Martin Heck

2.7k total citations
38 papers, 2.2k citations indexed

About

Martin Heck is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Organic Chemistry. According to data from OpenAlex, Martin Heck has authored 38 papers receiving a total of 2.2k indexed citations (citations by other indexed papers that have themselves been cited), including 38 papers in Molecular Biology, 30 papers in Cellular and Molecular Neuroscience and 1 paper in Organic Chemistry. Recurrent topics in Martin Heck's work include Receptor Mechanisms and Signaling (32 papers), Photoreceptor and optogenetics research (27 papers) and Retinal Development and Disorders (19 papers). Martin Heck is often cited by papers focused on Receptor Mechanisms and Signaling (32 papers), Photoreceptor and optogenetics research (27 papers) and Retinal Development and Disorders (19 papers). Martin Heck collaborates with scholars based in Germany, United States and Australia. Martin Heck's co-authors include Klaus Peter Hofmann, Oliver P. Ernst, Peter W. Hildebrand, Patrick Scheerer, Hui‐Woog Choe, Jung Hee Park, Franz Bartl, M. Sommer, Eglof Ritter and D Maretzki and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Martin Heck

38 papers receiving 2.2k citations

Peers

Martin Heck

CMN

RNMI

SPECT

Takefumi Morizumi Canada

Kevin D. Ridge United States

Susan M. Hanson United States

Claudio Villa United Kingdom

Paul S.‐H. Park United States

Kaleeckal G. Harikumar United States

Masahiro Kono United States

K. Palczewski United States

Ursula Wilden Germany

Anatol Arendt United States

Takefumi Morizumi Canada

Martin Heck

1.6k ×0.8

1.3k ×0.8

CMN

104 ×0.8

RNMI

64 ×0.5

172 ×1.9

SPECT

Citations per year, relative to Martin Heck Martin Heck (= 1×) peers Takefumi Morizumi

Countries citing papers authored by Martin Heck

Since Specialization

Citations

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

Fields of papers citing papers by Martin Heck

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Martin Heck

This figure shows the co-authorship network connecting the top 25 collaborators of Martin Heck. A scholar is included among the top collaborators of Martin Heck 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 Martin Heck. Martin Heck 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

Schmidt, Andrea, Elmar Behrmann, Jörg Bürger, et al.. (2018). Mechanistic insights into the role of prenyl-binding protein PrBP/δ in membrane dissociation of phosphodiesterase 6. Nature Communications. 9(1). 90–90. 13 indexed citations

Sommer, M., Michal Szczepek, Franz Bartl, et al.. (2015). Formation and Decay of the Arrestin·Rhodopsin Complex in Native Disc Membranes. Journal of Biological Chemistry. 290(20). 12919–12928. 9 indexed citations

Schöneberg, Johannes, et al.. (2014). Explicit Spatiotemporal Simulation of Receptor-G Protein Coupling in Rod Cell Disk Membranes. Biophysical Journal. 107(5). 1042–1053. 27 indexed citations

Szczepek, Michal, Matthias Elgeti, Alexander Rose, et al.. (2014). Crystal structure of a common GPCR-binding interface for G protein and arrestin. Nature Communications. 5(1). 4801–4801. 128 indexed citations

Sommer, M., Klaus Peter Hofmann, & Martin Heck. (2013). Not Just Signal Shutoff: The Protective Role of Arrestin-1 in Rod Cells. Handbook of experimental pharmacology. 219. 101–116. 8 indexed citations

Kümmel, Daniel, et al.. (2010). Characterization of the self-palmitoylation activity of the transport protein particle component Bet3. Cellular and Molecular Life Sciences. 67(15). 2653–2664. 8 indexed citations

Sommer, M., Klaus Peter Hofmann, & Martin Heck. (2010). Arrestin-Rhodopsin Binding Stoichiometry in Isolated Rod Outer Segment Membranes Depends on the Percentage of Activated Receptors. Journal of Biological Chemistry. 286(9). 7359–7369. 40 indexed citations

Hildebrand, Peter W., Patrick Scheerer, Jung Hee Park, et al.. (2009). A Ligand Channel through the G Protein Coupled Receptor Opsin. PLoS ONE. 4(2). e4382–e4382. 102 indexed citations

Herrmann, Rolf, Martin Heck, Peter Henklein, et al.. (2006). Rhodopsin–transducin coupling: Role of the Gα C-terminus in nucleotide exchange catalysis. Vision Research. 46(27). 4582–4593. 19 indexed citations

10.

Herrmann, Rolf, Martin Heck, Peter Henklein, Klaus Peter Hofmann, & Oliver P. Ernst. (2006). Signal Transfer from GPCRs to G Proteins. Journal of Biological Chemistry. 281(40). 30234–30241. 47 indexed citations

11.

Zimmermann, Kathryn, Martin Heck, Joachim Frank, et al.. (2005). Herbicide binding and thermal stability of photosystem II isolated from Thermosynechococcus elongatus. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1757(2). 106–114. 38 indexed citations

12.

Ritter, Eglof, et al.. (2004). Transition of Rhodopsin into the Active Metarhodopsin II State Opens a New Light-induced Pathway Linked to Schiff Base Isomerization. Journal of Biological Chemistry. 279(46). 48102–48111. 36 indexed citations

13.

Ritter, Eglof, et al.. (2004). Interaction with Transducin Depletes Metarhodopsin III. Journal of Biological Chemistry. 279(46). 48112–48119. 27 indexed citations

14.

Heck, Martin, D Maretzki, Sławomir Filipek, et al.. (2003). Ligand Channeling within a G-protein-coupled Receptor. Journal of Biological Chemistry. 278(27). 24896–24903. 98 indexed citations

15.

Heck, Martin, et al.. (2003). Secondary binding sites of retinoids in opsin: characterization and role in regeneration. Vision Research. 43(28). 3003–3010. 40 indexed citations

16.

Heck, Martin, D Maretzki, Franz Bartl, et al.. (2003). Signaling States of Rhodopsin. Journal of Biological Chemistry. 278(5). 3162–3169. 95 indexed citations

17.

Kuksa, Vladimir, Franz Bartl, Tadao Maeda, et al.. (2002). Biochemical and Physiological Properties of Rhodopsin Regenerated with 11-cis-6-Ring- and 7-Ring-retinals. Journal of Biological Chemistry. 277(44). 42315–42324. 39 indexed citations

18.

Heck, Martin & Klaus Peter Hofmann. (2001). Maximal Rate and Nucleotide Dependence of Rhodopsin-catalyzed Transducin Activation. Journal of Biological Chemistry. 276(13). 10000–10009. 140 indexed citations

19.

Körschen, Heinz G., Michael Beyermann, Frank Müller, et al.. (1999). Interaction of glutamic-acid-rich proteins with the cGMP signalling pathway in rod photoreceptors. Nature. 400(6746). 761–766. 108 indexed citations

20.

Heck, Martin & Klaus Peter Hofmann. (1993). G-protein-effector coupling: A real-time light-scattering assay for transducin-phosphodiesterase interaction. Biochemistry. 32(32). 8220–8227. 65 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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