Ronald E. Stenkamp

15.9k total citations · 3 hit papers
144 papers, 13.0k citations indexed

About

Ronald E. Stenkamp is a scholar working on Molecular Biology, Cell Biology and Organic Chemistry. According to data from OpenAlex, Ronald E. Stenkamp has authored 144 papers receiving a total of 13.0k indexed citations (citations by other indexed papers that have themselves been cited), including 79 papers in Molecular Biology, 32 papers in Cell Biology and 30 papers in Organic Chemistry. Recurrent topics in Ronald E. Stenkamp's work include Enzyme Structure and Function (22 papers), Biotin and Related Studies (21 papers) and Receptor Mechanisms and Signaling (19 papers). Ronald E. Stenkamp is often cited by papers focused on Enzyme Structure and Function (22 papers), Biotin and Related Studies (21 papers) and Receptor Mechanisms and Signaling (19 papers). Ronald E. Stenkamp collaborates with scholars based in United States, Switzerland and Poland. Ronald E. Stenkamp's co-authors include Isolde Le Trong, Krzysztof Palczewski, David C. Teller, Craig A. Behnke, Tetsuji Okada, Brian A. Fox, Hiroyuki Motoshima, Masaki Yamamoto, Masashi Miyano and Tetsuya Hori and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Ronald E. Stenkamp

144 papers receiving 12.6k citations

Hit Papers

Crystal Structure of Rhod... 1993 2026 2004 2015 2000 1993 2001 1000 2.0k 3.0k 4.0k

Author Peers

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

Author Last Decade Papers Cites
Ronald E. Stenkamp 8.8k 4.4k 1.2k 1.2k 1.1k 144 13.0k
Elizabeth D. Getzoff 7.6k 0.9× 2.3k 0.5× 1.1k 0.9× 1.5k 1.3× 570 0.5× 149 14.4k
L. Mario Amzel 9.7k 1.1× 968 0.2× 810 0.7× 1.7k 1.4× 1.3k 1.2× 246 14.7k
Kenneth A. Walsh 12.2k 1.4× 2.5k 0.6× 2.2k 1.8× 1.6k 1.3× 1.7k 1.6× 229 17.5k
Takashi Kumasaka 8.1k 0.9× 3.8k 0.9× 413 0.3× 1.5k 1.3× 495 0.5× 156 11.1k
Wayne L. Hubbell 15.2k 1.7× 6.3k 1.4× 1.7k 1.4× 4.2k 3.6× 589 0.5× 256 22.9k
Osamu Nureki 19.5k 2.2× 1.6k 0.4× 947 0.8× 1.2k 1.0× 1.2k 1.1× 367 23.8k
Robert J. Fletterick 12.0k 1.4× 1.2k 0.3× 3.6k 3.0× 1.5k 1.3× 845 0.8× 247 18.6k
Luis Moroder 9.9k 1.1× 2.6k 0.6× 1.1k 0.9× 2.5k 2.1× 501 0.5× 408 14.3k
Israel Pecht 5.3k 0.6× 871 0.2× 941 0.8× 1.1k 0.9× 2.4k 2.2× 368 10.6k
Karl Harlos 5.4k 0.6× 687 0.2× 734 0.6× 819 0.7× 2.5k 2.3× 156 10.5k

Countries citing papers authored by Ronald E. Stenkamp

Since Specialization
Citations

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

Fields of papers citing papers by Ronald E. Stenkamp

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Ronald E. Stenkamp. 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 Ronald E. Stenkamp. The network helps show where Ronald E. Stenkamp may publish in the future.

