0× 1.6k 0.8× 228 0.4× 554 1.4× 477 1.2× 52 3.7k
A. Ducruix 2.6k 0.8× 1.5k 0.7× 271 0.5× 132 0.3× 332 0.9× 103 3.8k
Christina Redfield 4.2k 1.3× 1.8k 0.9× 1.0k 2.0× 490 1.3× 497 1.3× 140 5.5k
Jochen Balbach 2.6k 0.8× 989 0.5× 412 0.8× 161 0.4× 293 0.8× 127 3.4k
Robert Fairman 3.5k 1.1× 976 0.5× 259 0.5× 129 0.3× 497 1.3× 102 4.4k
Manuel Rico 3.0k 0.9× 893 0.4× 322 0.6× 189 0.5× 145 0.4× 91 3.5k
Valentina E. Bychkova 1.8k 0.5× 979 0.5× 190 0.4× 442 1.1× 336 0.9× 50 2.6k
B. Birdsall 2.4k 0.7× 1.2k 0.6× 524 1.0× 206 0.5× 185 0.5× 114 3.4k

Countries citing papers authored by Philip A. Evans

Since Specialization
Citations

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

Fields of papers citing papers by Philip A. Evans

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Philip A. Evans. 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 Philip A. Evans. The network helps show where Philip A. Evans may publish in the future.

Co-authorship network of co-authors of Philip A. Evans

This figure shows the co-authorship network connecting the top 25 collaborators of Philip A. Evans. A scholar is included among the top collaborators of Philip A. Evans 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 Philip A. Evans. Philip A. Evans 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.
Crebolder, Harry, et al.. (2005). The European definition of Family Medicine (General Practice / Family Medicine). SHILAP Revista de lepidopterología. 3 indexed citations
2.
Evans, Philip A., et al.. (2002). Penetrating Injury of the Temporal Fossa with a Screwdriver with Associated Traumatic Optic Neuropathy. The Journal of Trauma: Injury, Infection, and Critical Care. 52(6). 1189–1191. 9 indexed citations
3.
Chen, Rita P.‐Y., et al.. (2001). The role of a β‐bulge in the folding of the β‐hairpin structure in ubiquitin. Protein Science. 10(10). 2063–2074. 24 indexed citations
4.
Williams, Dudley H., et al.. (2000). Structural characterization of a mutant peptide derived from ubiquitin: Implications for protein folding. Protein Science. 9(11). 2142–2150. 46 indexed citations
6.
Kuhlman, Brian, Donna L. Luisi, Philip A. Evans, & Daniel P. Raleigh. (1998). Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9 1 1Edited by P. E. Wright. Journal of Molecular Biology. 284(5). 1661–1670. 96 indexed citations
7.
Evans, Philip A., et al.. (1996). Experimental investigation of sidechain interactions in early folding intermediates. PubMed. 1(2). R31–R37. 14 indexed citations
8.
Evans, Philip A., et al.. (1996). Structure of very early protein folding intermediates: new insights through a variant of hydrogen exchange labelling. PubMed. 1(6). 407–417. 95 indexed citations
9.
Itzhaki, Laura S. & Philip A. Evans. (1996). Solvent isotope effects on the refolding kinetics of hen egg‐white lysozyme. Protein Science. 5(1). 140–146. 34 indexed citations
10.
Tisi, Laurence & Philip A. Evans. (1995). Conserved structural features on protein surfaces: Small exterior hydrophobic clusters. Journal of Molecular Biology. 249(2). 251–258. 29 indexed citations
11.
Itzhaki, Laura S., Philip A. Evans, Christopher M. Dobson, & Sheena E. Radford. (1994). Tertiary Interactions in the Folding Pathway of Hen Lysozyme: Kinetic Studies Using Fluorescent Probes. Biochemistry. 33(17). 5212–5220. 119 indexed citations
12.
Evans, Philip A., et al.. (1994). Understanding how proteins fold: the lysozyme story so far. Trends in Biochemical Sciences. 19(1). 31–37. 301 indexed citations
13.
Alexandrescu, Andrei T., Philip A. Evans, Maureen Pitkeathly, Jean Baum, & Christopher M. Dobson. (1993). Structure and dynamics of the acid-denatured molten globule state of .alpha.-lactalbumin: a two-dimensional NMR study. Biochemistry. 32(7). 1707–1718. 217 indexed citations
14.
Woolfson, Derek N., Philip A. Evans, E. Gail Hutchinson, & Janet M. Thornton. (1993). Topological and stereochemical restrictions in β-sandwich protein structures. Protein Engineering Design and Selection. 6(5). 461–470. 51 indexed citations
15.
Cox, J. P., Philip A. Evans, Leonard C. Packman, Dudley H. Williams, & Derek N. Woolfson. (1993). Dissecting the Structure of a Partially Folded Protein. Journal of Molecular Biology. 234(2). 483–492. 108 indexed citations
16.
Dobson, Christopher M., et al.. (1993). Structure and stability of the molten globule state of guinea pig .alpha.-lactalbumin: A hydrogen exchange study. Biochemistry. 32(21). 5681–5691. 158 indexed citations
17.
Woolfson, Derek N., Alan Cooper, Margaret M. Harding, Dudley H. Williams, & Philip A. Evans. (1993). Protein Folding in the Absence of the Solvent Ordering Contribution to the Hydrophobic Interaction. Journal of Molecular Biology. 229(2). 502–511. 56 indexed citations
18.
Radford, Sheena E., et al.. (1992). Hydrogen exchange in native and denatured states of hen egg‐white lysozyme. Proteins Structure Function and Bioinformatics. 14(2). 237–248. 144 indexed citations
19.
Evans, Philip A., et al.. (1991). Hydrophobic clustering in nonnative states of a protein: Interpretation of chemical shifts in NMR spectra of denatured states of lysozyme. Proteins Structure Function and Bioinformatics. 9(4). 248–266. 121 indexed citations
20.
Fox, Robert O., Philip A. Evans, & Christopher M. Dobson. (1986). Multiple conformations of a protein demonstrated by magnetization transfer NMR spectroscopy. Nature. 320(6058). 192–194. 94 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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