Steven C. Shewry

524 total citations
10 papers, 383 citations indexed

About

Steven C. Shewry is a scholar working on Molecular Biology, Materials Chemistry and Nutrition and Dietetics. According to data from OpenAlex, Steven C. Shewry has authored 10 papers receiving a total of 383 indexed citations (citations by other indexed papers that have themselves been cited), including 7 papers in Molecular Biology, 6 papers in Materials Chemistry and 4 papers in Nutrition and Dietetics. Recurrent topics in Steven C. Shewry's work include Enzyme Structure and Function (6 papers), Biochemical and Molecular Research (4 papers) and Infant Nutrition and Health (4 papers). Steven C. Shewry is often cited by papers focused on Enzyme Structure and Function (6 papers), Biochemical and Molecular Research (4 papers) and Infant Nutrition and Health (4 papers). Steven C. Shewry collaborates with scholars based in New Zealand, United States and Canada. Steven C. Shewry's co-authors include Edward N. Baker, Heather M. Baker, Xiaolin Sun, Geoffrey B. Jameson, Andrew A. McCarthy, Mark L. Patchett, Andrew G. Plaut, Bryan F. Anderson, David R. Hendrixson and John W. Tweedie and has published in prestigious journals such as Journal of Molecular Biology, Biochemistry and Molecular Microbiology.

In The Last Decade

Steven C. Shewry

10 papers receiving 378 citations

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Steven C. Shewry 200 148 53 43 41 10 383
Angelique N. Besold 180 0.9× 198 1.3× 28 0.5× 27 0.6× 16 0.4× 13 434
Sian Stafford 155 0.8× 165 1.1× 26 0.5× 58 1.3× 50 1.2× 11 600
Emma Tarrant 209 1.0× 111 0.8× 63 1.2× 36 0.8× 16 0.4× 12 449
Emily M. Zygiel 255 1.3× 153 1.0× 19 0.4× 37 0.9× 14 0.3× 11 434
Zachery R. Lonergan 347 1.7× 212 1.4× 43 0.8× 81 1.9× 31 0.8× 14 705
Scott T. Nolan 202 1.0× 122 0.8× 31 0.6× 43 1.0× 45 1.1× 7 550
Melania D’Orazio 219 1.1× 137 0.9× 17 0.3× 52 1.2× 9 0.2× 18 501
Akiko Sakuma 163 0.8× 138 0.9× 7 0.1× 69 1.6× 36 0.9× 32 417
Damien Leduc 444 2.2× 53 0.4× 147 2.8× 69 1.6× 66 1.6× 10 623
Norie Sugitani 605 3.0× 219 1.5× 28 0.5× 93 2.2× 23 0.6× 15 905

Countries citing papers authored by Steven C. Shewry

Since Specialization
Citations

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

Fields of papers citing papers by Steven C. Shewry

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Steven C. Shewry. 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 Steven C. Shewry. The network helps show where Steven C. Shewry may publish in the future.

Co-authorship network of co-authors of Steven C. Shewry

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

All Works

10 of 10 papers shown
1.
Nurizzo, Didier, Steven C. Shewry, Michael H. Perlin, et al.. (2003). The Crystal Structure of Aminoglycoside-3′-Phosphotransferase-IIa, an Enzyme Responsible for Antibiotic Resistance. Journal of Molecular Biology. 327(2). 491–506. 83 indexed citations
2.
Hendrixson, David R., Jiazhou Qiu, Steven C. Shewry, et al.. (2003). Human milk lactoferrin is a serine protease that cleaves Haemophilus surface proteins at arginine‐rich sites. Molecular Microbiology. 47(3). 607–617. 80 indexed citations
3.
McCarthy, Andrew A., Heather M. Baker, Steven C. Shewry, Mark L. Patchett, & Edward N. Baker. (2001). Crystal Structure of Methylmalonyl-Coenzyme A Epimerase from P. shermanii. Structure. 9(7). 637–646. 47 indexed citations
4.
McCarthy, Andrew A., Heather M. Baker, Steven C. Shewry, et al.. (2001). Expression, crystallization and preliminary characterization of methylmalonyl coenzyme A epimerase fromPropionibacterium shermanii. Acta Crystallographica Section D Biological Crystallography. 57(5). 706–708. 7 indexed citations
5.
Baker, Heather M., Richard Kidd, Steven C. Shewry, et al.. (2000). Lactoferrin three-dimensional structure: a framework for interpreting function.. Cold Spring Harbor Protocols. 2014(1). 3–15. 8 indexed citations
6.
McCarthy, Andrew A., Heather M. Baker, Steven C. Shewry, Mark L. Patchett, & Edward N. Baker. (2000). Crystal structure of methylmalonyl-CoA epimerase: a novel enzymatic function on an ancient metal-binding scaffold. Acta Crystallographica Section A Foundations of Crystallography. 56(s1). s238–s238. 4 indexed citations
7.
Sun, Xiaolin, et al.. (1999). Structure of recombinant human lactoferrin expressed in Aspergillus awamori. Acta Crystallographica Section D Biological Crystallography. 55(2). 403–407. 65 indexed citations
8.
Bewley, Maria C., Beatrice M. Tam, Jasmine Grewal, et al.. (1999). X-ray Crystallography and Mass Spectroscopy Reveal that the N-lobe of Human Transferrin Expressed inPichia pastorisIs Folded Correctly but Is Glycosylated on Serine-32,. Biochemistry. 38(8). 2535–2541. 22 indexed citations
9.
Baker, Edward N., Bryan F. Anderson, Heather M. Baker, et al.. (1998). Three-dimensional structure of lactoferrin. Implications for function, including comparisons with transferrin.. PubMed. 443. 1–14. 37 indexed citations
10.

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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