Scott A. White

3.2k total citations
81 papers, 2.5k citations indexed

About

Scott A. White is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, Scott A. White has authored 81 papers receiving a total of 2.5k indexed citations (citations by other indexed papers that have themselves been cited), including 47 papers in Molecular Biology, 29 papers in Materials Chemistry and 9 papers in Genetics. Recurrent topics in Scott A. White's work include Enzyme Structure and Function (22 papers), ATP Synthase and ATPases Research (18 papers) and Photosynthetic Processes and Mechanisms (10 papers). Scott A. White is often cited by papers focused on Enzyme Structure and Function (22 papers), ATP Synthase and ATPases Research (18 papers) and Photosynthetic Processes and Mechanisms (10 papers). Scott A. White collaborates with scholars based in United Kingdom, United States and France. Scott A. White's co-authors include Andrew L. Lovering, Peter F. Searle, J. Baz Jackson, Eva I. Hyde, F. Scott Mathews, Paul R. Race, Weiwen Dai, Zongxiang Xia, Jon P. Ride and Jane I. Grove and has published in prestigious journals such as Nucleic Acids Research, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

Scott A. White

78 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
Scott A. White United Kingdom 29 1.5k 606 239 238 222 81 2.5k
Esam A. Orabi Canada 36 1.9k 1.3× 372 0.6× 222 0.9× 550 2.3× 312 1.4× 138 3.7k
Yasuo Hata Japan 27 1.3k 0.8× 449 0.7× 157 0.7× 126 0.5× 303 1.4× 97 2.8k
Taro Tamada Japan 27 1.2k 0.8× 453 0.7× 72 0.3× 103 0.4× 172 0.8× 167 3.0k
Michael K. Johnson United States 26 1.1k 0.7× 490 0.8× 90 0.4× 145 0.6× 165 0.7× 45 2.8k
Fabio Tanfani Italy 28 1.3k 0.9× 547 0.9× 71 0.3× 139 0.6× 324 1.5× 117 2.8k
Vladimir O. Popov Russia 27 2.2k 1.5× 1.0k 1.7× 646 2.7× 148 0.6× 191 0.9× 269 3.6k
Rolandas Meškys Lithuania 25 1.2k 0.8× 215 0.4× 140 0.6× 56 0.2× 130 0.6× 160 2.5k
Xiao‐Feng Guo China 31 968 0.6× 1.1k 1.9× 402 1.7× 56 0.2× 169 0.8× 132 3.1k
E.J. Levin Canada 25 1.1k 0.7× 248 0.4× 158 0.7× 148 0.6× 235 1.1× 50 2.3k
Michael F. Rohde United States 33 1.4k 1.0× 298 0.5× 86 0.4× 342 1.4× 355 1.6× 86 3.1k

Countries citing papers authored by Scott A. White

Since Specialization
Citations

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

Fields of papers citing papers by Scott A. White

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Scott A. White

This figure shows the co-authorship network connecting the top 25 collaborators of Scott A. White. A scholar is included among the top collaborators of Scott A. White 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 Scott A. White. Scott A. White 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.
Christofferson, Andrew J., J. L. Ross Anderson, A. Evans, et al.. (2023). Structure and Dynamics of Three Escherichia coli NfsB Nitro-Reductase Mutants Selected for Enhanced Activity with the Cancer Prodrug CB1954. International Journal of Molecular Sciences. 24(6). 5987–5987. 2 indexed citations
2.
White, Scott A., et al.. (2022). The 3D‐structure, kinetics and dynamics of the E. coli nitroreductase NfsA with NADP+ provide glimpses of its catalytic mechanism. FEBS Letters. 596(18). 2425–2440. 11 indexed citations
3.
Ilias, Mohammad, Scott A. White, & Tom Young. (2011). Isoleucine 259 and isoleucine 260 residues in Streptococcus gordonii soluble inorganic pyrophosphatase play an important role in enzyme activity. Journal of Bioscience and Bioengineering. 112(1). 8–13. 3 indexed citations
4.
Shukla, Anshuman, Mark J. Pallen, Mark Anthony, & Scott A. White. (2010). The homodimeric GBS1074 fromStreptococcus agalactiae. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66(11). 1421–1425. 14 indexed citations
5.
Quirk, Philip G., et al.. (2010). The specificity of proton-translocating transhydrogenase for nicotinamide nucleotides. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1807(1). 85–94. 9 indexed citations
6.
Tame, Jeremy R. H., Gordon A. Morris, Christopher W. Wharton, et al.. (2010). Order and Disorder in the Domain Organization of the Plasmid Partition Protein KorB. Journal of Biological Chemistry. 285(20). 15440–15449. 11 indexed citations
7.
White, Scott A., Loı̈c Briand, David J. Scott, & Antoni J. Borysik. (2009). Structure of rat odorant-binding protein OBP1 at 1.6 Å resolution. Acta Crystallographica Section D Biological Crystallography. 65(5). 403–410. 18 indexed citations
8.
Ugochukwu, E., Andrew L. Lovering, O.C. Mather, Thomas W. Young, & Scott A. White. (2007). The Crystal Structure of the Cytosolic Exopolyphosphatase from Saccharomyces cerevisiae Reveals the Basis for Substrate Specificity. Journal of Molecular Biology. 371(4). 1007–1021. 31 indexed citations
9.
Ugochukwu, E., et al.. (2007). Kinetic and Mutational Analyses of the Major Cytosolic Exopolyphosphatase from Saccharomyces cerevisiae. Journal of Biological Chemistry. 282(13). 9302–9311. 20 indexed citations
10.
Munro, Catherine A., et al.. (2005). ‘Aquilla'—a premium quality facultative bread wheat ( Triticum aestivum ). New Zealand Journal of Crop and Horticultural Science. 33(3). 219–222.
11.
Grove, Jane I., Andrew L. Lovering, Christopher P. Guise, et al.. (2003). Generation of Escherichia coli nitroreductase mutants conferring improved cell sensitization to the prodrug CB1954.. University of Birmingham Research Portal (University of Birmingham). 63(17). 5532–7. 60 indexed citations
12.
13.
Jackson, J. Baz, et al.. (2000). The NADP(H)-binding component (dIII) of human heart transhydrogenase: crystallization and preliminary crystallographic analysis. Acta Crystallographica Section D Biological Crystallography. 56(4). 489–491. 2 indexed citations
14.
15.
16.
Thompson, Thomas L., et al.. (1999). Developing Sap Nitrate Tests for Durum Wheat and Barley, Maricopa, 1999. UA Campus Repository (The University of Arizona). 1 indexed citations
17.
Thompson, Thomas L., et al.. (1998). Late Season Tissue Tests for Critical Grain Protein Content in Durum, Maricopa, 1998. UA Campus Repository (The University of Arizona). 2 indexed citations
18.
Wang, Maggie Haitian, David Wade, Li‐Song Chen, Scott A. White, & Chung S. Yang. (1995). Probing the Active Sites of Rat and Human Cytochrome-P450 2E1 with Alcohols and Carboxylic Acids. Archives of Biochemistry and Biophysics. 317(1). 299–304. 34 indexed citations
19.
Tegoni, M., Scott A. White, Alain Roussel, F. Scott Mathews, & Christian Cambillau. (1993). A hypothetical complex between crystalline flavocytochrome b2 and Cytochrome c. Proteins Structure Function and Bioinformatics. 16(4). 408–422. 18 indexed citations
20.
Reid, Gillian, Scott A. White, Michael T. Black, et al.. (1988). Probing the active site of flavocytochrome b2 by site‐directed mutagenesis. European Journal of Biochemistry. 178(2). 329–333. 39 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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