Michela M. Pellizzoni

1.5k total citations · 1 hit paper
21 papers, 1.2k citations indexed

About

Michela M. Pellizzoni is a scholar working on Organic Chemistry, Molecular Biology and Inorganic Chemistry. According to data from OpenAlex, Michela M. Pellizzoni has authored 21 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 15 papers in Organic Chemistry, 12 papers in Molecular Biology and 10 papers in Inorganic Chemistry. Recurrent topics in Michela M. Pellizzoni's work include Asymmetric Hydrogenation and Catalysis (9 papers), Chemical Synthesis and Analysis (8 papers) and Cyclopropane Reaction Mechanisms (7 papers). Michela M. Pellizzoni is often cited by papers focused on Asymmetric Hydrogenation and Catalysis (9 papers), Chemical Synthesis and Analysis (8 papers) and Cyclopropane Reaction Mechanisms (7 papers). Michela M. Pellizzoni collaborates with scholars based in Switzerland, Italy and United Kingdom. Michela M. Pellizzoni's co-authors include Thomas R. Ward, Valentin Köhler, Tillmann Heinisch, Fabian Schwizer, Yasunori Okamoto, Yifan Gu, Vincent Lebrun, Jared C. Lewis, Raphael Reuter and Giorgio Facchetti and has published in prestigious journals such as Chemical Reviews, Journal of the American Chemical Society and Chemical Communications.

In The Last Decade

Michela M. Pellizzoni

20 papers receiving 1.2k 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.

Artificial Metalloenzymes: Reaction Scope and Optimization Strategies

2017 651 citations Fabian Schwizer, Yasunori Okamoto et al. Chemical Reviews profile →

Peers

Michela M. Pellizzoni

RESE

Fabian Schwizer Switzerland

Vincent Lebrun France

Yvonne M. Wilson Switzerland

Yifan Gu China

Raphael Reuter Switzerland

Marc Dürrenberger Switzerland

Anca Pordea United Kingdom

Julieta Gradinaru Switzerland

Brian V. Popp United States

Marc Creus Switzerland

Fabian Schwizer Switzerland

Michela M. Pellizzoni

545 ×0.9

552 ×1.0

252 ×0.8

171 ×0.9

155 ×0.9

RESE

Citations per year, relative to Michela M. Pellizzoni Michela M. Pellizzoni (= 1×) peers Fabian Schwizer

Countries citing papers authored by Michela M. Pellizzoni

Since Specialization

Citations

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

Fields of papers citing papers by Michela M. Pellizzoni

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Michela M. Pellizzoni. 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 Michela M. Pellizzoni. The network helps show where Michela M. Pellizzoni may publish in the future.

Co-authorship network of co-authors of Michela M. Pellizzoni

This figure shows the co-authorship network connecting the top 25 collaborators of Michela M. Pellizzoni. A scholar is included among the top collaborators of Michela M. Pellizzoni 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 Michela M. Pellizzoni. Michela M. Pellizzoni 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

Pellizzoni, Michela M., et al.. (2022). Author Correction: Design and evolution of chimeric streptavidin for protein-enabled dual gold catalysis. Nature Catalysis. 5(4). 354–354.

Guo, Chao, et al.. (2022). Peroxidase Activity of Myoglobin Variants Reconstituted with Artificial Cofactors. ChemBioChem. 23(18). e202200197–e202200197. 8 indexed citations

Guo, Chao, et al.. (2022). Engineered myoglobin as a catalyst for atom transfer radical cyclisation. Chemical Communications. 58(78). 10989–10992. 8 indexed citations

Vornholt, Tobias, et al.. (2021). Systematic engineering of artificial metalloenzymes for new-to-nature reactions. Science Advances. 7(4). 62 indexed citations

Pellizzoni, Michela M., et al.. (2021). Design and evolution of chimeric streptavidin for protein-enabled dual gold catalysis. Nature Catalysis. 4(8). 643–653. 51 indexed citations

Balog, Sandor, et al.. (2020). Rapid quantification of the malaria biomarker hemozoin by improved biocatalytically initiated precipitation atom transfer radical polymerizations. The Analyst. 145(23). 7741–7751. 5 indexed citations

