Matthew D. Truppo

3.8k total citations · 1 hit paper
28 papers, 2.1k citations indexed

About

Matthew D. Truppo is a scholar working on Molecular Biology, Organic Chemistry and Biomedical Engineering. According to data from OpenAlex, Matthew D. Truppo has authored 28 papers receiving a total of 2.1k indexed citations (citations by other indexed papers that have themselves been cited), including 24 papers in Molecular Biology, 9 papers in Organic Chemistry and 8 papers in Biomedical Engineering. Recurrent topics in Matthew D. Truppo's work include Enzyme Catalysis and Immobilization (20 papers), Microbial Metabolic Engineering and Bioproduction (8 papers) and Chemical Synthesis and Analysis (7 papers). Matthew D. Truppo is often cited by papers focused on Enzyme Catalysis and Immobilization (20 papers), Microbial Metabolic Engineering and Bioproduction (8 papers) and Chemical Synthesis and Analysis (7 papers). Matthew D. Truppo collaborates with scholars based in United States and United Kingdom. Matthew D. Truppo's co-authors include Nicholas J. Turner, J. David Rozzell, Paul N. Devine, Matthew P. Thompson, David Pollard, Roger M. Howard, Rajesh Kumar, Gregory Hughes, Jeffrey C. Moore and Kevin R. Campos and has published in prestigious journals such as Science, Angewandte Chemie International Edition and Chemical Communications.

In The Last Decade

Matthew D. Truppo

28 papers receiving 2.1k 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.

The importance of synthetic chemistry in the pharmaceutical industry

2019 454 citations Kevin R. Campos, Paul J. Coleman et al. Science profile →

Peers

Matthew D. Truppo

Fred J. Fleitz United States

Birgit Kosjek United States

Scott P. France United Kingdom

Hans Iding Switzerland

Diego Ghislieri United Kingdom

Christopher K. Savile Canada

Tanja Knaus Netherlands

Bettina M. Nestl Germany

Robert C. Simon Austria

Xianfu Lin China

Fred J. Fleitz United States

Matthew D. Truppo

1.3k ×0.9

954 ×1.1

305 ×0.6

219 ×0.9

210 ×1.1

Citations per year, relative to Matthew D. Truppo Matthew D. Truppo (= 1×) peers Fred J. Fleitz

Countries citing papers authored by Matthew D. Truppo

Since Specialization

Citations

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

Fields of papers citing papers by Matthew D. Truppo

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Matthew D. Truppo. 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 Matthew D. Truppo. The network helps show where Matthew D. Truppo may publish in the future.

Co-authorship network of co-authors of Matthew D. Truppo

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

All Works

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20 of 20 papers shown

Jiao, Qun, Tong‐Yuan Yang, M. Jack Borrok, et al.. (2021). Bifunctional molecules targeting SARS-CoV-2 spike and the polymeric Ig receptor display neutralization activity and mucosal enrichment. mAbs. 13(1). 1987180–1987180. 4 indexed citations

Campos, Kevin R., Paul J. Coleman, Juan C. Alvarez, et al.. (2019). The importance of synthetic chemistry in the pharmaceutical industry. Science. 363(6424). 454 indexed citations breakdown →

Moore, Jeffrey C., Agustina Rodriguez-Granillo, Alejandro Crespo, et al.. (2018). “Site and Mutation”-Specific Predictions Enable Minimal Directed Evolution Libraries. ACS Synthetic Biology. 7(7). 1730–1741. 26 indexed citations

Devine, Paul N., Roger M. Howard, Rajesh Kumar, et al.. (2018). Extending the application of biocatalysis to meet the challenges of drug development. Nature Reviews Chemistry. 2(12). 409–421. 327 indexed citations

Xu, Feng, Hongming Li, Ji Qi, et al.. (2017). Asymmetric Synthesis of Functionalizedtrans-Cyclopropoxy Building Block for Grazoprevir. Organic Letters. 19(21). 5880–5883. 11 indexed citations

