Mary C. Andorfer

974 total citations
21 papers, 698 citations indexed

About

Mary C. Andorfer is a scholar working on Molecular Biology, Organic Chemistry and Biochemistry. According to data from OpenAlex, Mary C. Andorfer has authored 21 papers receiving a total of 698 indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 7 papers in Organic Chemistry and 6 papers in Biochemistry. Recurrent topics in Mary C. Andorfer's work include Amino Acid Enzymes and Metabolism (6 papers), Enzyme Catalysis and Immobilization (6 papers) and Metalloenzymes and iron-sulfur proteins (6 papers). Mary C. Andorfer is often cited by papers focused on Amino Acid Enzymes and Metabolism (6 papers), Enzyme Catalysis and Immobilization (6 papers) and Metalloenzymes and iron-sulfur proteins (6 papers). Mary C. Andorfer collaborates with scholars based in United States, Austria and Canada. Mary C. Andorfer's co-authors include Jared C. Lewis, James T. Payne, Catherine B. Poor, Brian F. Fisher, Krysten A. Jones, Catherine L. Drennan, Piro Siuti, Jonathan E. Grob, Kian L. Tan and Christine E. Hajdin and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

Mary C. Andorfer

19 papers receiving 696 citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Mary C. Andorfer United States 13 319 297 154 116 97 21 698
Jonathan Latham United Kingdom 8 415 1.3× 383 1.3× 195 1.3× 74 0.6× 118 1.2× 10 807
Eugenio P. Patallo Germany 13 412 1.3× 310 1.0× 118 0.8× 81 0.7× 253 2.6× 19 725
Eileen Brandenburger Germany 8 225 0.7× 218 0.7× 102 0.7× 61 0.5× 185 1.9× 9 565
Hannes Leisch Canada 15 485 1.5× 361 1.2× 88 0.6× 57 0.5× 78 0.8× 25 826
Clemens Stueckler Austria 13 840 2.6× 250 0.8× 178 1.2× 43 0.4× 47 0.5× 16 939
Christian Schnepel United Kingdom 13 397 1.2× 293 1.0× 79 0.5× 47 0.4× 79 0.8× 24 627
Hannah Minges Germany 9 248 0.8× 182 0.6× 79 0.5× 57 0.5× 50 0.5× 10 455
Rainer Stuermer Austria 9 645 2.0× 197 0.7× 136 0.9× 35 0.3× 38 0.4× 12 777
Mark L. Thompson United Kingdom 11 500 1.6× 174 0.6× 38 0.2× 28 0.2× 104 1.1× 16 703
Richiro Ushimaru Japan 14 278 0.9× 326 1.1× 306 2.0× 19 0.2× 143 1.5× 38 677

Countries citing papers authored by Mary C. Andorfer

Since Specialization
Citations

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

Fields of papers citing papers by Mary C. Andorfer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Mary C. Andorfer. 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 Mary C. Andorfer. The network helps show where Mary C. Andorfer may publish in the future.

