Reto Horst

2.7k total citations · 1 hit paper
39 papers, 2.2k citations indexed

About

Reto Horst is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Materials Chemistry. According to data from OpenAlex, Reto Horst has authored 39 papers receiving a total of 2.2k indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Molecular Biology, 11 papers in Cellular and Molecular Neuroscience and 11 papers in Materials Chemistry. Recurrent topics in Reto Horst's work include Protein Structure and Dynamics (23 papers), Enzyme Structure and Function (11 papers) and Receptor Mechanisms and Signaling (8 papers). Reto Horst is often cited by papers focused on Protein Structure and Dynamics (23 papers), Enzyme Structure and Function (11 papers) and Receptor Mechanisms and Signaling (8 papers). Reto Horst collaborates with scholars based in United States, Switzerland and France. Reto Horst's co-authors include Kurt Wüthrich, Raymond C. Stevens, Jeffrey J. Liu, Vsevolod Katritch, Larisa Nikonova, Guihong Peng, Fred F. Damberger, Arthur L. Horwich, Peter Güntert and Walter Leal Filho and has published in prestigious journals such as Science, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Reto Horst

39 papers receiving 2.1k citations

Hit Papers

Biased Signaling Pathways in β 2 -Adrenergic Receptor Cha... 2012 2026 2016 2021 2012 100 200 300 400 500

Peers

Reto Horst
Franz Hagn Germany
Jade Li United Kingdom
Dianne Alewood Australia
Bruce R. Branchini United States
Achim Brinker United States
Monika G. Wood United States
Vincent Oliéric Switzerland
Paul Otto United States
Prashant Rao United States
Franz Hagn Germany
Reto Horst
Citations per year, relative to Reto Horst Reto Horst (= 1×) peers Franz Hagn

Countries citing papers authored by Reto Horst

Since Specialization
Citations

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

Fields of papers citing papers by Reto Horst

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Reto Horst

This figure shows the co-authorship network connecting the top 25 collaborators of Reto Horst. A scholar is included among the top collaborators of Reto Horst 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 Reto Horst. Reto Horst 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.
O’Brien, Matthew N., Reto Horst, Rohit Jaini, et al.. (2023). Self-Assembly Properties of an Amphiphilic Phosphate Ester Prodrug Designed for the Treatment of COVID-19. Journal of Pharmaceutical Sciences. 113(6). 1515–1522. 1 indexed citations
2.
Horst, Reto, Kathleen A. Farley, Bethany L. Kormos, & Jane M. Withka. (2020). NMR spectroscopy: the swiss army knife of drug discovery. Journal of Biomolecular NMR. 74(10-11). 509–519. 9 indexed citations
3.
Schiemer, James, Reto Horst, Yilin Meng, et al.. (2020). Snapshots and ensembles of BTK and cIAP1 protein degrader ternary complexes. Nature Chemical Biology. 17(2). 152–160. 83 indexed citations
4.
Torella, Rubben, John D. Knafels, Agnieszka Konopacka, et al.. (2018). An Intracellular Allosteric Modulator Binding Pocket in SK2 Ion Channels Is Shared by Multiple Chemotypes. Structure. 26(4). 533–544.e3. 25 indexed citations
5.
Eddy, Matthew T., Ming-Yue Lee, Zhan‐Guo Gao, et al.. (2017). Allosteric Coupling of Drug Binding and Intracellular Signaling in the A2A Adenosine Receptor. Cell. 172(1-2). 68–80.e12. 160 indexed citations
6.
Horst, Reto, Paweł Stańczak, & Kurt Wüthrich. (2014). NMR Polypeptide Backbone Conformation of the E. coli Outer Membrane Protein W. Structure. 22(8). 1204–1209. 28 indexed citations
7.
Sušac, Lukas, Reto Horst, & Kurt Wüthrich. (2014). Solution‐NMR Characterization of Outer‐Membrane Protein A from E. coli in Lipid Bilayer Nanodiscs and Detergent Micelles. ChemBioChem. 15(7). 995–1000. 37 indexed citations
8.
Horst, Reto, Jeffrey J. Liu, Raymond C. Stevens, & Kurt Wüthrich. (2013). β2‐Adrenergic Receptor Activation by Agonists Studied with 19F NMR Spectroscopy. Angewandte Chemie. 125(41). 10962–10965. 12 indexed citations
9.
Didenko, Tatiana, Jeffrey J. Liu, Reto Horst, Raymond C. Stevens, & Kurt Wüthrich. (2013). Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs. Current Opinion in Structural Biology. 23(5). 740–747. 77 indexed citations
10.
Liu, Jeffrey J., Reto Horst, Vsevolod Katritch, Raymond C. Stevens, & Kurt Wüthrich. (2012). Biased Signaling Pathways in β 2 -Adrenergic Receptor Characterized by 19 F-NMR. Science. 335(6072). 1106–1110. 570 indexed citations breakdown →
11.
Horst, Reto, Paweł Stańczak, Raymond C. Stevens, & Kurt Wüthrich. (2012). β2‐Adrenergic Receptor Solutions for Structural Biology Analyzed with Microscale NMR Diffusion Measurements. Angewandte Chemie International Edition. 52(1). 331–335. 21 indexed citations
12.
Koculi, Eda, Reto Horst, Arthur L. Horwich, & Kurt Wüthrich. (2011). Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single‐ring variant SR1 of the E. coli chaperonin GroEL. Protein Science. 20(8). 1380–1386. 17 indexed citations
13.
Jaudzems, Kristaps, M. Geralt, Pedro Serrano, et al.. (2010). NMR structure of the protein NP_247299.1: comparison with the crystal structure. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66(10). 1367–1380. 11 indexed citations
14.
Mohanty, Biswaranjan, Pedro Serrano, Bill Pedrini, et al.. (2010). Comparison of NMR and crystal structures for the proteins TM1112 and TM1367. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66(10). 1381–1392. 14 indexed citations
15.
Herrmann, Torsten, et al.. (2006). Automated Protein NMR Structure Determination in Crude Cell-Extract. Journal of Biomolecular NMR. 34(1). 3–11. 8 indexed citations
16.
Horst, Reto, Eric B. Bertelsen, Jocelyne Fiaux, et al.. (2005). Direct NMR observation of a substrate protein bound to the chaperonin GroEL. Proceedings of the National Academy of Sciences. 102(36). 12748–12753. 92 indexed citations
17.
Nishiyama, Mireille, Reto Horst, O. Eidam, et al.. (2005). Structural basis of chaperone–subunit complex recognition by the type 1 pilus assembly platform FimD. The EMBO Journal. 24(12). 2075–2086. 98 indexed citations
18.
Lee, Donghan, Fred F. Damberger, Guihong Peng, et al.. (2002). NMR structure of the unliganded Bombyx mori pheromone‐binding protein at physiological pH. FEBS Letters. 531(2). 314–318. 85 indexed citations
19.
Horst, Reto, Fred F. Damberger, Peter Luginbühl, et al.. (2001). NMR structure reveals intramolecular regulation mechanism for pheromone binding and release. Proceedings of the National Academy of Sciences. 98(25). 14374–14379. 234 indexed citations
20.
Damberger, Fred F., Reto Horst, Kurt Wüthrich, et al.. (2000). NMR characterization of a pH‐dependent equilibrium between two folded solution conformations of the pheromone‐binding protein from Bombyx mori. Protein Science. 9(5). 1038–1041. 106 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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