S. P. Wood

1.7k total citations
45 papers, 1.4k citations indexed

About

S. P. Wood is a scholar working on Molecular Biology, Materials Chemistry and Biotechnology. According to data from OpenAlex, S. P. Wood has authored 45 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 35 papers in Molecular Biology, 20 papers in Materials Chemistry and 7 papers in Biotechnology. Recurrent topics in S. P. Wood's work include Enzyme Structure and Function (19 papers), Protein Structure and Dynamics (8 papers) and Porphyrin Metabolism and Disorders (7 papers). S. P. Wood is often cited by papers focused on Enzyme Structure and Function (19 papers), Protein Structure and Dynamics (8 papers) and Porphyrin Metabolism and Disorders (7 papers). S. P. Wood collaborates with scholars based in United Kingdom, United States and Germany. S. P. Wood's co-authors include Ian J. Tickle, T.L. Blundell, J.B. Cooper, T.L. Blundell, Tom L. Blundell, Axel Wollmer, Robin Püllen, T. Blundell, Jørgen Gliemann and Steen Gammeltoft and has published in prestigious journals such as Nature, Annual Review of Biochemistry and Journal of Molecular Biology.

In The Last Decade

S. P. Wood

45 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
S. P. Wood United Kingdom	17	1.1k	235	147	139	121	45	1.4k
J.F. Cutfield New Zealand	22	1.2k 1.1×	299 1.3×	307 2.1×	221 1.6×	97 0.8×	36	1.8k
T.L. Blundell United Kingdom	21	1.3k 1.3×	305 1.3×	194 1.3×	307 2.2×	304 2.5×	30	1.8k
Charles A. Collyer Australia	24	915 0.9×	338 1.4×	176 1.2×	242 1.7×	50 0.4×	57	1.8k
Albert Light United States	20	835 0.8×	82 0.3×	70 0.5×	74 0.5×	159 1.3×	47	1.3k
Glynn Im United Kingdom	6	1.6k 1.5×	115 0.5×	124 0.8×	62 0.4×	117 1.0×	17	1.9k
Gregory D. Reinhart United States	25	1.6k 1.5×	463 2.0×	254 1.7×	161 1.2×	64 0.5×	75	2.0k
Judith Rittenhouse United States	17	653 0.6×	143 0.6×	88 0.6×	85 0.6×	61 0.5×	24	1.2k
Toshihide Okajima Japan	29	1.7k 1.6×	175 0.7×	30 0.2×	160 1.2×	91 0.8×	91	2.3k
Pirkko Heikinheimo Finland	18	866 0.8×	285 1.2×	69 0.5×	76 0.5×	21 0.2×	34	1.2k
John S. McKinley-McKee Norway	23	1.0k 1.0×	198 0.8×	116 0.8×	193 1.4×	100 0.8×	67	1.5k

Countries citing papers authored by S. P. Wood

Since Specialization

Citations

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

Fields of papers citing papers by S. P. Wood

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by S. P. Wood. 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 S. P. Wood. The network helps show where S. P. Wood may publish in the future.

Co-authorship network of co-authors of S. P. Wood

This figure shows the co-authorship network connecting the top 25 collaborators of S. P. Wood. A scholar is included among the top collaborators of S. P. Wood 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 S. P. Wood. S. P. Wood is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Guo, Jingxu, P.T. Erskine, Alun R. Coker, et al.. (2015). Extension of resolution and oligomerization-state studies of 2,4′-dihydroxyacetophenone dioxygenase fromAlcaligenessp. 4HAP. Acta Crystallographica Section F Structural Biology Communications. 71(10). 1258–1263. 4 indexed citations

Keegan, Ronan M., P.T. Erskine, Jingxu Guo, et al.. (2014). Structure of the 2,4′-dihydroxyacetophenone dioxygenase fromAlcaligenessp. 4HAP. Acta Crystallographica Section D Biological Crystallography. 70(9). 2444–2454. 13 indexed citations

Bailey, David, Elisabeth P. Carpenter, Alun R. Coker, et al.. (2012). An analysis of subdomain orientation, conformational change and disorder in relation to crystal packing of aspartic proteinases. Acta Crystallographica Section D Biological Crystallography. 68(5). 541–552. 5 indexed citations

Roberts, April K., Raj Gill, Halina Mikolajek, et al.. (2012). Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase fromArabidopsis thaliana. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68(12). 1491–1493. 3 indexed citations

