James F. Sinclair

1.0k total citations
18 papers, 811 citations indexed

About

James F. Sinclair is a scholar working on Molecular Biology, Infectious Diseases and Endocrinology. According to data from OpenAlex, James F. Sinclair has authored 18 papers receiving a total of 811 indexed citations (citations by other indexed papers that have themselves been cited), including 11 papers in Molecular Biology, 7 papers in Infectious Diseases and 7 papers in Endocrinology. Recurrent topics in James F. Sinclair's work include Viral gastroenteritis research and epidemiology (7 papers), Escherichia coli research studies (7 papers) and bioluminescence and chemiluminescence research (5 papers). James F. Sinclair is often cited by papers focused on Viral gastroenteritis research and epidemiology (7 papers), Escherichia coli research studies (7 papers) and bioluminescence and chemiluminescence research (5 papers). James F. Sinclair collaborates with scholars based in United States and United Kingdom. James F. Sinclair's co-authors include Alison D. O’Brien, Thomas Baldwin, Cory M. Robinson, Michael J. Smith, Miriam M. Ziegler, A. Clay Clark, Angela R. Melton‐Celsa, Evelyn A. Dean-Nystrom, David Shortle and Andrew J. Fisher and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and PLoS ONE.

In The Last Decade

James F. Sinclair

18 papers receiving 794 citations

Peers

James F. Sinclair

ENDOC

GENET

Steve Sarfaty United States

Marie-France Karwaski Canada

Stefanie Barbirz Germany

J.J. Michniewicz Canada

Ravi K. Lokareddy United States

Thierry Izoré Australia

Emma Byres Australia

Nora Cronin United Kingdom

Fatima Rasulova United States

Joel F. Schildbach United States

Steve Sarfaty United States

James F. Sinclair

300 ×0.8

ENDOC

700 ×1.8

87 ×0.3

117 ×1.1

GENET

110 ×1.2

Citations per year, relative to James F. Sinclair James F. Sinclair (= 1×) peers Steve Sarfaty

Countries citing papers authored by James F. Sinclair

Since Specialization

Citations

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

Fields of papers citing papers by James F. Sinclair

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by James F. Sinclair. 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 James F. Sinclair. The network helps show where James F. Sinclair may publish in the future.

Co-authorship network of co-authors of James F. Sinclair

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

All Works

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18 of 18 papers shown

Trojnár, Eszter, James F. Sinclair, Zhimei Liu, et al.. (2019). Shiga Toxin Type 1a (Stx1a) Reduces the Toxicity of the More Potent Stx2a In Vivo and In Vitro. Infection and Immunity. 87(4). 21 indexed citations

Teel, Louise D., et al.. (2013). Ricin Crosses Polarized Human Intestinal Cells and Intestines of Ricin-Gavaged Mice without Evident Damage and Then Disseminates to Mouse Kidneys. PLoS ONE. 8(7). e69706–e69706. 12 indexed citations

Zumbrun, Steven D., Leanne Hanson, James F. Sinclair, et al.. (2010). Human Intestinal Tissue and Cultured Colonic Cells Contain Globotriaosylceramide Synthase mRNA and the Alternate Shiga Toxin Receptor Globotetraosylceramide. Infection and Immunity. 78(11). 4488–4499. 61 indexed citations

Smith, Michael J., Angela R. Melton‐Celsa, James F. Sinclair, et al.. (2009). Monoclonal Antibody 11E10, Which Neutralizes Shiga Toxin Type 2 (Stx2), Recognizes Three Regions on the Stx2 A Subunit, Blocks the Enzymatic Action of the Toxin In Vitro, and Alters the Overall Cellular Distribution of the Toxin. Infection and Immunity. 77(7). 2730–2740. 34 indexed citations

Robinson, Cory M., James F. Sinclair, Michael J. Smith, & Alison D. O’Brien. (2006). Shiga toxin of enterohemorrhagic Escherichia coli type O157:H7 promotes intestinal colonization. Proceedings of the National Academy of Sciences. 103(25). 9667–9672. 136 indexed citations