Co-authorship network of co-authors of Ronald E. Stenkamp

This figure shows the co-authorship network connecting the top 25 collaborators of Ronald E. Stenkamp. A scholar is included among the top collaborators of Ronald E. Stenkamp 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 Ronald E. Stenkamp. Ronald E. Stenkamp 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.
Kisiela, Dagmara, Gianluca Interlandi, Veronika Tchesnokova, et al.. (2021). Toggle switch residues control allosteric transitions in bacterial adhesins by participating in a concerted repacking of the protein core. PLoS Pathogens. 17(4). e1009440–e1009440. 8 indexed citations
2.
Will, W. Ryan, Peter S. Brzović, Isolde Le Trong, et al.. (2019). The Evolution of SlyA/RovA Transcription Factors from Repressors to Countersilencers in Enterobacteriaceae. mBio. 10(2). 22 indexed citations
3.
Stenkamp, Ronald E.. (2018). Identifying G protein-coupled receptor dimers from crystal packings. Acta Crystallographica Section D Structural Biology. 74(7). 655–670. 14 indexed citations
4.
Pruneda, Jonathan N., F. Donelson Smith, Danielle L. Swaney, et al.. (2014). E2~Ub conjugates regulate the kinase activity of Shigella effector OspG during pathogenesis. The EMBO Journal. 33(5). n/a–n/a. 58 indexed citations
5.
Zhu, Li, Geeng-Fu Jang, Beata Jastrzębska, et al.. (2004). A Naturally Occurring Mutation of the Opsin Gene (T4R) in Dogs Affects Glycosylation and Stability of the G Protein-coupled Receptor. Journal of Biological Chemistry. 279(51). 53828–53839. 59 indexed citations
6.
Jastrzębska, Beata, Tadao Maeda, Li Zhu, et al.. (2004). Functional Characterization of Rhodopsin Monomers and Dimers in Detergents. Journal of Biological Chemistry. 279(52). 54663–54675. 111 indexed citations
7.
Stenkamp, Ronald E., Sławomir Filipek, C.A.G.G. Driessen, D.C. Teller, & Krzysztof Palczewski. (2002). Crystal structure of rhodopsin: a template for cone visual pigments and other G protein-coupled receptors. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1565(2). 168–182. 94 indexed citations
8.
Hyre, David E., Lynn M. Amon, Julie E. Penzotti, et al.. (2002). Early mechanistic events in biotin dissociation from streptavidin. Nature Structural Biology. 9(8). 582–5. 45 indexed citations
9.
Trong, Isolde Le, Ronald E. Stenkamp, Catherine Ibarra, William M. Atkins, & Elinor T. Adman. (2002). 1.3‐Å resolution structure of human glutathione S‐transferase with S‐hexyl glutathione bound reveals possible extended ligandin binding site. Proteins Structure Function and Bioinformatics. 48(4). 618–627. 54 indexed citations
10.
Dixon, R. W., Randall J. Radmer, Bernd Kuhn, et al.. (2002). Theoretical and Experimental Studies of Biotin Analogues That Bind Almost as Tightly to Streptavidin as Biotin. The Journal of Organic Chemistry. 67(6). 1827–1837. 21 indexed citations
11.
Palczewski, Krzysztof, Takashi Kumasaka, Tetsuya Hori, et al.. (2000). Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor. Science. 289(5480). 739–745. 4567 indexed citations breakdown →
12.
Sieker, Larry C., Michael Holmes, I. Le Trong, et al.. (2000). The 1.9 Å crystal structure of the “as isolated” rubrerythrin from Desulfovibrio vulgaris: some surprising results. JBIC Journal of Biological Inorganic Chemistry. 5(4). 505–513. 26 indexed citations
13.
Fox, Brian A., Vivien C. Yee, Lars C. Pedersen, et al.. (1999). Identification of the Calcium Binding Site and a Novel Ytterbium Site in Blood Coagulation Factor XIII by X-ray Crystallography. Journal of Biological Chemistry. 274(8). 4917–4923. 93 indexed citations
14.
Trong, I. Le, et al.. (1998). Structural studies of binding site tryptophan mutants in the high-affinity streptavidin-biotin complex 1 1Edited by I. A. Wilson. Journal of Molecular Biology. 279(1). 211–221. 74 indexed citations
15.
Stenkamp, Ronald E., et al.. (1995). Comparison of a protein model with its x-ray structure: The ligand binding domain of E-selectin. Bioconjugate Chemistry. 6(1). 3–6. 10 indexed citations
16.
Sieker, Larry C., Ronald E. Stenkamp, & Jean LeGall. (1994). [14] Rubredoxin in crystalline state. Methods in enzymology on CD-ROM/Methods in enzymology. 243. 203–216. 65 indexed citations
17.
Hollenbaugh, Diane, Jürgen Bajorath, Ronald E. Stenkamp, & A Aruffo. (1993). Interaction of P-selectin (CD62) and its cellular ligand: Analysis of critical residues. Biochemistry. 32(12). 2960–2966. 59 indexed citations
18.
Holmes, Margaret A., I. Le Trong, S. Turley, Larry C. Sieker, & Ronald E. Stenkamp. (1991). Structures of deoxy and oxy hemerythrin at 2.0 Å resolution. Journal of Molecular Biology. 218(3). 583–593. 167 indexed citations
19.
Stenkamp, Ronald E., Larry C. Sieker, & Lyle H. Jensen. (1990). The structure of rubredoxin from Desulfovibrio desulfuricans strain 27774 at 1.5 Å resolution. Proteins Structure Function and Bioinformatics. 8(4). 352–364. 44 indexed citations
20.
Pickart, Loren, Jonathan H. Freedman, J. Peisach, et al.. (1980). Growth-modulating plasma tripeptide may function by facilitating copper uptake into cells. Nature. 288(5792). 715–717. 147 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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