Jan Raap

3.8k total citations
123 papers, 3.1k citations indexed

About

Jan Raap is a scholar working on Molecular Biology, Spectroscopy and Biophysics. According to data from OpenAlex, Jan Raap has authored 123 papers receiving a total of 3.1k indexed citations (citations by other indexed papers that have themselves been cited), including 71 papers in Molecular Biology, 54 papers in Spectroscopy and 33 papers in Biophysics. Recurrent topics in Jan Raap's work include Advanced NMR Techniques and Applications (33 papers), Electron Spin Resonance Studies (33 papers) and Photoreceptor and optogenetics research (24 papers). Jan Raap is often cited by papers focused on Advanced NMR Techniques and Applications (33 papers), Electron Spin Resonance Studies (33 papers) and Photoreceptor and optogenetics research (24 papers). Jan Raap collaborates with scholars based in Netherlands, Russia and Italy. Jan Raap's co-authors include Johan Lugtenburg, Claudio Toniolo, Fernando Formaggio, Yu. D. Tsvetkov, A. D. Milov, Huub J. M. de Groot, Judith Herzfeld, A.J. Hoff, Peter Gast and Robert G. Griffin and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Nature Communications.

In The Last Decade

Jan Raap

122 papers receiving 3.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Jan Raap Netherlands 35 1.7k 1.1k 815 650 599 123 3.1k
R. Scott Prosser Canada 41 5.4k 3.2× 1.7k 1.6× 549 0.7× 1.6k 2.4× 1.8k 3.1× 109 7.4k
Edvards Liepinsh Latvia 30 2.6k 1.5× 849 0.8× 298 0.4× 859 1.3× 245 0.4× 96 4.0k
Clemens Glaubitz Germany 39 2.3k 1.4× 1.7k 1.6× 364 0.4× 858 1.3× 1.3k 2.2× 152 4.1k
Sergei A. Dzuba Russia 30 1.0k 0.6× 524 0.5× 1.7k 2.1× 848 1.3× 139 0.2× 155 2.9k
P. Bachmann Switzerland 8 2.6k 1.5× 1.8k 1.6× 339 0.4× 784 1.2× 219 0.4× 9 4.8k
L Braunschweiler Switzerland 7 1.7k 1.0× 1.2k 1.1× 375 0.5× 525 0.8× 153 0.3× 9 3.1k
Regitze R. Vold United States 34 1.7k 1.0× 2.5k 2.3× 476 0.6× 948 1.5× 175 0.3× 99 4.1k
Myer Bloom Canada 36 2.8k 1.6× 1.2k 1.1× 237 0.3× 407 0.6× 209 0.3× 76 4.3k
G. Kothe Germany 28 1.3k 0.8× 840 0.8× 561 0.7× 538 0.8× 238 0.4× 121 2.8k
Frans A. A. Mulder Denmark 38 4.1k 2.4× 1.5k 1.4× 355 0.4× 1.4k 2.1× 435 0.7× 109 5.4k