Knight, Mark, Halina Mikolajek, P.T. Erskine, et al.. (2006). Crystallization and preliminary X-ray diffraction analysis of BipD, a virulence factor fromBurkholderia pseudomallei. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62(8). 761–764. 6 indexed citations

Coates, Leighton, P.T. Erskine, Samuel I. Beale, et al.. (2005). Structure ofChlorobium vibrioforme5-aminolaevulinic acid dehydratase complexed with a diacid inhibitor. Acta Crystallographica Section D Biological Crystallography. 61(12). 1594–1598. 9 indexed citations

Aguilar, C. F., Nora Cronin, M. Badasso, et al.. (1997). The three-dimensional structure at 2.4 Å resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae. Journal of Molecular Biology. 267(4). 899–915. 29 indexed citations

Louie, Gordon V., Richard Lambert, J.B. Cooper, et al.. (1996). The three-dimensional structure ofEscherichia coliporphobilinogen deaminase at 1.76-Å resolution. Proteins Structure Function and Bioinformatics. 25(1). 48–78. 33 indexed citations

Aguilar, C. F., V. Dhanaraj, Kunchur Guruprasad, et al.. (1995). Comparisons of the Three-Dimensional Structures, Specificities and Glycosylation of Renins, Yeast Proteinase A and Cathepsin D. Advances in experimental medicine and biology. 362. 155–166. 6 indexed citations

10.

Jones, Arwyn T., et al.. (1995). Molecular Mass Determination by Electrospray Mass Spectrometry of Human Pepsins, Gastricsin, and Porcine Pepsin A Variants. Advances in experimental medicine and biology. 362. 83–89. 1 indexed citations

11.

Sowdhamini, Ramanathan, Narayanaswamy Srinivasan, Kunchur Guruprasad, et al.. (1995). Protein three-dimensional structure and molecular recognition: a story of soft locks and keys. Pharmaceutica Acta Helvetiae. 69(4). 185–192. 4 indexed citations

12.

Wood, S. P., Richard Lambert, Tom L. Blundell, et al.. (1994). The three‐dimensional structures of mutants of porphobilinogen deaminase: Toward an understanding of the structural basis of acute intermittent porphyria. Protein Science. 3(10). 1644–1650. 60 indexed citations

13.

Badasso, M., S. P. Wood, C. F. Aguilar, et al.. (1993). Crystallization and Preliminary Crystallographic Characterization of Aspartic Proteinase-A from Baker's Yeast and Its Complexes with Inhibitors. Journal of Molecular Biology. 232(2). 701–703. 7 indexed citations

14.

Dhanaraj, V., Chris Dealwis, Carlos Frazão, et al.. (1992). X-ray analyses of peptide–inhibitor complexes define the structural basis of specificity for human and mouse renins. Nature. 357(6378). 466–472. 102 indexed citations

15.

Badasso, M., B. L. Sibanda, J.B. Cooper, Chris Dealwis, & S. P. Wood. (1992). Crystal quality and inhibitor binding by aspartic proteinases; preparation of high quality crystals of mouse renin. Journal of Crystal Growth. 122(1-4). 393–399. 3 indexed citations

16.

Blundell, T.L., Sharon J. Cooper, Jim E. Pitts, et al.. (1990). The conformation of deamino-oxytocin: X-ray analysis of the ‘dry’ and ‘wet’ forms. Philosophical transactions of the Royal Society of London. Series B, Biological sciences. 327(1243). 625–654. 10 indexed citations

17.

Blundell, Tom L., John A. Jenkins, B.T. Sewell, et al.. (1990). X-ray analyses of aspartic proteinases. Journal of Molecular Biology. 211(4). 919–941. 90 indexed citations

18.

Foundling, S. I., J.B. Cooper, Laurence H. Pearl, et al.. (1987). Crystallographic Studies of Reduced Bond Inhibitors Complexed with an Aspartic Proteinase. Journal of Cardiovascular Pharmacology. 10. 59–68. 5 indexed citations

19.

Blundell, T. & S. P. Wood. (1982). The Conformation, Flexibility, and Dynamics of Polypeptide Hormones. Annual Review of Biochemistry. 51(1). 123–154. 70 indexed citations

20.

Bedarkar, S., et al.. (1978). Polypeptide Hormone‐Receptor Interactions: The Structure and Receptor Binding of Insulin and Glucagon. Novartis Foundation symposium. 105–121. 2 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.

Explore authors with similar magnitude of impact