Robert J. Hoey

592 total citations
9 papers, 336 citations indexed

About

Robert J. Hoey is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Physiology. According to data from OpenAlex, Robert J. Hoey has authored 9 papers receiving a total of 336 indexed citations (citations by other indexed papers that have themselves been cited), including 7 papers in Molecular Biology, 5 papers in Radiology, Nuclear Medicine and Imaging and 2 papers in Physiology. Recurrent topics in Robert J. Hoey's work include Monoclonal and Polyclonal Antibodies Research (5 papers), Glycosylation and Glycoproteins Research (4 papers) and Alzheimer's disease research and treatments (2 papers). Robert J. Hoey is often cited by papers focused on Monoclonal and Polyclonal Antibodies Research (5 papers), Glycosylation and Glycoproteins Research (4 papers) and Alzheimer's disease research and treatments (2 papers). Robert J. Hoey collaborates with scholars based in United States, Bulgaria and Japan. Robert J. Hoey's co-authors include Akiko Koide, Shohei Koide, Ryan Gilbreth, John Wojcik, James R. Horn, Anthony A. Kossiakoff, Vasilios Kalas, Wenguang Liang, Wei‐Jen Tang and L.J. Bailey and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Robert J. Hoey

8 papers receiving 334 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 J. Hoey United States 6 265 152 50 47 26 9 336
Dmitri Tolkatchev United States 14 292 1.1× 52 0.3× 24 0.5× 62 1.3× 33 1.3× 27 479
Matthias Haffke France 13 307 1.2× 46 0.3× 25 0.5× 17 0.4× 50 1.9× 17 387
Raphaël Boisgard France 8 92 0.3× 115 0.8× 39 0.8× 19 0.4× 35 1.3× 12 356
Joseph M. Perchiacca United States 8 519 2.0× 382 2.5× 21 0.4× 139 3.0× 64 2.5× 8 619
Peter Stenlund Sweden 9 309 1.2× 65 0.4× 31 0.6× 16 0.3× 25 1.0× 9 412
Philipp Bräuer United Kingdom 3 142 0.5× 81 0.5× 24 0.5× 16 0.3× 31 1.2× 5 229
Ku-chuan Hsiao United States 9 286 1.1× 79 0.5× 33 0.7× 9 0.2× 30 1.2× 9 356
Anna Hills United Kingdom 7 327 1.2× 158 1.0× 16 0.3× 32 0.7× 44 1.7× 9 445
Douglas D. Banks United States 10 505 1.9× 250 1.6× 32 0.6× 15 0.3× 42 1.6× 18 565
Adriana Kita United States 6 261 1.0× 182 1.2× 25 0.5× 62 1.3× 49 1.9× 7 357

Countries citing papers authored by Robert J. Hoey

Since Specialization
Citations

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

Fields of papers citing papers by Robert J. Hoey

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Robert J. Hoey

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

All Works

9 of 9 papers shown
1.
Smith, Christopher A., et al.. (2023). Molecular recognition requires dimerization of a VHH antibody. mAbs. 15(1). 2215363–2215363. 1 indexed citations
2.
Hoey, Robert J., et al.. (2019). Structure and development of single domain antibodies as modules for therapeutics and diagnostics. Experimental Biology and Medicine. 244(17). 1568–1576. 48 indexed citations
3.
Mukherjee, Somnath, et al.. (2015). A New Versatile Immobilization Tag Based on the Ultra High Affinity and Reversibility of the Calmodulin–Calmodulin Binding Peptide Interaction. Journal of Molecular Biology. 427(16). 2707–2725. 17 indexed citations
4.
Zhang, Xulun, Robert J. Hoey, Akiko Koide, et al.. (2014). A Synthetic Antibody Fragment Targeting Nicastrin Affects Assembly and Trafficking of γ-Secretase. Journal of Biological Chemistry. 289(50). 34851–34861. 4 indexed citations
5.
Bailey, L.J., et al.. (2014). Applications for an engineered Protein-G variant with a pH controllable affinity to antibody fragments. Journal of Immunological Methods. 415. 24–30. 31 indexed citations
6.
Liang, Wenguang, Vasilios Kalas, Robert J. Hoey, et al.. (2013). Conformational states and recognition of amyloidogenic peptides of human insulin-degrading enzyme. Proceedings of the National Academy of Sciences. 110(34). 13827–13832. 48 indexed citations
7.
Zhang, Xulun, Robert J. Hoey, Guoqing Lin, et al.. (2012). Identification of a tetratricopeptide repeat-like domain in the nicastrin subunit of γ-secretase using synthetic antibodies. Proceedings of the National Academy of Sciences. 109(22). 8534–8539. 29 indexed citations
8.
Koide, Akiko, John Wojcik, Ryan Gilbreth, Robert J. Hoey, & Shohei Koide. (2011). Teaching an Old Scaffold New Tricks: Monobodies Constructed Using Alternative Surfaces of the FN3 Scaffold. Journal of Molecular Biology. 415(2). 393–405. 157 indexed citations
9.
Vanýsek, Petr & Robert J. Hoey. (2006). Impedance mapping of voltammetric curves of classical redox systems. ECS Meeting Abstracts. MA2006-01(34). 1193–1193. 1 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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