Heino Prinz

4.1k total citations · 1 hit paper
62 papers, 3.3k citations indexed

About

Heino Prinz is a scholar working on Molecular Biology, Organic Chemistry and Biotechnology. According to data from OpenAlex, Heino Prinz has authored 62 papers receiving a total of 3.3k indexed citations (citations by other indexed papers that have themselves been cited), including 46 papers in Molecular Biology, 11 papers in Organic Chemistry and 11 papers in Biotechnology. Recurrent topics in Heino Prinz's work include Ion channel regulation and function (11 papers), Receptor Mechanisms and Signaling (9 papers) and Nicotinic Acetylcholine Receptors Study (9 papers). Heino Prinz is often cited by papers focused on Ion channel regulation and function (11 papers), Receptor Mechanisms and Signaling (9 papers) and Nicotinic Acetylcholine Receptors Study (9 papers). Heino Prinz collaborates with scholars based in Germany, Thailand and Austria. Heino Prinz's co-authors include Herbert Waldmann, Alfred Wittinghofer, Arturo Zychlinsky, Simone Heß, Tobias A. Fuchs, Nancy E. Martinez, Abdul Hakkim, Alfred Maelicke, Alois Fürstner and Mathias Gruen and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Heino Prinz

60 papers receiving 3.2k citations

Hit Papers

Activation of the Raf-MEK... 2010 2026 2015 2020 2010 200 400 600

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Heino Prinz Germany 29 2.0k 791 547 285 253 62 3.3k
Andrew A. McCarthy France 32 2.9k 1.5× 1.0k 1.3× 276 0.5× 299 1.0× 413 1.6× 75 5.0k
Kieran F. Geoghegan United States 32 3.3k 1.7× 349 0.4× 645 1.2× 411 1.4× 406 1.6× 89 5.7k
Scott D. Larsen United States 37 1.8k 0.9× 255 0.3× 988 1.8× 180 0.6× 384 1.5× 102 3.6k
Dianne L. Newton United States 35 3.1k 1.6× 768 1.0× 301 0.6× 179 0.6× 230 0.9× 87 4.6k
Michael Hennig Switzerland 38 3.2k 1.6× 427 0.5× 620 1.1× 228 0.8× 90 0.4× 88 4.9k
Masaaki Ishizuka Japan 35 2.0k 1.0× 406 0.5× 963 1.8× 919 3.2× 181 0.7× 141 4.0k
Robert S. McDowell United States 28 2.8k 1.4× 345 0.4× 969 1.8× 207 0.7× 192 0.8× 44 4.3k
Yoshimasa Uehara Japan 35 2.4k 1.2× 427 0.5× 706 1.3× 475 1.7× 502 2.0× 126 4.3k
Sandra B. Gabelli United States 34 3.6k 1.9× 562 0.7× 313 0.6× 99 0.3× 267 1.1× 100 5.4k

Countries citing papers authored by Heino Prinz

Since Specialization
Citations

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

Fields of papers citing papers by Heino Prinz

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Heino Prinz

This figure shows the co-authorship network connecting the top 25 collaborators of Heino Prinz. A scholar is included among the top collaborators of Heino Prinz 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 Heino Prinz. Heino Prinz 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
2.
Pantoom, Supansa, Ingrid R. Vetter, Heino Prinz, & Wipa Suginta. (2011). Potent Family-18 Chitinase Inhibitors. Journal of Biological Chemistry. 286(27). 24312–24323. 30 indexed citations
3.
Prinz, Heino. (2011). Simplification traps. PubMed. 5(1). 1–4. 2 indexed citations
4.
Prinz, Heino & André Schönichen. (2008). Transient binding patches: a plausible concept for drug binding. PubMed. 1(1-4). 95–104. 9 indexed citations
5.
Schwerk, W., et al.. (2008). Semiquantitative Analysen intrarenaler arterieller Dopplerflußspektren bei gesunden Erwachsenen. Ultraschall in der Medizin - European Journal of Ultrasound. 14(3). 117–122. 2 indexed citations
6.
Wagner, Stefanie, et al.. (2006). Drosophila photoreceptors express cysteine peptidase tan. The Journal of Comparative Neurology. 500(4). 601–611. 31 indexed citations
7.
Weide, Timo, et al.. (2005). 3-Substituted indolizine-1-carbonitrile derivatives as phosphatase inhibitors. Bioorganic & Medicinal Chemistry Letters. 16(1). 59–63. 123 indexed citations
8.
Suginta, Wipa, et al.. (2005). Enzymatic properties of wild‐type and active site mutants of chitinase A fromVibrio carchariae, as revealed by HPLC‐MS. FEBS Journal. 272(13). 3376–3386. 42 indexed citations
9.
Songsiriritthigul, Chomphunuch, et al.. (2005). Expression, purification, crystallization and preliminary crystallographic analysis of chitinase A fromVibrio carchariae. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(10). 895–898. 1 indexed citations
10.
Fürstner, Alois, et al.. (2004). The Core Structures of Roseophilin and the Prodigiosin Alkaloids Define a New Class of Protein Tyrosine Phosphatase Inhibitors. ChemBioChem. 5(11). 1575–1579. 55 indexed citations
11.
Prinz, Heino, et al.. (2004). Expression and refolding of Omp38 from Burkholderia pseudomallei and Burkholderia thailandensis, and its function as a diffusion porin. Biochemical Journal. 384(3). 609–617. 21 indexed citations
12.
Fürstner, Alois, et al.. (2003). Total Synthesis and Reassessment of the Phosphatase‐Inhibitory Activity of the Antitumor Agent TMC‐69‐6H. Angewandte Chemie. 115(43). 5519–5522. 21 indexed citations
13.
Jeyaraj, Duraiswamy A., Heino Prinz, & Herbert Waldmann. (2002). Synthesis of Nucleopeptides by Employing an Enzyme-Labile Urethane Protecting Group. Chemistry - A European Journal. 8(8). 1879–1879. 5 indexed citations
14.
Gruen, Mathias, Heino Prinz, & Mathias Gautel. (1999). cAPK‐phosphorylation controls the interaction of the regulatory domain of cardiac myosin binding protein C with myosin‐S2 in an on‐off fashion. FEBS Letters. 453(3). 254–259. 168 indexed citations
15.
Berger, Walter, et al.. (1994). Complex Molecular Mechanism for Dihydropyridine Binding to L-Type Ca2+-Channels As Revealed by Fluorescence Resonance Energy Transfer. Biochemistry. 33(39). 11875–11883. 23 indexed citations
16.
Covarrubias, Manuel, et al.. (1986). Equilibrium binding of cholinergic ligands to the membrane-bound acetylcholine receptor.. Journal of Biological Chemistry. 261(32). 14955–14961. 23 indexed citations
17.
Prinz, Heino. (1983). On the Interpretation of Equilibrium Binding Studies. Journal of Receptor Research. 3(1-2). 239–248. 10 indexed citations
18.
Prinz, Heino, et al.. (1980). On the kinetics of cholinergic excitation. Neurochemistry International. 2. 251–256. 5 indexed citations
19.
Prinz, Heino, et al.. (1979). NBD-5-acylcholine: fluorescent analog of acetylcholine and agonist at the neuromuscular junction.. Proceedings of the National Academy of Sciences. 76(3). 1064–1068. 41 indexed citations
20.
Prinz, Heino, et al.. (1976). Spermine stabilizes the conformation of tRNAPhe in crystals. Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis. 447(1). 110–115. 12 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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