Roger H. Pain

5.0k total citations · 1 hit paper
122 papers, 4.3k citations indexed

About

Roger H. Pain is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, Roger H. Pain has authored 122 papers receiving a total of 4.3k indexed citations (citations by other indexed papers that have themselves been cited), including 91 papers in Molecular Biology, 35 papers in Materials Chemistry and 12 papers in Spectroscopy. Recurrent topics in Roger H. Pain's work include Protein Structure and Dynamics (47 papers), Enzyme Structure and Function (33 papers) and Biochemical and Structural Characterization (14 papers). Roger H. Pain is often cited by papers focused on Protein Structure and Dynamics (47 papers), Enzyme Structure and Function (33 papers) and Biochemical and Structural Characterization (14 papers). Roger H. Pain collaborates with scholars based in United Kingdom, Slovenia and Belgium. Roger H. Pain's co-authors include Barry Robson, Oleg B. Ptitsyn, Gennady V. Semisotnov, Eva Žerovnik, Hans E. M. Christensen, Stewart Craig, Paul T. Wingfield, Valentina E. Bychkova, Paul Varley and Adrian Allen and has published in prestigious journals such as Nature, Science and Journal of Biological Chemistry.

In The Last Decade

Roger H. Pain

119 papers receiving 4.0k citations

Hit Papers

Evidence for a molten globule state as a general intermed... 1990 2026 2002 2014 1990 200 400 600
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. Evidence for a molten globule state as a general intermediate in protein folding
    1990 606 citations Oleg B. Ptitsyn, Roger H. Pain et al. FEBS Letters profile →

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Roger H. Pain United Kingdom 35 3.3k 1.3k 449 346 345 122 4.3k
Narasimha Sreerama United States 20 4.8k 1.5× 1.0k 0.8× 500 1.1× 329 1.0× 418 1.2× 32 6.6k
Lee Whitmore United Kingdom 13 3.5k 1.1× 638 0.5× 344 0.8× 263 0.8× 451 1.3× 21 5.3k
A. D’Arcy Switzerland 41 4.0k 1.2× 958 0.7× 311 0.7× 832 2.4× 94 0.3× 61 7.0k
Dirk W. Heinz Germany 42 3.6k 1.1× 972 0.7× 522 1.2× 305 0.9× 364 1.1× 101 5.3k
Gerald R. Grimsley United States 24 5.5k 1.7× 1.6k 1.2× 592 1.3× 374 1.1× 276 0.8× 31 7.3k
Se Won Suh South Korea 40 4.2k 1.3× 906 0.7× 287 0.6× 317 0.9× 142 0.4× 196 5.7k
Katsuhide Yutani Japan 41 3.8k 1.2× 2.1k 1.6× 370 0.8× 112 0.3× 263 0.8× 154 4.5k
Taiji Imoto Japan 39 4.1k 1.3× 1.5k 1.2× 355 0.8× 549 1.6× 379 1.1× 238 6.0k
Christine Ebel France 41 3.6k 1.1× 795 0.6× 489 1.1× 356 1.0× 98 0.3× 154 5.2k
D.C. Phillips United Kingdom 20 2.1k 0.6× 1.3k 1.0× 242 0.5× 76 0.2× 276 0.8× 29 3.0k

Countries citing papers authored by Roger H. Pain

Since Specialization
Citations

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

Fields of papers citing papers by Roger H. Pain

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Roger H. Pain. 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 Roger H. Pain. The network helps show where Roger H. Pain may publish in the future.