Truppo, Matthew D.. (2017). Biocatalysis in the Pharmaceutical Industry: The Need for Speed. ACS Medicinal Chemistry Letters. 8(5). 476–480. 278 indexed citations

Kelly, Paul P., Derek J. Quinn, Ken Lemon, et al.. (2016). Ene Reductase Enzymes for the Aromatisation of Tetralones and Cyclohexenones to Naphthols and Phenols. Advanced Synthesis & Catalysis. 358(5). 731–736. 11 indexed citations

Li, Hongmei, et al.. (2015). Development of an Immobilized Ketoreductase for Enzymatic (R)-1-(3,5-Bis(trifluoromethyl)phenyl)ethanol Production. Organic Process Research & Development. 19(7). 695–700. 40 indexed citations

Kuethe, Jeffrey T., et al.. (2014). A biocatalytic/reductive etherification approach to substituted piperidinyl ethers. Tetrahedron. 70(30). 4563–4570. 4 indexed citations

10.

Truppo, Matthew D. & Gregory Hughes. (2011). Development of an Improved Immobilized CAL-B for the Enzymatic Resolution of a Key Intermediate to Odanacatib. Organic Process Research & Development. 15(5). 1033–1035. 38 indexed citations

11.

Truppo, Matthew D., et al.. (2010). A fast and sensitive assay for measuring the activity and enantioselectivity of transaminases. Chemical Communications. 47(2). 773–775. 42 indexed citations

12.

Truppo, Matthew D. & Nicholas J. Turner. (2010). Micro-scale process development of transaminase catalysed reactions. Organic & Biomolecular Chemistry. 8(6). 1280–1280. 39 indexed citations

13.

Truppo, Matthew D., Nicholas J. Turner, & J. David Rozzell. (2009). Efficient kinetic resolution of racemic amines using a transaminase in combination with an amino acid oxidase. Chemical Communications. 2127–2127. 93 indexed citations

14.

Truppo, Matthew D., J. David Rozzell, & Nicholas J. Turner. (2009). Efficient Production of Enantiomerically Pure Chiral Amines at Concentrations of 50 g/L Using Transaminases. Organic Process Research & Development. 14(1). 234–237. 123 indexed citations

15.

Truppo, Matthew D., Franck Escalettes, & Nicholas J. Turner. (2008). Rapid Determination of Both the Activity and Enantioselectivity of Ketoreductases. Angewandte Chemie International Edition. 47(14). 2639–2641. 22 indexed citations

16.

Truppo, Matthew D., J. David Rozzell, Jeffrey C. Moore, & Nicholas J. Turner. (2008). Rapid screening and scale-up of transaminase catalysed reactions. Organic & Biomolecular Chemistry. 7(2). 395–398. 129 indexed citations

17.

Jen, Wendy S., Matthew D. Truppo, Paul N. Devine, et al.. (2008). Copper-Catalyzed Synthesis of Enantioenriched Tetraarylethanes. Organic Letters. 10(5). 741–744. 17 indexed citations

18.

Truppo, Matthew D., Franck Escalettes, & Nicholas J. Turner. (2008). Rapid Determination of Both the Activity and Enantioselectivity of Ketoreductases. Angewandte Chemie. 120(14). 2679–2681. 5 indexed citations

19.

Truppo, Matthew D., David Pollard, Jeffrey C. Moore, & Paul N. Devine. (2007). Production of (S)-γ-fluoroleucine ethyl ester by enzyme mediated dynamic kinetic resolution: Comparison of batch and fed batch stirred tank processes to a packed bed column reactor. Chemical Engineering Science. 63(1). 122–130. 12 indexed citations

20.

Truppo, Matthew D., Michel Journet, Ali Shafiee, & Jeffrey C. Moore. (2006). Optimization and Scale-Up of a Lipase-Catalyzed Enzymatic Resolution of an Indole Ester Intermediate for a Prostaglandin D₂(DP) Receptor Antagonist Targeting Allergic Rhinitis. Organic Process Research & Development. 10(3). 592–598. 2 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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