Richard Obexer

1.6k total citations · 1 hit paper
24 papers, 1.2k citations indexed

About

Richard Obexer is a scholar working on Molecular Biology, Biomedical Engineering and Organic Chemistry. According to data from OpenAlex, Richard Obexer has authored 24 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 6 papers in Biomedical Engineering and 4 papers in Organic Chemistry. Recurrent topics in Richard Obexer's work include Enzyme Catalysis and Immobilization (7 papers), Chemical Synthesis and Analysis (6 papers) and Innovative Microfluidic and Catalytic Techniques Innovation (4 papers). Richard Obexer is often cited by papers focused on Enzyme Catalysis and Immobilization (7 papers), Chemical Synthesis and Analysis (6 papers) and Innovative Microfluidic and Catalytic Techniques Innovation (4 papers). Richard Obexer collaborates with scholars based in United Kingdom, Switzerland and United States. Richard Obexer's co-authors include Donald Hilvert, David Baker, Andrew D. Griffiths, Hiroaki Suga, Louise J. Walport, Anthony P. Green, Peer R. E. Mittl, А. Т. Година, Xavier Garrabou and Lars Giger and has published in prestigious journals such as Nature, Science and Journal of the American Chemical Society.

In The Last Decade

Richard Obexer

22 papers receiving 1.1k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Emergence of a catalytic tetrad during evolution of a highly active artificial aldolase

2016 253 citations Richard Obexer, А. Т. Година et al. Nature Chemistry profile →

Peers

Richard Obexer

MB

OC

BE

MC

EEE

Cathleen Zeymer Germany

Roberto A. Chica Canada

Claudio Iacobucci Germany

Helena M. Lovick United States

Jeremy H. Mills United States

Yakov Kipnis United States

Martin Norin Sweden

Ivana Drienovská Netherlands

Dongxing Zha United States

Fabio De Moliner United Kingdom

Cathleen Zeymer Germany

Richard Obexer

647 ×0.8

MB

163 ×0.5

OC

127 ×0.5

BE

192 ×1.3

MC

56 ×0.5

EEE

Citations per year, relative to Richard Obexer Richard Obexer (= 1×) peers Cathleen Zeymer

Countries citing papers authored by Richard Obexer

Since Specialization

Citations

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

Fields of papers citing papers by Richard Obexer

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Richard Obexer

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

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

1.

Meng, Qinglong, Charlotte Morrill, Ying Zhuo, et al.. (2025). Enzymatic synthesis of key RNA therapeutic building blocks using simple phosphate donors. Nature Communications. 17(1). 622–622.

2.

Crawshaw, Rebecca, Johannes Hofer, Florence J. Hardy, et al.. (2025). Efficient and selective energy transfer photoenzymes powered by visible light. Nature Chemistry. 17(7). 1083–1090. 9 indexed citations

3.

Hodgson, Lorna, Judith Mantell, Christopher R. Neal, et al.. (2024). Maturation and Conformational Switching of a De Novo Designed Phase-Separating Polypeptide. Journal of the American Chemical Society. 146(15). 10240–10245. 4 indexed citations

4.

Foster, Jake, Rebecca Crawshaw, Florence J. Hardy, et al.. (2024). A non-canonical nucleophile unlocks a new mechanistic pathway in a designed enzyme. Nature Communications. 15(1). 1956–1956. 20 indexed citations

5.

Obexer, Richard, et al.. (2024). Modern approaches to therapeutic oligonucleotide manufacturing. Science. 384(6692). eadl4015–eadl4015. 43 indexed citations

6.

Davidson, Joanne O., et al.. (2023). Engineering Enzymes for Environmental Sustainability. Angewandte Chemie. 135(52). 6 indexed citations

7.

Davidson, Joanne O., et al.. (2023). Engineering Enzymes for Environmental Sustainability. Angewandte Chemie International Edition. 62(52). e202309305–e202309305. 34 indexed citations

8.

Cross, Stephen, et al.. (2023). Assembling membraneless organelles from de novo designed proteins. Nature Chemistry. 16(1). 89–97. 42 indexed citations

9.

Crawshaw, Rebecca, Florence J. Hardy, Colin Levy, et al.. (2022). A designed photoenzyme for enantioselective [2+2] cycloadditions. Nature. 611(7937). 709–714. 149 indexed citations

10.

Nagano, Masanobu, Yichao Huang, Richard Obexer, & Hiroaki Suga. (2022). Chemical peptide macrolactonization via intramolecular S‐to‐S‐to‐O acyl transfer. Peptide Science. 114(4). 3 indexed citations

11.

Obexer, Richard, et al.. (2021). De novo macrocyclic peptides dissect energy coupling of a heterodimeric ABC transporter by multimode allosteric inhibition. eLife. 10. 13 indexed citations

12.

Nagano, Masanobu, Yichao Huang, Richard Obexer, & Hiroaki Suga. (2021). One-Pot In Vitro Ribosomal Synthesis of Macrocyclic Depsipeptides. Journal of the American Chemical Society. 143(12). 4741–4750. 13 indexed citations

13.

Pott, Moritz, Richard Obexer, Anthony P. Green, et al.. (2019). Ultrahigh-throughput screening enables efficient single-round oxidase remodelling. Nature Catalysis. 2(9). 740–747. 79 indexed citations

14.

Walport, Louise J., Richard Obexer, & Hiroaki Suga. (2017). Strategies for transitioning macrocyclic peptides to cell-permeable drug leads. Current Opinion in Biotechnology. 48. 242–250. 57 indexed citations

15.

Obexer, Richard, Louise J. Walport, & Hiroaki Suga. (2017). Exploring sequence space: harnessing chemical and biological diversity towards new peptide leads. Current Opinion in Chemical Biology. 38. 52–61. 67 indexed citations

16.

Obexer, Richard, Moritz Pott, Cathleen Zeymer, Andrew D. Griffiths, & Donald Hilvert. (2017). Efficient laboratory evolution of computationally designed enzymes with low starting activities using fluorescence-activated droplet sorting. Protein Engineering Design and Selection. 30(7). 531–531. 4 indexed citations

17.

Obexer, Richard, А. Т. Година, Xavier Garrabou, et al.. (2016). Emergence of a catalytic tetrad during evolution of a highly active artificial aldolase. Nature Chemistry. 9(1). 50–56. 253 indexed citations breakdown →

18.

Obexer, Richard, Lars Giger, Daniel M. Pinkas, et al.. (2014). Active Site Plasticity of a Computationally Designed Retro‐Aldolase Enzyme. ChemCatChem. 6(4). 1043–1050. 20 indexed citations

19.

Giger, Lars, S. Caner, Richard Obexer, et al.. (2013). Evolution of a designed retro-aldolase leads to complete active site remodeling. Nature Chemical Biology. 9(8). 494–498. 220 indexed citations

20.

Wörsdörfer, Bigna, et al.. (2012). Harnessing Protein Symmetry for Enzyme Design. ACS Catalysis. 2(6). 982–985. 17 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.

Explore authors with similar magnitude of impact