Hans‐Lothar Fuchsbauer

1.1k total citations
37 papers, 910 citations indexed

About

Hans‐Lothar Fuchsbauer is a scholar working on Molecular Biology, Pulmonary and Respiratory Medicine and Biotechnology. According to data from OpenAlex, Hans‐Lothar Fuchsbauer has authored 37 papers receiving a total of 910 indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 19 papers in Pulmonary and Respiratory Medicine and 14 papers in Biotechnology. Recurrent topics in Hans‐Lothar Fuchsbauer's work include Blood properties and coagulation (19 papers), Protein purification and stability (11 papers) and Enzyme Production and Characterization (11 papers). Hans‐Lothar Fuchsbauer is often cited by papers focused on Blood properties and coagulation (19 papers), Protein purification and stability (11 papers) and Enzyme Production and Characterization (11 papers). Hans‐Lothar Fuchsbauer collaborates with scholars based in Germany, United States and France. Hans‐Lothar Fuchsbauer's co-authors include Ralf Pasternack, Jens Zotzel, Patricia J. Keller, Simone Dorsch, Sabine Wolf, Harald Kolmar, Helmut Quast, Susan Y. Schmidt, Frank Adolf and Arthur J.L. Cooper and has published in prestigious journals such as Journal of Biological Chemistry, Angewandte Chemie International Edition and PLoS ONE.

In The Last Decade

Hans‐Lothar Fuchsbauer

37 papers receiving 888 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Hans‐Lothar Fuchsbauer Germany 19 459 419 309 193 86 37 910
Masayo Date Japan 12 624 1.4× 115 0.3× 174 0.6× 90 0.5× 70 0.8× 18 875
Marion Hoffmann Germany 14 279 0.6× 69 0.2× 88 0.3× 620 3.2× 39 0.5× 26 1.1k
Yanyun Gao China 16 345 0.8× 185 0.4× 90 0.3× 30 0.2× 17 0.2× 49 869
Kohta Kurohane Japan 16 251 0.5× 177 0.4× 82 0.3× 17 0.1× 63 0.7× 53 863
J. Steven Stanley United States 12 280 0.6× 33 0.1× 235 0.8× 104 0.5× 83 1.0× 15 1.6k
Zengpeng Li China 17 543 1.2× 46 0.1× 87 0.3× 34 0.2× 45 0.5× 52 904
Susumu Nagasaki Japan 13 256 0.6× 113 0.3× 115 0.4× 24 0.1× 38 0.4× 74 660
Jingyao Qu United States 22 1.2k 2.5× 56 0.1× 198 0.6× 27 0.1× 92 1.1× 44 1.5k
Kęstutis Sužiedėlis Lithuania 16 526 1.1× 57 0.1× 38 0.1× 37 0.2× 62 0.7× 48 920
Raphaël Culerrier France 19 378 0.8× 36 0.1× 122 0.4× 78 0.4× 37 0.4× 40 972

Countries citing papers authored by Hans‐Lothar Fuchsbauer

Since Specialization
Citations

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

Fields of papers citing papers by Hans‐Lothar Fuchsbauer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Hans‐Lothar Fuchsbauer. 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 Hans‐Lothar Fuchsbauer. The network helps show where Hans‐Lothar Fuchsbauer may publish in the future.

