Christopher W. Borysenko

753 total citations
18 papers, 633 citations indexed

About

Christopher W. Borysenko is a scholar working on Molecular Biology, Organic Chemistry and Oncology. According to data from OpenAlex, Christopher W. Borysenko has authored 18 papers receiving a total of 633 indexed citations (citations by other indexed papers that have themselves been cited), including 7 papers in Molecular Biology, 4 papers in Organic Chemistry and 4 papers in Oncology. Recurrent topics in Christopher W. Borysenko's work include Bone Metabolism and Diseases (4 papers), Organometallic Complex Synthesis and Catalysis (3 papers) and Cell Adhesion Molecules Research (3 papers). Christopher W. Borysenko is often cited by papers focused on Bone Metabolism and Diseases (4 papers), Organometallic Complex Synthesis and Catalysis (3 papers) and Cell Adhesion Molecules Research (3 papers). Christopher W. Borysenko collaborates with scholars based in United States, Italy and United Kingdom. Christopher W. Borysenko's co-authors include Harry C. Blair, J H Collins, Lisa Robinson, Adrian Whitty, Sara E. Kalla, Lihuan Cao, Yanan Li, Thomas Lehmann, Afsie Sabokbar and İvet Bahar and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Christopher W. Borysenko

18 papers receiving 610 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 W. Borysenko United States 14 395 134 101 81 64 18 633
Kálman G. Büki United States 20 714 1.8× 559 4.2× 87 0.9× 211 2.6× 66 1.0× 44 1.1k
Zee‐Fen Chang Taiwan 17 553 1.4× 144 1.1× 140 1.4× 130 1.6× 9 0.1× 26 857
Emily N. Chin United States 13 484 1.2× 102 0.8× 48 0.5× 197 2.4× 17 0.3× 19 863
Amy Baumann United States 10 358 0.9× 87 0.6× 42 0.4× 37 0.5× 7 0.1× 10 580
N Takami Japan 10 312 0.8× 60 0.4× 114 1.1× 77 1.0× 7 0.1× 13 535
Charlene M. Downey Canada 11 327 0.8× 130 1.0× 74 0.7× 287 3.5× 23 0.4× 13 716
Martina Schnoelzer Germany 8 612 1.5× 75 0.6× 208 2.1× 78 1.0× 6 0.1× 9 974
Paula S. Espino Canada 12 458 1.2× 118 0.9× 62 0.6× 48 0.6× 8 0.1× 13 635
Anja Stefanski Germany 15 474 1.2× 94 0.7× 40 0.4× 56 0.7× 7 0.1× 33 711
Arivusudar Marimuthu United States 14 606 1.5× 190 1.4× 88 0.9× 91 1.1× 5 0.1× 17 933

