Joseph Rucker

8.9k total citations · 1 hit paper
47 papers, 5.0k citations indexed

About

Joseph Rucker is a scholar working on Molecular Biology, Immunology and Virology. According to data from OpenAlex, Joseph Rucker has authored 47 papers receiving a total of 5.0k indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 20 papers in Immunology and 18 papers in Virology. Recurrent topics in Joseph Rucker's work include HIV Research and Treatment (18 papers), Immune Cell Function and Interaction (15 papers) and Monoclonal and Polyclonal Antibodies Research (9 papers). Joseph Rucker is often cited by papers focused on HIV Research and Treatment (18 papers), Immune Cell Function and Interaction (15 papers) and Monoclonal and Polyclonal Antibodies Research (9 papers). Joseph Rucker collaborates with scholars based in United States, Belgium and France. Joseph Rucker's co-authors include Robert W. Doms, Benjamin J. Doranz, Marc Parmentier, Michel Samson, Ronald G. Collman, Stephen C. Peiper, Robert Smyth, Yanjie Yi, Joanne F. Berson and Matthew Sharron and has published in prestigious journals such as Science, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Joseph Rucker

46 papers receiving 4.8k citations

Hit Papers

A Dual-Tropic Primary HIV... 1996 2026 2006 2016 1996 500 1000 1.5k

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Joseph Rucker 3.2k 2.8k 1.3k 1.1k 817 47 5.0k
Martin S. Springer 872 0.3× 1.8k 0.6× 530 0.4× 2.0k 1.8× 844 1.0× 65 4.9k
Lijun Wu 4.6k 1.4× 4.6k 1.7× 1.7k 1.3× 1.2k 1.1× 1.2k 1.4× 26 7.1k
Graham P. Allaway 4.8k 1.5× 3.2k 1.2× 2.3k 1.8× 1.7k 1.5× 720 0.9× 47 6.6k
Monsef Benkirane 4.0k 1.3× 3.1k 1.1× 1.6k 1.3× 4.4k 4.0× 754 0.9× 77 8.4k
Katsumi Maenaka 333 0.1× 3.1k 1.1× 664 0.5× 3.1k 2.8× 621 0.8× 191 7.2k
Éric A. Cohen 5.1k 1.6× 2.2k 0.8× 2.7k 2.1× 2.9k 2.6× 337 0.4× 175 7.6k
Russell D. Salter 328 0.1× 4.3k 1.6× 223 0.2× 2.2k 1.9× 760 0.9× 75 6.3k
Thomas Kieber‐Emmons 393 0.1× 1.5k 0.6× 254 0.2× 2.6k 2.3× 568 0.7× 175 4.6k
Romas Geleziunas 1.9k 0.6× 1.6k 0.6× 1.2k 0.9× 1.3k 1.2× 436 0.5× 89 3.9k
Yong Xiong 1.1k 0.4× 797 0.3× 730 0.6× 4.0k 3.6× 495 0.6× 151 5.8k

Countries citing papers authored by Joseph Rucker

Since Specialization
Citations

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

Fields of papers citing papers by Joseph Rucker

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Joseph Rucker. 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 Joseph Rucker. The network helps show where Joseph Rucker may publish in the future.