Co-authorship network of co-authors of Roger H. Pain

This figure shows the co-authorship network connecting the top 25 collaborators of Roger H. Pain. A scholar is included among the top collaborators of Roger H. Pain 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 Roger H. Pain. Roger H. Pain 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.
Craig, Stewart, et al.. (2009). Determination of the contributions of individual aromatic residues to the CD spectrum of IL-lβ using site directed mutagenesis. International journal of peptide & protein research. 33(4). 256–262. 2 indexed citations
2.
Lejeune, Annabelle, Roger H. Pain, P. Charlier, Jean-Marie Frère, & André Matagne. (2008). TEM-1 β-Lactamase Folds in a Nonhierarchical Manner with Transient Non-Native Interactions Involving the C-Terminal Region. Biochemistry. 47(4). 1186–1193. 10 indexed citations
3.
Thomas, Richard M., et al.. (2004). Clitocypin, a new cysteine proteinase inhibitor, is monomeric: impact on the mechanism of folding. Biochemical and Biophysical Research Communications. 324(2). 576–578. 7 indexed citations
4.
Štrukelj, Borut, Kristina Gruden, Anka Ritonja, et al.. (2001). A basic residue at position 36p of the propeptide is not essential for the correct folding and subsequent autocatalytic activation of prochymosin. European Journal of Biochemistry. 268(8). 2362–2368. 7 indexed citations
5.
Cigić, Blaž & Roger H. Pain. (1999). Location of the binding site for chloride ion activation of cathepsin C. European Journal of Biochemistry. 264(3). 944–951. 60 indexed citations
6.
Hawkins, Alastair R., et al.. (1998). The slow step of folding ofStaphylococcus aureus PC1 β-lactamase involves the collapse of a surface loop rate limited by theTrans toCis isomerization of a non-proline peptide bond. Proteins Structure Function and Bioinformatics. 33(4). 550–557. 11 indexed citations
7.
Pain, Roger H.. (1996). Determining the Fluorescence Spectrum of a Protein. Current Protocols in Protein Science. 6(1). 3 indexed citations
8.
Pain, Roger H.. (1995). Overview of Protein Folding. Current Protocols in Protein Science. 0(1). Unit 6.4–Unit 6.4. 6 indexed citations
9.
Hlodan, Roman & Roger H. Pain. (1995). The Folding and Assembly Pathway of Tumour Necrosis Factor TNFalpha, a Globular Trimeric Protein. European Journal of Biochemistry. 231(2). 381–387. 23 indexed citations
10.
Varley, Paul & Roger H. Pain. (1991). Relation between stability, dynamics and enzyme activity in 3-phosphoglycerate kinases from yeast and Thermus thermophilus. Journal of Molecular Biology. 220(2). 531–538. 100 indexed citations
11.
Lindsay, Christopher & Roger H. Pain. (1990). The folding and solution conformation of penicillin G acylase. European Journal of Biochemistry. 192(1). 133–141. 47 indexed citations
12.
Ptitsyn, Oleg B., et al.. (1990). Evidence for a molten globule state as a general intermediate in protein folding. FEBS Letters. 262(1). 20–24. 606 indexed citations breakdown →
13.
Wingfield, Paul T., Pierre Graber, Peter Moonen, Stewart Craig, & Roger H. Pain. (1988). The conformation and stability of recombinant‐derived granulocyte‐macrophage colony stimulating factors. European Journal of Biochemistry. 173(1). 65–72. 47 indexed citations
14.
Thomas, Richard M., et al.. (1983). Identification by n.m.r. spectroscopy of a stable intermediate structure in the unfolding of staphylococcal β-lactamase. Biochemical Journal. 215(3). 525–529. 9 indexed citations
15.
Privat, Jean‐Paul, Philippe Wahl, Jean‐Claude Auchet, & Roger H. Pain. (1980). Time resolved spectroscgpy of tryptopkyl fluorescence of yeast 3-phosphoglycerate kinase. Biophysical Chemistry. 11(2). 239–248. 40 indexed citations
16.
17.
Jones, Peter, A. Suggett, & Roger H. Pain. (1968). Sub-unit Nature of Catalase Compound II. Nature. 217(5133). 1050–1050. 18 indexed citations
18.
Creeth, J. M. & Roger H. Pain. (1967). The determination of molecular weights of biological macromolecules by ultracentrifuge methods. Progress in Biophysics and Molecular Biology. 17. 217–287. 107 indexed citations
19.
Butler, John, Roger H. Pain, A. B. Robins, & Joseph Rotblat. (1958). The relative effects of direct and indirect actions of ionizing radiations on deoxyribonucleic acid. Proceedings of the Royal Society of London. Series B, Biological sciences. 149(934). 12–20. 8 indexed citations
20.
Pain, Roger H. & J. A. V. Butler. (1957). The preparation and properties of ribonucleic acids from rat liver. Biochemical Journal. 66(2). 299–302. 14 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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