Robert N. Ben

3.5k total citations
88 papers, 2.5k citations indexed

About

Robert N. Ben is a scholar working on Ecology, Mechanics of Materials and Molecular Biology. According to data from OpenAlex, Robert N. Ben has authored 88 papers receiving a total of 2.5k indexed citations (citations by other indexed papers that have themselves been cited), including 35 papers in Ecology, 21 papers in Mechanics of Materials and 19 papers in Molecular Biology. Recurrent topics in Robert N. Ben's work include Physiological and biochemical adaptations (35 papers), Freezing and Crystallization Processes (21 papers) and Neurobiology and Insect Physiology Research (17 papers). Robert N. Ben is often cited by papers focused on Physiological and biochemical adaptations (35 papers), Freezing and Crystallization Processes (21 papers) and Neurobiology and Insect Physiology Research (17 papers). Robert N. Ben collaborates with scholars based in Canada, United States and Australia. Robert N. Ben's co-authors include Chantelle J. Capicciotti, Jennie G. Briard, Tony Durst, Roger Y. Tam, Jason P. Acker, Vincent Bouvet, Pawel Czechura, Joy E. Swanson, Robert S. Parker and Graham W. Burton and has published in prestigious journals such as Journal of the American Chemical Society, Angewandte Chemie International Edition and Langmuir.

In The Last Decade

Robert N. Ben

87 papers receiving 2.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert N. Ben Canada 30 863 639 602 556 311 88 2.5k
Chantelle J. Capicciotti Canada 17 277 0.3× 519 0.8× 344 0.6× 216 0.4× 117 0.4× 36 1.2k
Nelly M. Tsvetkova United States 25 191 0.2× 1.3k 2.0× 106 0.2× 42 0.1× 29 0.1× 53 2.4k
Rebecca Notman United Kingdom 21 170 0.2× 665 1.0× 318 0.5× 166 0.3× 50 0.2× 33 1.6k
Stéphane M. Gagné Canada 30 384 0.4× 1.6k 2.5× 91 0.2× 160 0.3× 70 0.2× 66 3.0k
Thomas Boesen Denmark 27 279 0.3× 1.2k 1.9× 349 0.6× 134 0.2× 14 0.0× 94 2.8k
R.E. Feeney United States 26 646 0.7× 609 1.0× 74 0.1× 203 0.4× 57 0.2× 45 1.9k
Ann E. Oliver United States 23 133 0.2× 1.0k 1.6× 100 0.2× 22 0.0× 51 0.2× 39 2.5k
Hidemasa Kondo Japan 27 635 0.7× 842 1.3× 65 0.1× 232 0.4× 140 0.5× 57 2.3k
Lois M. Crowe United States 17 271 0.3× 696 1.1× 45 0.1× 41 0.1× 30 0.1× 21 1.6k
Daniel S.C. Yang Canada 19 464 0.5× 874 1.4× 63 0.1× 135 0.2× 67 0.2× 37 2.1k

Countries citing papers authored by Robert N. Ben

Since Specialization
Citations

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

Fields of papers citing papers by Robert N. Ben

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Robert N. Ben. 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 Robert N. Ben. The network helps show where Robert N. Ben may publish in the future.