Co-authorship network of co-authors of Joseph Rucker

This figure shows the co-authorship network connecting the top 25 collaborators of Joseph Rucker. A scholar is included among the top collaborators of Joseph Rucker 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 Joseph Rucker. Joseph Rucker 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.
Rucker, Joseph, Ileine M. Sanchez, Anna Lobley, et al.. (2023). 1183 Development of CTIM-76, a highly specific Claudin 6 bispecific antibody. SHILAP Revista de lepidopterología. A1304–A1304. 1 indexed citations
2.
Stafford, Lewis J., Trevor Barnes, Rebecca N. Wright, et al.. (2022). Antibody specificity against highly conserved membrane protein Claudin 6 driven by single atomic contact point. iScience. 25(12). 105665–105665. 9 indexed citations
3.
Tucker, David, Jonathan T. Sullivan, Christine R. Fisher, et al.. (2018). Isolation of state-dependent monoclonal antibodies against the 12-transmembrane domain glucose transporter 4 using virus-like particles. Proceedings of the National Academy of Sciences. 115(22). E4990–E4999. 48 indexed citations
4.
Klarenbeek, A., Vladimir Bobkov, Jordi Doijen, et al.. (2018). CXCR4-targeting nanobodies differentially inhibit CXCR4 function and HIV entry. Biochemical Pharmacology. 158. 402–412. 43 indexed citations
5.
Thomas, Anu, Chidananda Sulli, Edgar Davidson, et al.. (2017). The Bitter Taste Receptor TAS2R16 Achieves High Specificity and Accommodates Diverse Glycoside Ligands by using a Two-faced Binding Pocket. Scientific Reports. 7(1). 7753–7753. 31 indexed citations
6.
Izquierdo, Shelley, Minha Park, Ellen J. Collarini, et al.. (2016). High-efficiency antibody discovery achieved with multiplexed microscopy. Microscopy. 65(4). 341–352. 30 indexed citations
7.
Sandau, Michelle M., et al.. (2015). A functional comparison of the domestic cat bitter receptors Tas2r38 and Tas2r43 with their human orthologs. BMC Neuroscience. 16(1). 33–33. 23 indexed citations
8.
Campbell, Michael C., Alessia Ranciaro, Jibril Hirbo, et al.. (2013). Origin and Differential Selection of Allelic Variation at TAS2R16 Associated with Salicin Bitter Taste Sensitivity in Africa. Molecular Biology and Evolution. 31(2). 288–302. 39 indexed citations
9.
Payne, Riley, et al.. (2012). Maturation of the Gag core decreases the stability of retroviral lipid membranes. Virology. 433(2). 401–409. 9 indexed citations
10.
Thomas, Anu, et al.. (2011). Probenecid Inhibits the Human Bitter Taste Receptor TAS2R16 and Suppresses Bitter Perception of Salicin. PLoS ONE. 6(5). e20123–e20123. 112 indexed citations
11.
Rucker, Joseph, et al.. (2010). Measuring Membrane Protein Interactions Using Optical Biosensors. Methods in molecular biology. 617. 445–456. 6 indexed citations
12.
Ahmed, Osama M., et al.. (2009). Perceptual variation in umami taste and polymorphisms in TAS1R taste receptor genes. American Journal of Clinical Nutrition. 90(3). 770S–779S. 104 indexed citations
13.
Rucker, Joseph. (2003). Optical Biosensor Assay Using Retroviral Receptor Pseudotypes. Humana Press eBooks. 228. 317–328. 4 indexed citations
14.
Blanpain, Cédric, Benjamin J. Doranz, Jalal Vakili, et al.. (1999). Multiple Charged and Aromatic Residues in CCR5 Amino-terminal Domain Are Involved in High Affinity Binding of Both Chemokines and HIV-1 Env Protein. Journal of Biological Chemistry. 274(49). 34719–34727. 133 indexed citations
15.
Horuk, Richard, Joseph Hesselgesser, Yiqing Zhou, et al.. (1998). The CC Chemokine I-309 Inhibits CCR8-dependent Infection by Diverse HIV-1 Strains. Journal of Biological Chemistry. 273(1). 386–391. 140 indexed citations
16.
Rucker, Joseph, Benjamin J. Doranz, Aimee L. Edinger, et al.. (1997). [9] Cell-cell fusion assay to study role of chemokine receptors in human immunodeficiency virus type 1 entry. Methods in enzymology on CD-ROM/Methods in enzymology. 288. 119–133. 74 indexed citations
17.
Doranz, Benjamin J., Joanne F. Berson, Joseph Rucker, & Robert W. Doms. (1997). Chemokine receptors as fusion cofactors for human immunodeficiency virus type 1 (HIV-1). Immunologic Research. 16(1). 15–28. 58 indexed citations
18.
Doranz, Benjamin J., Joseph Rucker, Yanjie Yi, et al.. (1996). A Dual-Tropic Primary HIV-1 Isolate That Uses Fusin and the β-Chemokine Receptors CKR-5, CKR-3, and CKR-2b as Fusion Cofactors. Cell. 85(7). 1149–1158. 1580 indexed citations breakdown →
19.
Rucker, Joseph, Michel Samson, Benjamin J. Doranz, et al.. (1996). Regions in β-Chemokine Receptors CCR5 and CCR2b That Determine HIV-1 Cofactor Specificity. Cell. 87(3). 437–446. 264 indexed citations
20.
Rucker, Joseph, et al.. (1992). Role of internal thermodynamics in determining hydrogen tunneling in enzyme-catalyzed hydrogen transfer reactions. Biochemistry. 31(46). 11489–11499. 45 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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