Simon Daff

2.9k total citations
58 papers, 2.4k citations indexed

About

Simon Daff is a scholar working on Physiology, Molecular Biology and Inorganic Chemistry. According to data from OpenAlex, Simon Daff has authored 58 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 27 papers in Physiology, 26 papers in Molecular Biology and 14 papers in Inorganic Chemistry. Recurrent topics in Simon Daff's work include Nitric Oxide and Endothelin Effects (27 papers), Metal-Catalyzed Oxygenation Mechanisms (14 papers) and Photosynthetic Processes and Mechanisms (13 papers). Simon Daff is often cited by papers focused on Nitric Oxide and Endothelin Effects (27 papers), Metal-Catalyzed Oxygenation Mechanisms (14 papers) and Photosynthetic Processes and Mechanisms (13 papers). Simon Daff collaborates with scholars based in United Kingdom, Japan and United States. Simon Daff's co-authors include Stephen K. Chapman, Andrew W. Munro, Ikuko Sagami, Tôru Shimizu, Tobias W. B. Ost, Caroline S. Miles, Gillian Reid, Michael A. Noble, D.A. Lysek and Christopher Page and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Simon Daff

57 papers receiving 2.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Simon Daff United Kingdom 27 1.2k 812 719 516 358 58 2.4k
Ryu Makino Japan 30 1.3k 1.1× 422 0.5× 500 0.7× 629 1.2× 768 2.1× 58 2.5k
Richard J. Kulmacz United States 38 1.5k 1.3× 707 0.9× 701 1.0× 514 1.0× 161 0.4× 114 4.7k
N R Orme-Johnson United States 26 1.2k 1.0× 238 0.3× 249 0.3× 157 0.3× 219 0.6× 36 2.2k
Shingo Nagano Japan 28 1.1k 0.9× 131 0.2× 635 0.9× 764 1.5× 406 1.1× 55 2.3k
Toshìo Yamano Japan 29 1.4k 1.2× 189 0.2× 706 1.0× 103 0.2× 278 0.8× 155 2.6k
Kerry T. Yasunobu United States 35 2.6k 2.2× 320 0.4× 194 0.3× 313 0.6× 559 1.6× 123 3.7k
Tohru Fukuyama Japan 52 2.2k 1.9× 387 0.5× 760 1.1× 440 0.9× 196 0.5× 210 7.7k
Huiying Li China 23 633 0.5× 872 1.1× 126 0.2× 255 0.5× 177 0.5× 81 1.9k
Rosemary Paschke United States 9 979 0.8× 213 0.3× 344 0.5× 126 0.2× 103 0.3× 10 1.5k
Thomas M. Shea United States 11 537 0.5× 325 0.4× 273 0.4× 123 0.2× 125 0.3× 16 1.1k

