Christopher P. Garnham

2.1k total citations
27 papers, 1.6k citations indexed

About

Christopher P. Garnham is a scholar working on Molecular Biology, Ecology and Cell Biology. According to data from OpenAlex, Christopher P. Garnham has authored 27 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 11 papers in Ecology and 9 papers in Cell Biology. Recurrent topics in Christopher P. Garnham's work include Physiological and biochemical adaptations (10 papers), Microtubule and mitosis dynamics (5 papers) and Mycotoxins in Agriculture and Food (5 papers). Christopher P. Garnham is often cited by papers focused on Physiological and biochemical adaptations (10 papers), Microtubule and mitosis dynamics (5 papers) and Mycotoxins in Agriculture and Food (5 papers). Christopher P. Garnham collaborates with scholars based in Canada, United States and Japan. Christopher P. Garnham's co-authors include Peter L. Davies, Robert L. Campbell, Antonina Roll‐Mecak, Ian Yu, Jack A. Gilbert, Laurie A. Graham, Andrew J. Scotter, Christopher B. Marshall, Sakae Tsuda and Virginia K. Walker and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Christopher P. Garnham

26 papers receiving 1.6k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Christopher P. Garnham Canada 18 797 507 453 336 197 27 1.6k
Christopher B. Marshall Canada 33 828 1.0× 1.7k 3.4× 415 0.9× 456 1.4× 218 1.1× 64 3.0k
Chi-Hing C. Cheng United States 23 1.3k 1.6× 603 1.2× 321 0.7× 113 0.3× 384 1.9× 33 2.2k
Sakae Tsuda Japan 35 1.2k 1.5× 1.4k 2.7× 449 1.0× 178 0.5× 231 1.2× 117 3.3k
Hidemasa Kondo Japan 27 635 0.8× 842 1.7× 232 0.5× 81 0.2× 117 0.6× 57 2.3k
Steffen P. Graether Canada 23 643 0.8× 778 1.5× 258 0.6× 113 0.3× 165 0.8× 52 1.9k
Yoshiyuki Nishimiya Japan 22 691 0.9× 255 0.5× 254 0.6× 60 0.2× 109 0.6× 46 1.1k
Jason Baardsnes Canada 22 628 0.8× 639 1.3× 255 0.6× 53 0.2× 148 0.8× 46 1.7k
Yin Yeh United States 20 648 0.8× 479 0.9× 283 0.6× 92 0.3× 129 0.7× 44 1.6k
Heman Chao Canada 16 917 1.2× 347 0.7× 409 0.9× 62 0.2× 119 0.6× 24 1.4k
K. Vanya Ewart Canada 26 965 1.2× 488 1.0× 139 0.3× 61 0.2× 202 1.0× 53 2.1k