Co-authorship network of co-authors of Hans‐Lothar Fuchsbauer

This figure shows the co-authorship network connecting the top 25 collaborators of Hans‐Lothar Fuchsbauer. A scholar is included among the top collaborators of Hans‐Lothar Fuchsbauer 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 Hans‐Lothar Fuchsbauer. Hans‐Lothar Fuchsbauer 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.
Ebenig, Aileen, et al.. (2019). Biochemical study of sortase E2 from Streptomyces mobaraensis and determination of transglutaminase cross‐linking sites. FEBS Letters. 593(15). 1944–1956. 2 indexed citations
2.
Kolmar, Harald, et al.. (2019). The metal-binding properties of the long chaplin from Streptomyces mobaraensis: A bioinformatic and biochemical approach. Journal of Inorganic Biochemistry. 202. 110878–110878. 2 indexed citations
3.
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5.
Meyners, Christian, et al.. (2018). Features of the transglutaminase-activating metalloprotease from Streptomyces mobaraensis DSM 40847 produced in Escherichia coli. Journal of Biotechnology. 281. 115–122. 9 indexed citations
6.
Schmelz, Stefan, et al.. (2018). Illuminating structure and acyl donor sites of a physiological transglutaminase substrate from Streptomyces mobaraensis. Protein Science. 27(5). 910–922. 17 indexed citations
7.
Schmelz, Stefan, Aileen Ebenig, Sabrina Fröls, et al.. (2016). Structure of the Dispase Autolysis-inducing Protein from Streptomyces mobaraensis and Glutamine Cross-linking Sites for Transglutaminase. Journal of Biological Chemistry. 291(39). 20417–20426. 20 indexed citations
8.
Krämer, Andreas, et al.. (2016). Involvement of a Novel Class C Beta-Lactamase in the Transglutaminase Mediated Cross-Linking Cascade of Streptomyces mobaraensis DSM 40847. PLoS ONE. 11(2). e0149145–e0149145. 8 indexed citations
9.
Schmelz, Stefan, Stephan Dickgießer, Aileen Ebenig, et al.. (2015). Locked by Design: A Conformationally Constrained Transglutaminase Tag Enables Efficient Site‐Specific Conjugation. Angewandte Chemie International Edition. 54(45). 13420–13424. 47 indexed citations
10.
Albert, Markus, et al.. (2010). Significance of Cuscutain, a cysteine protease from Cuscuta reflexa, in host-parasite interactions. BMC Plant Biology. 10(1). 227–227. 24 indexed citations
11.
Schmidt, Susan Y., et al.. (2009). A Novel Transglutaminase Substrate fromStreptomyces mobaraensisTriggers Autolysis of Neutral Metalloproteases. Bioscience Biotechnology and Biochemistry. 73(5). 993–999. 14 indexed citations
12.
Schmidt, Susan Y., Frank Adolf, & Hans‐Lothar Fuchsbauer. (2008). The transglutaminase activating metalloprotease inhibitor from Streptomyces mobaraensis is a glutamine and lysine donor substrate of the intrinsic transglutaminase. FEBS Letters. 582(20). 3132–3138. 28 indexed citations
13.
Pfleiderer, Christa, et al.. (2005). Inhibition of bacterial transglutaminase by its heat-treated pro-enzyme. Microbiological Research. 160(3). 265–271. 9 indexed citations
14.
Zotzel, Jens, Patricia J. Keller, & Hans‐Lothar Fuchsbauer. (2003). Transglutaminase from Streptomyces mobaraensis is activated by an endogenous metalloprotease. European Journal of Biochemistry. 270(15). 3214–3222. 77 indexed citations
15.
Jeitner, Thomas M., Hans‐Lothar Fuchsbauer, John P. Blass, & Arthur J.L. Cooper. (2001). A Sensitive Fluorometric Assay for Tissue Transglutaminase. Analytical Biochemistry. 292(2). 198–206. 28 indexed citations
16.
Bechtold, Ulrike, et al.. (2000). Enzymic Preparation of Protein G-peroxidase Conjugates Catalysed by Transglutaminase. The Journal of Biochemistry. 127(2). 239–245. 28 indexed citations
17.
18.
Pasternack, Ralf, et al.. (1998). Bacterial pro‐transglutaminase from Streptoverticillium mobaraense. European Journal of Biochemistry. 257(3). 570–576. 133 indexed citations
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20.
Fuchsbauer, Hans‐Lothar, et al.. (1994). A rapid and simple method for the purification of transglutaminase from Streptoverticillium mobaraense.. Biochemical Journal. 299(3). 825–829. 70 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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