Stefan Hofbauer

1.7k total citations
66 papers, 1.3k citations indexed

About

Stefan Hofbauer is a scholar working on Molecular Biology, Health, Toxicology and Mutagenesis and Cell Biology. According to data from OpenAlex, Stefan Hofbauer has authored 66 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 45 papers in Molecular Biology, 19 papers in Health, Toxicology and Mutagenesis and 19 papers in Cell Biology. Recurrent topics in Stefan Hofbauer's work include Porphyrin Metabolism and Disorders (34 papers), Chemical Analysis and Environmental Impact (19 papers) and Hemoglobin structure and function (17 papers). Stefan Hofbauer is often cited by papers focused on Porphyrin Metabolism and Disorders (34 papers), Chemical Analysis and Environmental Impact (19 papers) and Hemoglobin structure and function (17 papers). Stefan Hofbauer collaborates with scholars based in Austria, Italy and Slovenia. Stefan Hofbauer's co-authors include Christian Obinger, Paul G. Furtmüller, Irene Schaffner, Katharina F. Pirker, Kristina Djinović‐Carugo, Vera Pfanzagl, Monika Soudi, Georg Mlynek, Giulietta Smulevich and Marcel Zámocký and has published in prestigious journals such as Journal of Biological Chemistry, SHILAP Revista de lepidopterología and Biochemistry.

In The Last Decade

Stefan Hofbauer

65 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Stefan Hofbauer Austria 23 686 269 258 224 183 66 1.3k
Marzia Bellei Italy 21 490 0.7× 142 0.5× 133 0.5× 189 0.8× 193 1.1× 44 1.0k
Irene Schaffner Austria 13 287 0.4× 173 0.6× 81 0.3× 77 0.3× 101 0.6× 17 590
Stefano M. Marino United States 22 1.3k 1.9× 75 0.3× 221 0.9× 130 0.6× 73 0.4× 27 1.9k
Georg Mlynek Austria 17 450 0.7× 218 0.8× 95 0.4× 43 0.2× 55 0.3× 29 761
Jolanda Van der Zee Netherlands 19 433 0.6× 84 0.3× 115 0.4× 47 0.2× 69 0.4× 36 1.2k
Xiangshi Tan China 20 604 0.9× 29 0.1× 328 1.3× 82 0.4× 59 0.3× 70 1.0k
John I. Toohey United States 19 1.0k 1.5× 66 0.2× 78 0.3× 69 0.3× 155 0.8× 33 1.8k
K. G. Paul Sweden 18 852 1.2× 52 0.2× 505 2.0× 103 0.5× 214 1.2× 56 1.5k
Hiroki Inoue Japan 22 597 0.9× 245 0.9× 74 0.3× 39 0.2× 147 0.8× 51 1.7k
Rajib Sengupta India 20 980 1.4× 37 0.1× 78 0.3× 99 0.4× 135 0.7× 49 1.5k

Countries citing papers authored by Stefan Hofbauer

Since Specialization
Citations

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

Fields of papers citing papers by Stefan Hofbauer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Stefan Hofbauer

