F. Parak

9.5k total citations · 3 hit papers
177 papers, 7.6k citations indexed

About

F. Parak is a scholar working on Molecular Biology, Cell Biology and Atomic and Molecular Physics, and Optics. According to data from OpenAlex, F. Parak has authored 177 papers receiving a total of 7.6k indexed citations (citations by other indexed papers that have themselves been cited), including 92 papers in Molecular Biology, 84 papers in Cell Biology and 49 papers in Atomic and Molecular Physics, and Optics. Recurrent topics in F. Parak's work include Hemoglobin structure and function (83 papers), Protein Structure and Dynamics (58 papers) and Spectroscopy and Quantum Chemical Studies (36 papers). F. Parak is often cited by papers focused on Hemoglobin structure and function (83 papers), Protein Structure and Dynamics (58 papers) and Spectroscopy and Quantum Chemical Studies (36 papers). F. Parak collaborates with scholars based in Germany, Russia and United States. F. Parak's co-authors include Hans Frauenfelder, Robert Young, Christoph Alexiou, Christian Bergemann, E. W. Knapp, G. Ulrich Nienhaus, Benjamin H. McMahon, Paul W. Fenimore, W. Arnold and W. Erhardt 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

F. Parak

175 papers receiving 7.3k citations

Hit Papers

Conformational Substates in Proteins 1988 2026 2000 2013 1988 2000 2002 250 500 750

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
F. Parak Germany 42 4.3k 2.3k 2.1k 2.1k 1.2k 177 7.6k
James Hofrichter United States 64 8.5k 2.0× 3.5k 1.5× 3.6k 1.7× 2.1k 1.0× 388 0.3× 92 13.0k
Phillip L. Geissler United States 43 3.1k 0.7× 2.7k 1.1× 662 0.3× 4.6k 2.2× 1.5k 1.3× 119 10.3k
Robert Young United States 32 3.3k 0.8× 1.5k 0.6× 1.6k 0.7× 1.7k 0.8× 502 0.4× 59 5.8k
Greg L. Hura United States 40 4.7k 1.1× 2.6k 1.1× 370 0.2× 1.8k 0.8× 881 0.7× 91 8.4k
Shin‐ichi Adachi Japan 45 2.0k 0.5× 2.0k 0.8× 921 0.4× 699 0.3× 188 0.2× 208 6.3k
Bertil Halle Sweden 54 4.4k 1.0× 2.2k 0.9× 462 0.2× 3.2k 1.5× 753 0.6× 160 9.1k
Denis L. Rousseau United States 57 4.9k 1.1× 2.7k 1.2× 3.6k 1.7× 1.7k 0.8× 699 0.6× 225 10.6k
William A. Eaton United States 79 13.8k 3.2× 5.8k 2.5× 5.0k 2.3× 3.9k 1.9× 897 0.8× 167 19.6k
Giuseppe Zaccaı̈ France 48 6.7k 1.6× 2.9k 1.3× 728 0.3× 2.0k 1.0× 468 0.4× 183 9.3k
Hyotcherl Ihee South Korea 47 1.9k 0.4× 4.1k 1.7× 345 0.2× 2.1k 1.0× 812 0.7× 195 8.4k