Countries citing papers authored by Christopher W. Borysenko

Since Specialization
Citations

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

Fields of papers citing papers by Christopher W. Borysenko

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Christopher W. Borysenko

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

All Works

18 of 18 papers shown
1.
Day, Eric S., Allan D. Capili, Christopher W. Borysenko, Mohammad Zafari, & Adrian Whitty. (2013). Determining the affinity and stoichiometry of interactions between unmodified proteins in solution using Biacore. Analytical Biochemistry. 440(1). 96–107. 15 indexed citations
2.
Trân, Kien, Christopher W. Borysenko, Michael Cascio, et al.. (2007). Tenascin cytotactin epidermal growth factor‐like repeat binds epidermal growth factor receptor with low affinity. Journal of Cellular Physiology. 211(3). 748–758. 57 indexed citations
3.
Robinson, Lisa, Christopher W. Borysenko, & Harry C. Blair. (2007). Tumor Necrosis Factor Family Receptors Regulating Bone Turnover. Annals of the New York Academy of Sciences. 1116(1). 432–443. 26 indexed citations
4.
Borysenko, Christopher W., Yanan Li, Anand Krishnan V. Iyer, et al.. (2006). Death receptor‐3 mediates apoptosis in human osteoblasts under narrowly regulated conditions. Journal of Cellular Physiology. 209(3). 1021–1028. 24 indexed citations
5.
Virji, Mohamed A., et al.. (2006). Serum phosphate and lactate vary with FSH in an early postmenopausal population. Clinical Biochemistry. 39(12). 1164–1167. 1 indexed citations
6.
Cao, Lihuan, Xiaomei Yan, Christopher W. Borysenko, et al.. (2005). CHDL: A cadherin-like domain in Proteobacteria and Cyanobacteria. FEMS Microbiology Letters. 251(2). 203–209. 23 indexed citations
7.
Borysenko, Christopher W., William Furey, & Harry C. Blair. (2005). Comparative modeling of TNFRSF25 (DR3) predicts receptor destabilization by a mutation linked to rheumatoid arthritis. Biochemical and Biophysical Research Communications. 328(3). 794–799. 18 indexed citations
8.
Robinson, Lisa, et al.. (2005). Negative Regulation of RANKL-induced Osteoclastic Differentiation in RAW264.7 Cells by Estrogen and Phytoestrogens. Journal of Biological Chemistry. 280(14). 13720–13727. 109 indexed citations
9.
Blair, Harry C., Christopher W. Borysenko, Anna Villa, et al.. (2004). In Vitro Differentiation of CD14 Cells From Osteopetrotic Subjects: Contrasting Phenotypes With TCIRG1, CLCN7, and Attachment Defects. Journal of Bone and Mineral Research. 19(8). 1329–1338. 26 indexed citations
10.
Borysenko, Christopher W., et al.. (2003). Expression and function of TNF-family proteins and receptors in human osteoblasts☆. Bone. 33(5). 760–770. 88 indexed citations
11.
Zhang, Lei, et al.. (2001). The Cis−Trans Isomerization of 1,2,5,6-Tetrasilacycloocta-3,7-dienes:  Analysis by Mechanistic Probes and Density Functional Theory. The Journal of Organic Chemistry. 66(16). 5275–5283. 7 indexed citations
12.
Zhang, Lei, et al.. (2001). Kinetics of the Cis,Cis to Trans,Trans Isomerization of 1,1,2,2,5,5,6,6-Octamethyl-1,2,5,6-tetrasilacycloocta-3,7-diene. The Journal of Organic Chemistry. 66(16). 5284–5290. 3 indexed citations
13.
Zhang, Lei, Christopher W. Borysenko, Thomas A. Albright, Eric R. Bittner, & T. Randall Lee. (2001). ChemInform Abstract: The cis—trans Isomerization of 1,2,5,6‐Tetrasilacycloocta‐3,7‐dienes: Analysis by Mechanistic Probes and Density Functional Theory.. ChemInform. 32(46). 1 indexed citations
14.
Whitty, Adrian & Christopher W. Borysenko. (1999). Small molecule cytokine mimetics. Chemistry & Biology. 6(4). R107–R118. 34 indexed citations
15.
Whitty, Adrian, Dian L. Olson, Christopher W. Borysenko, et al.. (1998). Interaction affinity between cytokine receptor components on the cell surface. Proceedings of the National Academy of Sciences. 95(22). 13165–13170. 33 indexed citations
16.
Curran, Timothy P., et al.. (1994). Intramolecular Acylolysis of Amide Derivatives of Kemp's Triacid: Strain Effects and Reaction Rates. The Journal of Organic Chemistry. 59(13). 3522–3529. 14 indexed citations
17.
Borysenko, Christopher W., Andreas Spaltenstein, Julie A. Straub, & George M. Whitesides. (1989). The synthesis of aldose sugars from half-protected dialdehydes using rabbit muscle aldolase. Journal of the American Chemical Society. 111(26). 9275–9276. 29 indexed citations
18.
Collins, J H & Christopher W. Borysenko. (1984). The 110,000-dalton actin- and calmodulin-binding protein from intestinal brush border is a myosin-like ATPase.. Journal of Biological Chemistry. 259(22). 14128–14135. 125 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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