Stephen P. Wood

2.4k total citations
32 papers, 1.3k citations indexed

About

Stephen P. Wood is a scholar working on Molecular Biology, Materials Chemistry and Physiology. According to data from OpenAlex, Stephen P. Wood has authored 32 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Molecular Biology, 10 papers in Materials Chemistry and 4 papers in Physiology. Recurrent topics in Stephen P. Wood's work include Enzyme Structure and Function (9 papers), Protein Structure and Dynamics (7 papers) and Porphyrin Metabolism and Disorders (4 papers). Stephen P. Wood is often cited by papers focused on Enzyme Structure and Function (9 papers), Protein Structure and Dynamics (7 papers) and Porphyrin Metabolism and Disorders (4 papers). Stephen P. Wood collaborates with scholars based in United Kingdom, United States and Italy. Stephen P. Wood's co-authors include Peter M. Shoolingin‐Jordan, T.L. Blundell, Jon Cooper, Martin J. Warren, Shaoxia Chen, Helen R. Saibil, Anthony R. Clarke, Alan M. Roseman, Neil A. Ranson and Axel Wollmer and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Molecular Biology.

In The Last Decade

Stephen P. Wood

29 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Stephen P. Wood United Kingdom 19 946 342 150 98 97 32 1.3k
Jason G. McCoy United States 23 1.1k 1.1× 173 0.5× 124 0.8× 40 0.4× 98 1.0× 41 1.6k
Klaus Klarskov Canada 20 537 0.6× 167 0.5× 46 0.3× 99 1.0× 92 0.9× 56 1.2k
Dean A. Malencik United States 24 1.2k 1.3× 174 0.5× 250 1.7× 65 0.7× 224 2.3× 57 1.9k
William J. Steele United States 25 1.3k 1.4× 101 0.3× 116 0.8× 38 0.4× 139 1.4× 75 1.9k
Lijuan Liu China 22 473 0.5× 165 0.5× 102 0.7× 47 0.5× 77 0.8× 47 1.4k
Ronald S. Kaplan United States 25 1.4k 1.5× 131 0.4× 122 0.8× 35 0.4× 146 1.5× 46 1.8k
Roy A. Johanson United States 17 793 0.8× 120 0.4× 94 0.6× 30 0.3× 178 1.8× 30 1.1k
Denis V. Titov United States 17 1.3k 1.3× 94 0.3× 70 0.5× 67 0.7× 83 0.9× 27 1.7k
Masatoshi Murai Japan 26 1.4k 1.4× 71 0.2× 235 1.6× 83 0.8× 73 0.8× 91 2.1k

Countries citing papers authored by Stephen P. Wood

Since Specialization
Citations

This map shows the geographic impact of Stephen 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 Stephen 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 Stephen P. Wood more than expected).

Fields of papers citing papers by Stephen P. Wood

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

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

This figure shows the co-authorship network connecting the top 25 collaborators of Stephen P. Wood. A scholar is included among the top collaborators of Stephen 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 Stephen P. Wood. Stephen P. Wood 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.
Tadesse, Girmaw Abebe, et al.. (2024). Weak Labeling for Cropland Mapping in Africa. 258–262.
2.
Kolstoe, Simon, A. C. Purvis, Mark E. Light, et al.. (2014). Interaction of serum amyloid P component with hexanoyl bis(D-proline) (CPHPC). Acta Crystallographica Section D Biological Crystallography. 70(8). 2232–2240. 11 indexed citations
3.
Wood, Stephen P., et al.. (2012). The Potential Regulatory Challenges of Increasingly Autonomous Motor Vehicles. Santa Clara law review. 52(4). 1423. 26 indexed citations
4.
Wood, Stephen P.. (2012). Vaccination Programs among Urban Homeless Populations: A Literature Review. Journal of Vaccines & Vaccination. 3(6). 3 indexed citations
5.
Wood, Stephen P., et al.. (2011). Morphological Differences between β2‐Microglobulin in Fibrils and Inclusion Bodies. ChemBioChem. 12(4). 556–558. 2 indexed citations
6.
Mikolajek, Halina, Simon Kolstoe, Valerie E. Pye, et al.. (2011). Structural basis of ligand specificity in the human pentraxins, C‐reactive protein and serum amyloid P component. Journal of Molecular Recognition. 24(2). 371–377. 34 indexed citations
7.
8.
Wood, Stephen P., et al.. (2007). Caustic Gouging in a Refinery Boiler – Root Cause and Remediation. 1–13. 1 indexed citations
9.
Gill, Raj, Fiyaz Mohammed, Leighton Coates, et al.. (2005). High-resolution structure ofmyo-inositol monophosphatase, the putative target of lithium therapy. Acta Crystallographica Section D Biological Crystallography. 61(5). 545–555. 43 indexed citations
10.
Li, Chen, et al.. (2004). Catalytic Mechanism of C–C Hydrolase MhpC from Escherichia coli: Kinetic Analysis of His263 and Ser110 Site-directed Mutants. Journal of Molecular Biology. 346(1). 241–251. 31 indexed citations
11.
12.
Chen, Shaoxia, Alan M. Roseman, Stephen P. Wood, et al.. (1994). Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy. Nature. 371(6494). 261–264. 284 indexed citations
13.
Price, Nicholas C., et al.. (1993). The unfolding and attempted refolding of the bacterial chaperone protein groEL (cpn60). Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1161(1). 52–58. 29 indexed citations
14.
Hädener, Alfons, V.N. Malashkevich, Gordon V. Louie, et al.. (1993). Purification, characterization, crystallisation and X‐ray analysis of selenomethionine‐labelled hydroxymethylbilane synthase from Escherichia coli. European Journal of Biochemistry. 211(3). 615–624. 30 indexed citations
15.
Price, Nicholas C., et al.. (1991). The aromatic amino acid content of the bacterial chaperone protein groEL (cpn60) Evidence for the presence of a single tryptophan. FEBS Letters. 292(1-2). 9–12. 10 indexed citations
16.
Hemmings, Andrew M., Stephen I. Foundling, B. L. Sibanda, et al.. (1985). Energy calculations on aspartic proteinases: human renin, endothiapepsin and its complex with an angiotensinogen fragment analogue, H-142. Biochemical Society Transactions. 13(6). 1036–1041. 13 indexed citations
17.
Glover, I. D., David J. Barlow, Stephen P. Wood, et al.. (1984). Conformational studies on the pancreatic polypeptide hormone family. European Journal of Biochemistry. 142(2). 379–385. 138 indexed citations
18.
Bajaj‐Elliott, Mona, T.L. Blundell, Stephen P. Wood, et al.. (1983). Dogfish insulin. European Journal of Biochemistry. 135(3). 535–542. 43 indexed citations
19.
Blundell, T.L., et al.. (1982). The Conformation and Molecular Biology of Pancreatic Hormones and Homologous Growth Factor. PubMed. 13(2). 141–213. 12 indexed citations
20.
Wood, Stephen P., et al.. (1975). The Relation of Conformation and Association of Insulin to Receptor Binding; X‐Ray and Circular‐Dichroism Studies on Bovine and Hystricomorph Insulins. European Journal of Biochemistry. 55(3). 531–542. 98 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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