Pellizzoni, Michela M., et al.. (2019). Enzyme-initiated free radical polymerizations of vinyl monomers using horseradish peroxidase. Methods in enzymology on CD-ROM/Methods in enzymology. 627. 249–262. 10 indexed citations

Pellizzoni, Michela M., et al.. (2019). Biocatalytic ATRP in solution and on surfaces. Methods in enzymology on CD-ROM/Methods in enzymology. 627. 263–290. 1 indexed citations

Pellizzoni, Michela M., et al.. (2018). Repurposing Biocatalysts to Control Radical Polymerizations. ACS Macro Letters. 7(9). 1111–1119. 52 indexed citations

10.

Zhao, Jingming, Johannes G. Rebelein, Hendrik Mallin, et al.. (2018). Genetic Engineering of an Artificial Metalloenzyme for Transfer Hydrogenation of a Self-Immolative Substrate in Escherichia coli’s Periplasm. Journal of the American Chemical Society. 140(41). 13171–13175. 57 indexed citations

11.

Pellizzoni, Michela M., Fabian Schwizer, Christopher W. Wood, et al.. (2018). Chimeric Streptavidins as Host Proteins for Artificial Metalloenzymes. ACS Catalysis. 8(2). 1476–1484. 31 indexed citations

12.

Schwizer, Fabian, Yasunori Okamoto, Tillmann Heinisch, et al.. (2017). Artificial Metalloenzymes: Reaction Scope and Optimization Strategies. Chemical Reviews. 118(1). 142–231. 651 indexed citations breakdown →

13.

Pellizzoni, Michela M., Giorgio Facchetti, Raffaella Gandolfi, et al.. (2016). Evaluation of Chemical Diversity of Biotinylated Chiral 1,3‐Diamines as a Catalytic Moiety in Artificial Imine Reductase. ChemCatChem. 8(9). 1665–1670. 26 indexed citations

14.

Heinisch, Tillmann, Michela M. Pellizzoni, Marc Dürrenberger, et al.. (2015). Improving the Catalytic Performance of an Artificial Metalloenzyme by Computational Design. Journal of the American Chemical Society. 137(32). 10414–10419. 72 indexed citations

15.

Facchetti, Giorgio, Raffaella Gandolfi, Marco Fusè, et al.. (2015). Simple 1,3-diamines and their application as ligands in ruthenium(ii) catalysts for asymmetric transfer hydrogenation of aryl ketones. New Journal of Chemistry. 39(5). 3792–3800. 23 indexed citations

16.

Facchetti, Giorgio, Marco Fusè, Michela M. Pellizzoni, et al.. (2014). 8-Amino-5,6,7,8-tetrahydroquinolines as ligands in iridium(III) catalysts for the reduction of aryl ketones by asymmetric transfer hydrogenation (ATH). Tetrahedron Asymmetry. 25(13-14). 1031–1037. 24 indexed citations

17.

Ferri, Nicola, Stefano Cazzaniga, Luca Mazzarella, et al.. (2013). Cytotoxic effect of (1-methyl-1H-imidazol-2-yl)-methanamine and its derivatives in PtII complexes on human carcinoma cell lines: A comparative study with cisplatin. Bioorganic & Medicinal Chemistry. 21(8). 2379–2386. 22 indexed citations

18.

Rimoldi, Isabella, et al.. (2012). Enantioselective Transfer Hydrogenation of Aryl Ketones: Synthesis and 2D-NMR Characterization of New 8-amino-5,6,7,8-tetrahydroquinoline Ru(II)-complexes. Current Organic Chemistry. 16(24). 2982–2988. 17 indexed citations

19.

Facchetti, Giorgio, et al.. (2012). “In situ” Activation of Racemic Ru^II Complexes: Separation of trans and cis Species and Their Application in Asymmetric Reduction. European Journal of Inorganic Chemistry. 2012(27). 4365–4370. 18 indexed citations

20.

Rimoldi, Isabella, et al.. (2011). Chemo- and biocatalytic strategies to obtain phenylisoserine, a lateral chain of Taxol by asymmetric reduction. Tetrahedron Asymmetry. 22(24). 2110–2116. 16 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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