Countries citing papers authored by Simon Daff

Since Specialization
Citations

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

Fields of papers citing papers by Simon Daff

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Simon Daff

This figure shows the co-authorship network connecting the top 25 collaborators of Simon Daff. A scholar is included among the top collaborators of Simon Daff 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 Simon Daff. Simon Daff 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.
Ost, Tobias W. B., Sidong Liu, & Simon Daff. (2011). Cytochrome P450 BM3, NO binding and real-time NO detection. Nitric Oxide. 25(2). 89–94. 2 indexed citations
2.
Collison, David, Simon Daff, Nicola Austin, et al.. (2011). An in situ electrochemical cell for Q- and W-band EPR spectroscopy. Journal of Magnetic Resonance. 213(1). 206–209. 32 indexed citations
3.
Suckling, Colin J., et al.. (2010). Blocked dihydropteridines as nitric oxide synthase activators. Pteridines. 20. 27–35. 1 indexed citations
4.
Daff, Simon. (2010). NO synthase: Structures and mechanisms. Nitric Oxide. 23(1). 1–11. 192 indexed citations
5.
Daff, Simon, et al.. (2010). Conformation‐dependent hydride transfer in neuronal nitric oxide synthase reductase domain. FEBS Journal. 277(18). 3833–3834. 19 indexed citations
6.
Suckling, Colin J., et al.. (2008). 6-Acetyl-7,7-dimethyl-5,6,7,8-tetrahydropterin is an activator of nitric oxide synthases. Bioorganic & Medicinal Chemistry Letters. 18(5). 1563–1566. 21 indexed citations
7.
Miles, Caroline S., Christopher G. Mowat, Malcolm D. Walkinshaw, et al.. (2006). The role of Thr268 and Phe393 in cytochrome P450 BM3. Journal of Inorganic Biochemistry. 100(5-6). 1075–1090. 56 indexed citations
8.
Munro, Andrew W., David Leys, Kirsty J. McLean, et al.. (2002). P450 BM3: the very model of a modern flavocytochrome. Trends in Biochemical Sciences. 27(5). 250–257. 364 indexed citations
9.
Chapman, Stephen K., et al.. (2002). Calmodulin Activates Electron Transfer through Neuronal Nitric-oxide Synthase Reductase Domain by Releasing an NADPH-dependent Conformational Lock. Journal of Biological Chemistry. 277(37). 33987–33994. 84 indexed citations
10.
Noguchi, Tomoko, Ikuko Sagami, Simon Daff, & Tôru Shimizu. (2001). Important Role of Tetrahydrobiopterin in NO Complex Formation and Interdomain Electron Transfer in Neuronal Nitric-Oxide Synthase. Biochemical and Biophysical Research Communications. 282(5). 1092–1097. 10 indexed citations
11.
Talfournier, François, Andrew W. Munro, Jaswir Basran, et al.. (2001). αArg-237 in Methylophilus methylotrophus (sp. W3A1) Electron-transferring Flavoprotein Affords ∼200-Millivolt Stabilization of the FAD Anionic Semiquinone and a Kinetic Block on Full Reduction to the Dihydroquinone. Journal of Biological Chemistry. 276(23). 20190–20196. 33 indexed citations
12.
Kobayashi, Kazuo, Seiichi Tagawa, Simon Daff, Ikuko Sagami, & Tôru Shimizu. (2001). Rapid Calmodulin-dependent Interdomain Electron Transfer in Neuronal Nitric-oxide Synthase Measured by Pulse Radiolysis. Journal of Biological Chemistry. 276(43). 39864–39871. 38 indexed citations
13.
Daff, Simon, Matt Noble, Stuart L. Rivers, et al.. (2001). Control of electron transfer in neuronal NO synthase. Biochemical Society Transactions. 29(2). 147–147. 33 indexed citations
14.
Sagami, Ikuko, et al.. (2000). Azo Reduction of Methyl Red by Neuronal Nitric Oxide Synthase: The Important Role of FMN in Catalysis. Biochemical and Biophysical Research Communications. 275(3). 752–758. 15 indexed citations
15.
Sagami, Ikuko, Yuko Sato, Simon Daff, & Tôru Shimizu. (2000). Aromatic Residues and Neighboring Arg414 in the (6R)-5,6,7,8-Tetrahydro-l-Biopterin Binding Site of Full-length Neuronal Nitric-oxide Synthase Are Crucial in Catalysis and Heme Reduction with NADPH. Journal of Biological Chemistry. 275(34). 26150–26157. 23 indexed citations
16.
Sagami, Ikuko, et al.. (2000). Roles of the heme proximal side residues tryptophan409 and tryptophan421 of neuronal nitric oxide synthase in the electron transfer reaction. Journal of Inorganic Biochemistry. 82(1-4). 163–170. 12 indexed citations
17.
Daff, Simon, Ikuko Sagami, & Tôru Shimizu. (1999). The 42-Amino Acid Insert in the FMN Domain of Neuronal Nitric-oxide Synthase Exerts Control over Ca2+/Calmodulin-dependent Electron Transfer. Journal of Biological Chemistry. 274(43). 30589–30595. 110 indexed citations
18.
Campopiano, Dominic J., et al.. (1998). Characterisation of flavodoxin NADP+ oxidoreductase and flavodoxin; key components of electron transfer in Escherichia coli. European Journal of Biochemistry. 257(3). 577–585. 88 indexed citations
19.
Reid, Gillian, et al.. (1996). Flavocytochrome b2: an ideal model system for studying protein-mediated electron transfer. Biochemical Society Transactions. 24(1). 73–77. 7 indexed citations
20.
Munro, Andrew W., Simon Daff, John R. Coggins, J. Gordon Lindsay, & Stephen K. Chapman. (1996). Probing Electron Transfer in Flavocytochrome P‐450 BM3 and Its Component Domains. European Journal of Biochemistry. 239(2). 403–409. 103 indexed citations

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