Co-authorship network of co-authors of Mary C. Andorfer

This figure shows the co-authorship network connecting the top 25 collaborators of Mary C. Andorfer. A scholar is included among the top collaborators of Mary C. Andorfer 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 Mary C. Andorfer. Mary C. Andorfer 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.
Vats, Arpita, et al.. (2025). Activation of X-Succinate Synthases for Fumarate Hydroalkylation Using an In Vitro Activation Method. BIO-PROTOCOL. 15(1374). e5357–e5357. 1 indexed citations
2.
Liu, Jian, et al.. (2025). Accessory Subunit Regulates Thiyl Radical Formation in Benzylsuccinate Synthase. Biochemistry. 64(21). 4414–4423.
3.
Andorfer, Mary C., et al.. (2023). Development of an in vitro method for activation of X-succinate synthases for fumarate hydroalkylation. iScience. 26(6). 106902–106902. 3 indexed citations
4.
Bian, Ke, Mary C. Andorfer, Catherine L. Drennan, et al.. (2022). A haem-sequestering plant peptide promotes iron uptake in symbiotic bacteria. Nature Microbiology. 7(9). 1453–1465. 40 indexed citations
5.
Andorfer, Mary C., Declan Evans, Cyndi Qixin He, et al.. (2022). Analysis of laboratory-evolved flavin-dependent halogenases affords a computational model for predicting halogenase site selectivity. Chem Catalysis. 2(10). 2658–2674. 14 indexed citations
6.
Andorfer, Mary C., et al.. (2021). Rescuing activity of oxygen-damaged pyruvate formate-lyase by a spare part protein. Journal of Biological Chemistry. 297(6). 101423–101423. 7 indexed citations
7.
Huang, Yolanda Y., Mary C. Andorfer, Brian Gold, et al.. (2020). Molecular basis for catabolism of the abundant metabolite trans-4-hydroxy-L-proline by a microbial glycyl radical enzyme. eLife. 9. 18 indexed citations
8.
Bowman, Sarah, et al.. (2019). Solution structure and biochemical characterization of a spare part protein that restores activity to an oxygen-damaged glycyl radical enzyme. JBIC Journal of Biological Inorganic Chemistry. 24(6). 817–829. 12 indexed citations
9.
Fisher, Brian F., et al.. (2019). Site-Selective C–H Halogenation Using Flavin-Dependent Halogenases Identified via Family-Wide Activity Profiling. ACS Central Science. 5(11). 1844–1856. 81 indexed citations
10.
Andorfer, Mary C. & Jared C. Lewis. (2018). Understanding and Improving the Activity of Flavin-Dependent Halogenases via Random and Targeted Mutagenesis. Annual Review of Biochemistry. 87(1). 159–185. 68 indexed citations
11.
Andorfer, Mary C., et al.. (2017). Aromatic Halogenation by Using Bifunctional Flavin Reductase–Halogenase Fusion Enzymes. ChemBioChem. 18(21). 2099–2103. 35 indexed citations
12.
Andorfer, Mary C., Jonathan E. Grob, Christine E. Hajdin, et al.. (2017). Understanding Flavin-Dependent Halogenase Reactivity via Substrate Activity Profiling. ACS Catalysis. 7(3). 1897–1904. 61 indexed citations
13.
Andorfer, Mary C., et al.. (2016). Directed evolution of RebH for catalyst-controlled halogenation of indole C–H bonds. Chemical Science. 7(6). 3720–3729. 80 indexed citations
14.
Andorfer, Mary C., et al.. (2016). A Simple Combinatorial Codon Mutagenesis Method for Targeted Protein Engineering. ACS Synthetic Biology. 6(3). 416–420. 25 indexed citations
15.
Payne, James T., Mary C. Andorfer, & Jared C. Lewis. (2016). Engineering Flavin-Dependent Halogenases. Methods in enzymology on CD-ROM/Methods in enzymology. 575. 93–126. 13 indexed citations
16.
Poor, Catherine B., Mary C. Andorfer, & Jared C. Lewis. (2014). Improving the Stability and Catalyst Lifetime of the Halogenase RebH By Directed Evolution. ChemBioChem. 15(9). 1286–1289. 75 indexed citations
17.
Payne, James T., Mary C. Andorfer, & Jared C. Lewis. (2013). Regioselective Arene Halogenation using the FAD‐Dependent Halogenase RebH. Angewandte Chemie. 125(20). 5379–5382. 40 indexed citations
18.
Payne, James T., Mary C. Andorfer, & Jared C. Lewis. (2013). Regioselective Arene Halogenation using the FAD‐Dependent Halogenase RebH. Angewandte Chemie International Edition. 52(20). 5271–5274. 123 indexed citations
19.
Johnson, R. Jeremy, Mary C. Andorfer, Lauren Garnett, et al.. (2011). Proteopedia entry: Bovine pancreatic ribonuclease a. Biochemistry and Molecular Biology Education. 40(1). 75–75. 1 indexed citations
20.
Zwölfer, W., M. Hiesmayr, Mary C. Andorfer, et al.. (1989). Myocardial metabolism during infusion of glucose-insulin-potassium before coronary artery bypass grafting. Journal of Cardiothoracic Anesthesia. 3(5). 46–46.

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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