Countries citing papers authored by F. Parak

Since Specialization
Citations

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

Fields of papers citing papers by F. Parak

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of F. Parak

This figure shows the co-authorship network connecting the top 25 collaborators of F. Parak. A scholar is included among the top collaborators of F. Parak 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 F. Parak. F. Parak 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.
Schmidt, Marius, et al.. (2009). Protein dynamics of a β-sheet protein. European Biophysics Journal. 38(5). 687–700. 14 indexed citations
2.
Weber, Birgit, et al.. (2008). Synthesis and Characterization of a Dinuclear Iron(II) Spin Crossover Complex with Wide Hysteresis. Inorganic Chemistry. 47(22). 10779–10787. 63 indexed citations
3.
Renner, Christian, Stella Fiori, Ferdinando Fiorino, et al.. (2004). Micellar environments induce structuring of the N‐terminal tail of the prion protein. Biopolymers. 73(4). 421–433. 18 indexed citations
4.
Parak, F.. (2003). Proteins in action: the physics of structural fluctuations and conformational changes. Current Opinion in Structural Biology. 13(5). 552–557. 101 indexed citations
5.
Achterhold, Klaus, Bernt Krebs, E. W. Knapp, et al.. (2001). The X-ray absorption spectroscopy Debye-Waller factors of an iron compound and of met-myoglobin as a function of temperature. European Biophysics Journal. 30(6). 393–403. 11 indexed citations
6.
Achterhold, Klaus, Andreas Ostermann, U. van Bürck, et al.. (2000). Nuclear forward scattering of synchrotron radiation by deoxymyoglobin. European Biophysics Journal. 29(2). 146–152. 10 indexed citations
7.
Parak, F. & Klaus Achterhold. (1999). Protein dynamics studied on myoglobin. Hyperfine Interactions. 123-124(1-4). 825–840. 13 indexed citations
8.
Knapp, E. W., et al.. (1996). Structural fluctuations of myoglobin from normal-modes, Mössbauer, Raman, and absorption spectroscopy. Biophysical Journal. 70(5). 2092–2099. 71 indexed citations
9.
Achterhold, Klaus, U. van Bürck, W. Potzel, et al.. (1996). Temperature dependent inelastic X-ray scattering of synchrotron radiation on myoglobin analyzed by the Mössbauer effect. European Biophysics Journal. 25(1). 43–46. 17 indexed citations
10.
Parak, F., et al.. (1994). Relaxation of non-equilibrium states of myoglobin studied by Mössbauer spectroscopy. Hyperfine Interactions. 91(1). 885–890. 10 indexed citations
11.
Friedrich, J., et al.. (1993). Hole burning and pressure phenomena in chromoproteins. Journal of Luminescence. 56(1-6). 157–164. 2 indexed citations
12.
Winkler, H., et al.. (1992). Molecular tunneling and pumping effects in low temperature MBCO recombination. Hyperfine Interactions. 71(1-4). 1291–1294. 1 indexed citations
13.
Frolov, E. N., et al.. (1991). Hemoglobin dynamics in rat erythrocytes investigated by M�ssbauer spectroscopy. European Biophysics Journal. 19(5). 253–6. 7 indexed citations
14.
Cichutek, Klaus, Herbert Witzel, & F. Parak. (1988). The different iron binding sites of bovine spleen purple acid phosphatase. Hyperfine Interactions. 42(1-4). 885–888. 10 indexed citations
15.
Nienhaus, G. Ulrich, et al.. (1987). A multiwire proportional counter with spherical drift chamber for protein crystallography with X-rays and gamma-rays. Nuclear Instruments and Methods in Physics Research Section A Accelerators Spectrometers Detectors and Associated Equipment. 256(3). 581–586. 6 indexed citations
16.
Parak, F.. (1985). Schwerpunkt Biophysik: Strukturfluktuationen in Proteinen. Physikalische Blätter. 41(12). 396–400. 3 indexed citations
17.
Knapp, E. W., Sighart F. Fischer, & F. Parak. (1982). Protein dynamics from Moessbauer spectra. The temperature dependence. The Journal of Physical Chemistry. 86(26). 5042–5047. 92 indexed citations
18.
Mayo, Kevin H., F. Parak, & R. L. Mößbauer. (1981). Observations of elastic and quasi-elastic nuclear gamma resonance absorption in hemoglobin crystals. Physics Letters A. 82(9). 468–470. 27 indexed citations
19.
Krupyanskiǐ, Yu. F., et al.. (1980). Determination of the mean square displacement of the atomic vibrations in myoglobin molecules by measuring Rayleigh scattering of the Mössbauer radiation. Journal of Experimental and Theoretical Physics. 52. 31. 1 indexed citations
20.
Parak, F., et al.. (1973). A position-sensitive surface-barrier Si(Li) detector for low energy γ rays. Nuclear Instruments and Methods. 112(3). 455–461. 6 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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