Frank Eisenmenger

1.3k total citations
20 papers, 1.1k citations indexed

About

Frank Eisenmenger is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, Frank Eisenmenger has authored 20 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 10 papers in Materials Chemistry and 6 papers in Spectroscopy. Recurrent topics in Frank Eisenmenger's work include Protein Structure and Dynamics (14 papers), Enzyme Structure and Function (10 papers) and Spectroscopy and Quantum Chemical Studies (3 papers). Frank Eisenmenger is often cited by papers focused on Protein Structure and Dynamics (14 papers), Enzyme Structure and Function (10 papers) and Spectroscopy and Quantum Chemical Studies (3 papers). Frank Eisenmenger collaborates with scholars based in Germany, United Kingdom and United States. Frank Eisenmenger's co-authors include Ulrich H. E. Hansmann, Yuko Okamoto, Simon J. Hubbard, Janet M. Thornton, Shura Hayryan, Chin‐Kun Hu, Ruben Abagyan, Patrick Argos, Tom L. Blundell and John P. Overington and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Molecular Biology and The Journal of Physical Chemistry B.

In The Last Decade

Frank Eisenmenger

20 papers receiving 1.1k citations

Peers

Frank Eisenmenger
H. A. Scheraga United States
Jarek Juraszek Netherlands
Daniel Trzesniak Switzerland
Iosif I. Vaisman United States
Michael Andrec United States
J. R. Quine United States
Wolfgang Rieping France
Kaizhi Yue United States
Nuria Plattner Switzerland
Tim N. Heinz Switzerland
H. A. Scheraga United States
Frank Eisenmenger
Citations per year, relative to Frank Eisenmenger Frank Eisenmenger (= 1×) peers H. A. Scheraga

Countries citing papers authored by Frank Eisenmenger

Since Specialization
Citations

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

Fields of papers citing papers by Frank Eisenmenger

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Frank Eisenmenger

This figure shows the co-authorship network connecting the top 25 collaborators of Frank Eisenmenger. A scholar is included among the top collaborators of Frank Eisenmenger 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 Frank Eisenmenger. Frank Eisenmenger 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.
Stevens, Tim J., Rasmus H. Fogh, Wayne Boucher, et al.. (2011). A software framework for analysing solid-state MAS NMR data. Journal of Biomolecular NMR. 51(4). 437–447. 127 indexed citations
2.
Scholz, Ingo, Stefan Jehle, Peter Schmieder, et al.. (2007). J-Deconvolution Using Maximum Entropy Reconstruction Applied to 13C−13C Solid-State Cross-Polarization Magic-Angle-Spinning NMR of Proteins. Journal of the American Chemical Society. 129(21). 6682–6683. 8 indexed citations
3.
Meinke, Jan H., Sandipan Mohanty, Frank Eisenmenger, & Ulrich H. E. Hansmann. (2007). SMMP v. 3.0—Simulating proteins and protein interactions in Python and Fortran. Computer Physics Communications. 178(6). 459–470. 19 indexed citations
4.
Appelt, C., et al.. (2005). Interaction of the Antimicrobial Peptide Cyclo(RRWWRF) with Membranes by Molecular Dynamics Simulations. Biophysical Journal. 89(4). 2296–2306. 39 indexed citations
5.
Eisenmenger, Frank, Ulrich H. E. Hansmann, Shura Hayryan, & Chin‐Kun Hu. (2005). An enhanced version of SMMP—open-source software package for simulation of proteins. Computer Physics Communications. 174(5). 422–429. 41 indexed citations
6.
Eisenmenger, Frank, Ulrich H. E. Hansmann, Shura Hayryan, & Chin‐Kun Hu. (2001). [SMMP] A modern package for simulation of proteins. Computer Physics Communications. 138(2). 192–212. 94 indexed citations
7.
Hansmann, Ulrich H. E., Frank Eisenmenger, & Yuko Okamoto. (1998). Stochastic dynamics simulations in a new generalized ensemble. Chemical Physics Letters. 297(5-6). 374–382. 11 indexed citations
8.
Eisenmenger, Frank & Ulrich H. E. Hansmann. (1997). Variation of the Energy Landscape of a Small Peptide under a Change from the ECEPP/2 Force Field to ECEPP/3. The Journal of Physical Chemistry B. 101(16). 3304–3310. 37 indexed citations
9.
Eisenmenger, Frank & Ulrich H. E. Hansmann. (1997). Global minimum configuration of a small peptide for the ECEPP/2 and ECEPP/3 force fields. Chemical Physics Letters. 268(1-2). 86–92. 3 indexed citations
10.
Hansmann, Ulrich H. E., Yuko Okamoto, & Frank Eisenmenger. (1996). Molecular dynamics, Langevin and hydrid Monte Carlo simulations in a multicanonical ensemble. Chemical Physics Letters. 259(3-4). 321–330. 231 indexed citations
11.
Hubbard, Simon J., Frank Eisenmenger, & Janet M. Thornton. (1994). Modeling studies of the change in conformation required for cleavage of limited proteolytic sites. Protein Science. 3(5). 757–768. 173 indexed citations
12.
Topham, Christopher M., et al.. (1993). Fragment Ranking in Modelling of Protein Structure. Journal of Molecular Biology. 229(1). 194–220. 88 indexed citations
13.
Eisenmenger, Frank, Patrick Argos, & Ruben Abagyan. (1993). A Method to Configure Protein Side-chains from the Main-chain Trace in Homology Modelling. Journal of Molecular Biology. 231(3). 849–860. 93 indexed citations
14.
Hinzmann, Bernd, Dirk Wernicke, Ute Zacharias, et al.. (1993). Tissue‐type plasminogen activator mutants imitating urokinase in the peptide link between kringle and protease domains and at selected sites with the protease domain. European Journal of Biochemistry. 213(1). 437–443. 1 indexed citations
15.
Rose, Julie M. & Frank Eisenmenger. (1991). A fast unbiased comparison of protein structures by means of the Needleman-Wunsch algorithm. Journal of Molecular Evolution. 32(4). 340–354. 23 indexed citations
16.
Topham, Christopher M., Patrick B. Thomas, John P. Overington, et al.. (1990). An assessment of COMPOSER: a rule-based approach to modelling protein structure.. PubMed. 57. 1–9. 19 indexed citations
17.
18.
Adzhubei, Alexei A., et al.. (1987). Third type of secondary structure: Noncooperative mobile conformation. Protein Data Bank analysis. Biochemical and Biophysical Research Communications. 146(3). 934–938. 32 indexed citations
19.
Adzhubei, Alexei A., et al.. (1987). Approaching a Complete Classification of Protein Secondary Structure. Journal of Biomolecular Structure and Dynamics. 5(3). 689–704. 28 indexed citations
20.
Eisenmenger, Frank, et al.. (1987). [A new type of secondary structure: mobile conformation of polypeptide chain. Data bank for protein structures].. PubMed. 32(1). 159–61. 2 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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