Countries citing papers authored by Jan Raap

Since Specialization
Citations

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

Fields of papers citing papers by Jan Raap

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jan Raap

This figure shows the co-authorship network connecting the top 25 collaborators of Jan Raap. A scholar is included among the top collaborators of Jan Raap 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 Jan Raap. Jan Raap 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.
Steendam, René R. E., Michael Kulka, Hugo Meekes, et al.. (2014). Enantiopure Isoindolinones through Viedma Ripening. Chemistry - A European Journal. 20(42). 13527–13530. 38 indexed citations
2.
Samoilova, Rimma I., Yuri D. Tsvetkov, Marta De Zotti, et al.. (2009). Structure of Self-Aggregated Alamethicin in ePC Membranes Detected by Pulsed Electron-Electron Double Resonance and Electron Spin Echo Envelope Modulation Spectroscopies. Biophysical Journal. 96(8). 3197–3209. 29 indexed citations
3.
Salnikov, Evgeniy S., Xing Li, Philippe Bertani, et al.. (2008). Structure and Alignment of the Membrane-Associated Peptaibols Ampullosporin A and Alamethicin by Oriented 15N and 31P Solid-State NMR Spectroscopy. Biophysical Journal. 96(1). 86–100. 83 indexed citations
4.
Tsvetkov, Yuri D., et al.. (2007). Solvent Effects on the Secondary Structure of the Membrane‐Active Zervamicin Determined by PELDOR Spectroscopy. Chemistry & Biodiversity. 4(6). 1243–1255. 15 indexed citations
5.
Samoilova, Rimma I., Yuri D. Tsvetkov, Micha Jost, et al.. (2007). Supramolecular Structure of Self‐Assembling Alamethicin Analog Studied by ESR and PELDOR. Chemistry & Biodiversity. 4(6). 1275–1298. 20 indexed citations
6.
Salnikov, Evgeniy S., Denis A. Erilov, A. D. Milov, et al.. (2006). Location and Aggregation of the Spin-Labeled Peptide Trichogin GA IV in a Phospholipid Membrane as Revealed by Pulsed EPR. Biophysical Journal. 91(4). 1532–1540. 55 indexed citations
7.
Salnikov, Evgeniy S., Hoai‐Huong Nguyen, Siegmund Reißmann, et al.. (2005). Membrane association and activity of 15/16-membered peptide antibiotics: Zervamicin IIB, ampullosporin A and antiamoebin I. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1715(1). 6–18. 20 indexed citations
8.
Шенкарев, Захар О., Alexander S. Paramonov, T. A. Balashova, et al.. (2004). High stability of the hinge region in the membrane-active peptide helix of zervamicin: paramagnetic relaxation enhancement studies. Biochemical and Biophysical Research Communications. 325(3). 1099–1105. 11 indexed citations
9.
Raap, Jan, et al.. (2002). Ion transport across a phospholipid membrane mediated by the peptide trichogin GA IV. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1567(1-2). 193–203. 27 indexed citations
10.
Шенкарев, Захар О., et al.. (2002). Spatial Structure of Zervamicin IIB Bound to DPC Micelles: Implications for Voltage-Gating. Biophysical Journal. 82(2). 762–771. 39 indexed citations
12.
Dam, Lorens van, et al.. (2002). Solid-State NMR Determination of Sugar Ring Pucker in 13C-Labeled 2′-Deoxynucleosides. Biophysical Journal. 83(5). 2835–2844. 11 indexed citations
13.
Matysik, Jörg, Peter Gast, Jan Raap, et al.. (2001). Photo-CIDNP 13C Magic Angle Spinning NMR on Bacterial Reaction Centres: Exploring the Electronic Structure of the Special Pair and Its Surroundings. Biological Chemistry. 382(8). 1271–1276. 18 indexed citations
14.
Lugtenburg, Johan, et al.. (1997). Total synthesis of zervamicin IIB and its deuterium-labelled analogues. Journal of Peptide Science. 3(3). 193–208. 10 indexed citations
15.
Egorova‐Zachernyuk, T. A., Kees Versluis, W. Heerma, et al.. (1996). Preparation of Site‐Specific Isotopically Labelled Zervamicins, the Antibiotic Peptaibols Produced by Emericellopsis Salmosynnemata. Journal of Peptide Science. 2(6). 341–350. 14 indexed citations
17.
Lakshmi, K. V., Steven O. Smith, Robert S. Brown, et al.. (1993). Solid state NMR study of [epsilon-13C]Lys-bacteriorhodopsin: Schiff base photoisomerization. Biophysical Journal. 65(1). 310–315. 28 indexed citations
18.
Ames, James B., et al.. (1992). Time-resolved ultraviolet resonance Raman studies of protein structure: application to bacteriorhodopsin. Biochemistry. 31(23). 5328–5334. 38 indexed citations
20.
Thompson, Lynmarie K., Ann E. McDermott, Jan Raap, et al.. (1992). Rotational resonance NMR study of the active site structure in bacteriorhodopsin: conformation of the Schiff base linkage. Biochemistry. 31(34). 7931–7938. 68 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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