Countries citing papers authored by Christopher P. Garnham

Since Specialization
Citations

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

Fields of papers citing papers by Christopher P. Garnham

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Christopher P. Garnham

This figure shows the co-authorship network connecting the top 25 collaborators of Christopher P. Garnham. A scholar is included among the top collaborators of Christopher P. Garnham 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 Christopher P. Garnham. Christopher P. Garnham 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
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Hoogstra, Shawn, et al.. (2024). Enzymatic Hydrolysis of Resorcylic Acid Lactones by an Aeromicrobium sp.. Toxins. 16(9). 404–404. 3 indexed citations
4.
Telmer, Patrick G., et al.. (2022). Application of Aspergillus niger Fumonisin Amine Oxidase (AnFAO) to Detoxify Fumonisin-Contaminated Maize. Toxins. 14(8). 544–544. 5 indexed citations
5.
Renaud, Justin B., et al.. (2021). Structure Activity Relationship for Fumonisin Phytotoxicity. Chemical Research in Toxicology. 34(6). 1604–1611. 15 indexed citations
6.
Garnham, Christopher P., Ian Yu, Yan Li, & Antonina Roll‐Mecak. (2017). Crystal structure of tubulin tyrosine ligase-like 3 reveals essential architectural elements unique to tubulin monoglycylases. Proceedings of the National Academy of Sciences. 114(25). 6545–6550. 21 indexed citations
7.
Garnham, Christopher P., Annapurna Vemu, Elizabeth M. Wilson-Kubalek, et al.. (2015). Multivalent Microtubule Recognition by Tubulin Tyrosine Ligase-like Family Glutamylases. Cell. 161(5). 1112–1123. 78 indexed citations
8.
Yu, Ian, Christopher P. Garnham, & Antonina Roll‐Mecak. (2015). Writing and Reading the Tubulin Code. Journal of Biological Chemistry. 290(28). 17163–17172. 143 indexed citations
9.
Guo, Shuaiqi, et al.. (2013). Role of Ca2+ in folding the tandem β‐sandwich extender domains of a bacterial ice‐binding adhesin. FEBS Journal. 280(22). 5919–5932. 23 indexed citations
10.
Liu, Yanjie, Christopher P. Garnham, Antonina Roll‐Mecak, & Martin E. Tanner. (2013). Phosphinic acid-based inhibitors of tubulin polyglutamylases. Bioorganic & Medicinal Chemistry Letters. 23(15). 4408–4412. 12 indexed citations
11.
Basu, Koli, Christopher P. Garnham, Yoshiyuki Nishimiya, et al.. (2013). Determining the Ice-binding Planes of Antifreeze Proteins by Fluorescence-based Ice Plane Affinity. Journal of Visualized Experiments. e51185–e51185. 38 indexed citations
12.
Guo, Shuaiqi, Christopher P. Garnham, John C. Whitney, Laurie A. Graham, & Peter L. Davies. (2012). Re-Evaluation of a Bacterial Antifreeze Protein as an Adhesin with Ice-Binding Activity. PLoS ONE. 7(11). e48805–e48805. 56 indexed citations
13.
Garnham, Christopher P. & Antonina Roll‐Mecak. (2012). The chemical complexity of cellular microtubules: Tubulin post‐translational modification enzymes and their roles in tuning microtubule functions. Cytoskeleton. 69(7). 442–463. 133 indexed citations
14.
Garnham, Christopher P., Yoshiyuki Nishimiya, Sakae Tsuda, & Peter L. Davies. (2012). Engineering a naturally inactive isoform of type III antifreeze protein into one that can stop the growth of ice. FEBS Letters. 586(21). 3876–3881. 25 indexed citations
15.
Kondo, Hidemasa, Yuichi Hanada, Hiroshi Sugimoto, et al.. (2012). Ice-binding site of snow mold fungus antifreeze protein deviates from structural regularity and high conservation. Proceedings of the National Academy of Sciences. 109(24). 9360–9365. 82 indexed citations
16.
Garnham, Christopher P., Robert L. Campbell, Virginia K. Walker, & Peter L. Davies. (2011). Novel dimeric β-helical model of an ice nucleation protein with bridged active sites. BMC Structural Biology. 11(1). 36–36. 100 indexed citations
17.
Garnham, Christopher P., et al.. (2008). A Ca2+-dependent bacterial antifreeze protein domain has a novel β-helical ice-binding fold. Biochemical Journal. 411(1). 171–180. 112 indexed citations
18.
Scotter, Andrew J., Christopher B. Marshall, Laurie A. Graham, et al.. (2006). The basis for hyperactivity of antifreeze proteins. Cryobiology. 53(2). 229–239. 218 indexed citations
19.
Fu, Qin, Christopher P. Garnham, Steven T. Elliott, Diane E. Bovenkamp, & Jennifer E. Van Eyk. (2005). A robust, streamlined, and reproducible method for proteomic analysis of serum by delipidation, albumin and IgG depletion, and two‐dimensional gel electrophoresis. PROTEOMICS. 5(10). 2656–2664. 89 indexed citations
20.
Graham, David R., Christopher P. Garnham, Qin Fu, Jeffrey Robbins, & Jennifer E. Van Eyk. (2005). Improvements in two‐dimensional gel electrophoresis by utilizing a low cost “in‐house” neutral pH sodium dodecyl sulfate‐polyacrylamide gel electrophoresis system. PROTEOMICS. 5(9). 2309–2314. 27 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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