Sinclair, James F., Evelyn A. Dean-Nystrom, & Alison D. O’Brien. (2006). The Established Intimin Receptor Tir and the Putative Eucaryotic Intimin Receptors Nucleolin and β1 Integrin Localize at or near the Site of Enterohemorrhagic Escherichia coli O157:H7 Adherence to Enterocytes In Vivo. Infection and Immunity. 74(2). 1255–1265. 42 indexed citations

Sinclair, James F. & Alison D. O’Brien. (2004). Intimin Types α, β, and γ Bind to Nucleolin with Equivalent Affinity but Lower Avidity than to the Translocated Intimin Receptor. Journal of Biological Chemistry. 279(32). 33751–33758. 54 indexed citations

Lawrence, Anthony J., J. G. Coote, R. Parton, et al.. (2002). A Direct Pyrophosphatase-coupled Assay Provides New Insights into the Activation of the Secreted Adenylate Cyclase from Bordetella pertussis by Calmodulin. Journal of Biological Chemistry. 277(25). 22289–22296. 7 indexed citations

Sinclair, James F. & Alison D. O’Brien. (2002). Cell Surface-localized Nucleolin Is a Eukaryotic Receptor for the Adhesin Intimin-γ of Enterohemorrhagic Escherichia coliO157:H7. Journal of Biological Chemistry. 277(4). 2876–2885. 157 indexed citations

10.

Sinclair, James F. & David Shortle. (1999). Analysis of long‐range interactions in a model denatured state of staphylococcal nuclease based on correlated changes in backbone dynamics. Protein Science. 8(5). 991–1000. 25 indexed citations

11.

Thoden, James B., Hazel M. Holden, Andrew J. Fisher, et al.. (1997). Structure of the β₂ homodimer of bacterial luciferase from vibrio harveyi: X‐ray analysis of a kinetic protein folding trap. Protein Science. 6(1). 13–23. 25 indexed citations

12.

Clark, A. Clay, Stephen W. Raso, James F. Sinclair, et al.. (1997). Kinetic Mechanism of Luciferase Subunit Folding and Assembly. Biochemistry. 36(7). 1891–1899. 29 indexed citations

13.

Xia, Jinqiang, James F. Sinclair, Thomas Baldwin, & Paul A. Lindahl. (1996). Carbon Monoxide Dehydrogenase from Clostridium thermoaceticum: Quaternary Structure, Stoichiometry of Its SDS-Induced Dissociation, and Characterization of the Faster-Migrating Form. Biochemistry. 35(6). 1965–1971. 19 indexed citations

14.

Baldwin, Thomas, Jon A. Christopher, Frank M. Raushel, et al.. (1995). Structure of bacterial luciferase. Current Opinion in Structural Biology. 5(6). 798–809. 46 indexed citations

15.

Xia, Jinqiang, Mark E. Anderson, D.P. Barondeau, et al.. (1995). The nickel and iron-sulfur centers in carbon monoxide dehydrogenase. Journal of Inorganic Biochemistry. 59(2-3). 634–634. 1 indexed citations

16.

Sinclair, James F., Miriam M. Ziegler, & Thomas Baldwin. (1994). Kinetic partitioning during protein folding yields multiple native states. Nature Structural & Molecular Biology. 1(5). 320–326. 48 indexed citations

17.

Sinclair, James F., et al.. (1993). Purified native subunits of bacterial luciferase are active in the bioluminescence reaction but fail to assemble into the .alpha..beta. structure. Biochemistry. 32(19). 5036–5044. 31 indexed citations

18.

Clark, A. Clay, James F. Sinclair, & Thomas Baldwin. (1993). Folding of bacterial luciferase involves a non-native heterodimeric intermediate in equilibrium with the native enzyme and the unfolded subunits. Journal of Biological Chemistry. 268(15). 10773–10779. 63 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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