Richard Virden

1.5k total citations
53 papers, 1.3k citations indexed

About

Richard Virden is a scholar working on Molecular Biology, Materials Chemistry and Biotechnology. According to data from OpenAlex, Richard Virden has authored 53 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 42 papers in Molecular Biology, 12 papers in Materials Chemistry and 8 papers in Biotechnology. Recurrent topics in Richard Virden's work include Enzyme Structure and Function (12 papers), Protein Structure and Dynamics (8 papers) and Enzyme Production and Characterization (8 papers). Richard Virden is often cited by papers focused on Enzyme Structure and Function (12 papers), Protein Structure and Dynamics (8 papers) and Enzyme Production and Characterization (8 papers). Richard Virden collaborates with scholars based in United Kingdom, Slovenia and Spain. Richard Virden's co-authors include David C. Watts, Jeremy H. Lakey, Roger H. Pain, Harry J. Gilbert, Geoffrey P. Hazlewood, Simon J. Charnock, Enoch P. Baldwin, Jonathan P. Waltho, Neil A. Hughes and Adrian F. Bristow and has published in prestigious journals such as Nature, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Richard Virden

53 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Richard Virden United Kingdom 23 838 269 224 186 175 53 1.3k
J. Van Beeumen Belgium 19 811 1.0× 150 0.6× 90 0.4× 115 0.6× 64 0.4× 39 1.6k
Ronny Helland Norway 20 735 0.9× 263 1.0× 236 1.1× 164 0.9× 47 0.3× 39 1.2k
Valery Belakhov Israel 31 1.6k 1.9× 424 1.6× 341 1.5× 163 0.9× 110 0.6× 108 2.5k
Ohsuk Kwon South Korea 28 1.8k 2.2× 179 0.7× 234 1.0× 156 0.8× 74 0.4× 71 2.4k
L. Chantalat France 16 805 1.0× 188 0.7× 46 0.2× 172 0.9× 46 0.3× 27 1.2k
Hiroko Tokunaga Japan 20 985 1.2× 215 0.8× 94 0.4× 240 1.3× 58 0.3× 84 1.3k
James F. Parsons United States 23 1.2k 1.4× 86 0.3× 81 0.4× 177 1.0× 79 0.5× 52 1.6k
Ichiro Matsumura United States 20 1.3k 1.6× 182 0.7× 157 0.7× 149 0.8× 48 0.3× 41 1.6k
Allan Matte Canada 31 1.9k 2.2× 236 0.9× 93 0.4× 679 3.7× 51 0.3× 64 2.6k
David H. Calhoun United States 22 1.0k 1.2× 118 0.4× 80 0.4× 238 1.3× 29 0.2× 50 1.5k

Countries citing papers authored by Richard Virden

Since Specialization
Citations

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

Fields of papers citing papers by Richard Virden

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Richard Virden. 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 Richard Virden. The network helps show where Richard Virden may publish in the future.