Co-authorship network of co-authors of Robert N. Ben

This figure shows the co-authorship network connecting the top 25 collaborators of Robert N. Ben. A scholar is included among the top collaborators of Robert N. Ben 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 Robert N. Ben. Robert N. Ben 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.
Suchý, Mojmı́r, et al.. (2024). It’s a Trap! Aldolase-Prescribed C4Deoxyradiofluorination Affords Intracellular Trapping and the Tracing of Fructose Metabolism by PET. Journal of Nuclear Medicine. 65(3). 475–480. 2 indexed citations
2.
Mommaerts, Kathleen, Satoshi Okawa, Tracey R. Turner, et al.. (2024). Ice recrystallization inhibitors enable efficient cryopreservation of induced pluripotent stem cells: A functional and transcriptomic analysis. Stem Cell Research. 81. 103583–103583. 1 indexed citations
3.
Nagashima, Jennifer B., Jason P. Acker, Robert N. Ben, et al.. (2022). First Report of Successful Laser Warming for Frozen Gonadal Tissues and Oocytes in the Domestic Cat Model. Biopreservation and Biobanking. 21(4). 433–438. 2 indexed citations
4.
Ben, Robert N., et al.. (2020). Characterizing the ability of an ice recrystallization inhibitor to improve platelet cryopreservation. Cryobiology. 96. 152–158. 14 indexed citations
5.
Aohara, Tsutomu, Jun Furukawa, Kenji Miura, et al.. (2019). Presence of a basic secretory protein in xylem sap and shoots of poplar in winter and its physicochemical activities against winter environmental conditions. Journal of Plant Research. 132(5). 655–665. 1 indexed citations
6.
7.
Ben, Robert N., et al.. (2018). The Ice Recrystalization Inhibitor 2FA Increases the Engraftment Activities of Cord Blood Stem and Progenitor Cells. Experimental Hematology. 64. S74–S74. 1 indexed citations
8.
Ben, Robert N., et al.. (2016). Photoswitchable carbohydrate-based fluorosurfactants as tuneable ice recrystallization inhibitors. Carbohydrate Research. 439. 1–8. 12 indexed citations
9.
Briard, Jennie G., et al.. (2016). Inhibition of ice recrystallization and cryoprotective activity of wheat proteins in liver and pancreatic cells. Protein Science. 25(5). 974–986. 14 indexed citations
10.
Capicciotti, Chantelle J., et al.. (2015). Modulation of antifreeze activity and the effect upon post-thaw HepG2 cell viability after cryopreservation. Cryobiology. 70(2). 79–89. 19 indexed citations
11.
Capicciotti, Chantelle J., Jayme Kurach, Tracey R. Turner, et al.. (2015). Small Molecule Ice Recrystallization Inhibitors Enable Freezing of Human Red Blood Cells with Reduced Glycerol Concentrations. Scientific Reports. 5(1). 9692–9692. 106 indexed citations
12.
Corcilius, Leo, et al.. (2013). Synthesis of peptides and glycopeptides with polyproline II helical topology as potential antifreeze molecules. Bioorganic & Medicinal Chemistry. 21(12). 3569–3581. 28 indexed citations
13.
Wilkinson, Brendan L., Chantelle J. Capicciotti, Morten Thaysen‐Andersen, et al.. (2012). Total Synthesis of Homogeneous Antifreeze Glycopeptides and Glycoproteins. Angewandte Chemie International Edition. 51(15). 3606–3610. 102 indexed citations
14.
Chaytor, Jennifer L., Lin Wu, Mathieu Leclère, et al.. (2011). Inhibiting ice recrystallization and optimization of cell viability after cryopreservation. Glycobiology. 22(1). 123–133. 91 indexed citations
15.
Chaytor, Jennifer L. & Robert N. Ben. (2010). Assessing the ability of a short fluorinated antifreeze glycopeptide and a fluorinated carbohydrate derivative to inhibit ice recrystallization. Bioorganic & Medicinal Chemistry Letters. 20(17). 5251–5254. 16 indexed citations
16.
Ben, Robert N., et al.. (2010). The adsorption of antifreeze glycoprotein fraction 8 on dry and wet mica. Colloids and Surfaces B Biointerfaces. 82(1). 134–140. 5 indexed citations
17.
Tam, Roger Y., Sandra S. Ferreira, Pawel Czechura, Jennifer L. Chaytor, & Robert N. Ben. (2008). Hydration IndexA Better Parameter for Explaining Small Molecule Hydration in Inhibition of Ice Recrystallization. Journal of the American Chemical Society. 130(51). 17494–17501. 93 indexed citations
18.
Madhusudhan, P., et al.. (2003). A Serendipitous Discovery of Antifreeze Protein-Specific Activity in C-Linked Antifreeze Glycoprotein Analogs. Cell Biochemistry and Biophysics. 38(2). 115–124. 38 indexed citations
19.
Bouvet, Vincent & Robert N. Ben. (2003). Antifreeze Glycoproteins: Structure, Conformation, and Biological Applications. Cell Biochemistry and Biophysics. 39(2). 133–144. 52 indexed citations
20.
Swanson, Joy E., Robert N. Ben, Graham W. Burton, & Robert S. Parker. (1999). Urinary excretion of 2,7,8-trimethyl-2-(β-carboxyethyl)-6-hydroxychroman is a major route of elimination of γ-tocopherol in humans. Journal of Lipid Research. 40(4). 665–671. 157 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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