This figure shows the co-authorship network connecting the top 25 collaborators of Stefan Hofbauer. A scholar is included among the top collaborators of Stefan Hofbauer 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 Stefan Hofbauer. Stefan Hofbauer 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.
Bellei, Marzia, Federico Sebastiani, Maurizio Becucci, et al.. (2024). Revisiting catalytic His and Glu residues in coproporphyrin ferrochelatase – unexpected activities of active site variants. FEBS Journal. 291(10). 2260–2272. 2 indexed citations
2.
Sebastiani, Federico, Diego M. Moreno, Darío A. Estrı́n, et al.. (2024). Proximal ligand tunes active site structure and reactivity in bacterial L. monocytogenes coproheme ferrochelatase. Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy. 313. 124120–124120. 1 indexed citations
3.
Furtmüller, Paul G., et al.. (2023). Reactivity of Coproheme Decarboxylase with Monovinyl, Monopropionate Deuteroheme. Biomolecules. 13(6). 946–946. 2 indexed citations
4.
Sebastiani, Federico, et al.. (2023). The role of the distal cavity in carbon monoxide stabilization in the coproheme decarboxylase enzyme from C. diphtheriae. Journal of Inorganic Biochemistry. 245. 112243–112243. 2 indexed citations
5.
Paumann-Page, Martina, Irada Khalilova, Nicholas J. Magon, et al.. (2023). Hypochlorous acid inactivates myeloperoxidase inside phagocytosing neutrophils. SHILAP Revista de lepidopterología. 5-6. 100008–100008. 7 indexed citations
6.
7.
Schmidt, Daniel, Marzia Bellei, Vera Pfanzagl, et al.. (2023). Compound I Formation and Reactivity in Dimeric Chlorite Dismutase: Impact of pH and the Dynamics of the Catalytic Arginine. Biochemistry. 62(3). 835–850. 2 indexed citations
8.
Sebastiani, Federico, Paul G. Furtmüller, Vera Pfanzagl, et al.. (2022). Active site architecture of coproporphyrin ferrochelatase with its physiological substrate coproporphyrin III: Propionate interactions and porphyrin core deformation. Protein Science. 32(1). e4534–e4534. 10 indexed citations
9.
10.
Hofbauer, Stefan, Marco Borsari, Carlo Augusto Bortolotti, et al.. (2021). Pseudoperoxidase activity, conformational stability, and aggregation propensity of the His98Tyr myoglobin variant: implications for the onset of myoglobinopathy. FEBS Journal. 289(4). 1105–1117. 2 indexed citations
11.
Hofbauer, Stefan, et al.. (2020). Understanding molecular enzymology of porphyrin-binding α + β barrel proteins - One fold, multiple functions. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1869(1). 140536–140536. 27 indexed citations
12.
Paumann-Page, Martina, Vera Pfanzagl, Marcel Zámocký, et al.. (2018). Posttranslational modification of heme in peroxidases – Impact on structure and catalysis. Archives of Biochemistry and Biophysics. 643. 14–23. 18 indexed citations
13.
Pfanzagl, Vera, Marzia Bellei, Georg Mlynek, et al.. (2018). Roles of distal aspartate and arginine of B-class dye-decolorizing peroxidase in heterolytic hydrogen peroxide cleavage. Journal of Biological Chemistry. 293(38). 14823–14838. 46 indexed citations
14.
Grishkovskaya, Irina, Martina Paumann-Page, Rupert Tscheließnig, et al.. (2017). Structure of human promyeloperoxidase (proMPO) and the role of the propeptide in processing and maturation. Journal of Biological Chemistry. 292(20). 8244–8261. 42 indexed citations
15.
Hofbauer, Stefan, Georg Mlynek, Lisa Milazzo, et al.. (2016). Hydrogen peroxide‐mediated conversion of coproheme to heme b by HemQ—lessons from the first crystal structure and kinetic studies. FEBS Journal. 283(23). 4386–4401. 35 indexed citations
16.
Chromikova, Veronika, Stefan Hofbauer, Christoph Göbl, et al.. (2015). Introduction of germline residues improves the stability of anti-HIV mAb 2G12-IgM. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1854(10). 1536–1544. 6 indexed citations
17.
Zámocký, Marcel, Stefan Hofbauer, Irene Schaffner, et al.. (2015). Independent evolution of four heme peroxidase superfamilies. Archives of Biochemistry and Biophysics. 574. 108–119. 178 indexed citations
18.
Hofbauer, Stefan, Irene Schaffner, Georg Mlynek, et al.. (2015). Structure and heme-binding properties of HemQ (chlorite dismutase-like protein) from Listeria monocytogenes. Archives of Biochemistry and Biophysics. 574. 36–48. 39 indexed citations
19.
Hofbauer, Stefan, Irene Schaffner, Paul G. Furtmüller, & Christian Obinger. (2014). Chlorite dismutases – a heme enzyme family for use in bioremediation and generation of molecular oxygen. Biotechnology Journal. 9(4). 461–473. 51 indexed citations
20.
Grünwald‐Gruber, Clemens, Marzia Bellei, Katharina F. Pirker, et al.. (2013). A Stable Bacterial Peroxidase with Novel Halogenating Activity and an Autocatalytically Linked Heme Prosthetic Group. Journal of Biological Chemistry. 288(38). 27181–27199. 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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