Co-authorship network of co-authors of Richard Virden

This figure shows the co-authorship network connecting the top 25 collaborators of Richard Virden. A scholar is included among the top collaborators of Richard Virden 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 Richard Virden. Richard Virden 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.
Anderluh, Gregor, Qi Hong, Ruth Boetzel, et al.. (2003). Concerted Folding and Binding of a Flexible Colicin Domain to Its Periplasmic Receptor TolA. Journal of Biological Chemistry. 278(24). 21860–21868. 25 indexed citations
2.
Morillas, Manuel, Colin E. McVey, J.A. Brannigan, et al.. (2003). Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding. Biochemical Journal. 371(1). 143–150. 17 indexed citations
3.
Gökçe, İ̇sa, et al.. (2000). The TolA-recognition Site of Colicin N. ITC, SPR and Stopped-flow Fluorescence Define a Crucial 27-residue Segment. Journal of Molecular Biology. 304(4). 621–632. 39 indexed citations
4.
Virden, Richard, et al.. (1999). Differences in the effects of TFE on the folding pathways of human stefins A and B. Proteins Structure Function and Bioinformatics. 36(2). 205–216. 26 indexed citations
5.
Žerovnik, Eva, Richard Virden, Roman Jerala, Vito Türk, & Jonathan P. Waltho. (1998). On the mechanism of human stefin B folding: I. Comparison to homologous stefin A. Influence of pH and trifluoroethanol on the fast and slow folding phases. Proteins Structure Function and Bioinformatics. 32(3). 296–303. 1 indexed citations
6.
Charnock, Simon J., Tracey D. Spurway, Hefang Xie, et al.. (1998). The Topology of the Substrate Binding Clefts of Glycosyl Hydrolase Family 10 Xylanases Are Not Conserved. Journal of Biological Chemistry. 273(48). 32187–32199. 99 indexed citations
7.
Žerovnik, Eva, et al.. (1998). On the mechanism of human stefin B folding: II. Folding from GuHCl unfolded, TFE denatured, acid denatured, and acid intermediate states. Proteins Structure Function and Bioinformatics. 32(3). 304–313. 18 indexed citations
8.
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
9.
Charnock, Simon J., Jeremy H. Lakey, Richard Virden, et al.. (1997). Key Residues in Subsite F Play a Critical Role in the Activity of Pseudomonas fluorescens Subspecies cellulosa Xylanase A Against Xylooligosaccharides but Not Against Highly Polymeric Substrates such as Xylan. Journal of Biological Chemistry. 272(5). 2942–2951. 71 indexed citations
10.
Roa, Ana, et al.. (1995). New Insights on the Specificity of Penicillin Acylase. Biochemical and Biophysical Research Communications. 206(2). 629–636. 14 indexed citations
11.
Poole, Debbie M., Geoffrey P. Hazlewood, N. S. Huskisson, Richard Virden, & Harry J. Gilbert. (1993). The role of conserved tryptophan residues in the interaction of a bacterial cellulose binding domain with its ligand. FEMS Microbiology Letters. 106(1). 77–83. 71 indexed citations
12.
Monnaie, Didier, Richard Virden, & Jean‐Marie Frère. (1992). A rapid‐kinetic study of the class C β‐lactamase of Enterobacter cloacae 908R. FEBS Letters. 306(2-3). 108–112. 21 indexed citations
13.
Slade, Andrew, et al.. (1991). Site‐directed chemical conversion of serine to cysteine in penicillin acylase from Escherichia coli ATCC 11105. European Journal of Biochemistry. 197(1). 75–80. 32 indexed citations
14.
Virden, Richard, Anthony K. Tan, & Anthony L. Fink. (1990). Cryoenzymology of staphylococcal .beta.-lactamase: trapping a serine-70-linked acyl-enzyme. Biochemistry. 29(1). 145–153. 25 indexed citations
15.
Burchill, Susan A., Richard Virden, & A. J. Thody. (1989). Regulation of Tyrosinase Synthesis and its Processing in the Hair Follicular Melanocytes of the Mouse During Eumelanogenesis and Phaeomelanogenesis. Journal of Investigative Dermatology. 93(2). 236–240. 32 indexed citations
16.
Burchill, Susan A., Richard Virden, Bryan B. Fuller, & A. J. Thody. (1988). Regulation of tyrosinase synthesis by α-melanocyte-stimulating hormone in hair follicular melanocytes of the mouse. Journal of Endocrinology. 116(1). 17–23. 25 indexed citations
17.
Carrey, Elizabeth A., Richard Virden, & Roger H. Pain. (1984). The reversible deactivation of β-lactamase from Staphylococcus aureus by quinacillin and cephaloridine and its modification by antibodies. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 785(3). 104–110. 14 indexed citations
18.
Augusti, K T, M E Benaim, H. A. Dewar, & Richard Virden. (1975). Partial identification of the fibrinolytic activators in onion. Atherosclerosis. 21(3). 409–416. 17 indexed citations
19.
Virden, Richard, et al.. (1966). Adenosine 5′-triphosphate-arginine phosphotransferase from lobster muscle. Molecular weight. Biochemical Journal. 99(1). 155–158. 16 indexed citations
20.
Virden, Richard, David C. Watts, & Enoch P. Baldwin. (1965). ADENOSINE 5′-TRIPHOSPHATE-ARGININE PHOSPHOTRANSFERASE FROM LOBSTER MUSCLE: PURIFICATION AND PROPERTIES. Biochemical Journal. 94(3). 536–544. 66 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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