Dieter Perl

1.5k total citations
16 papers, 1.3k citations indexed

About

Dieter Perl is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Dieter Perl has authored 16 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 13 papers in Materials Chemistry and 5 papers in Cell Biology. Recurrent topics in Dieter Perl's work include Protein Structure and Dynamics (16 papers), Enzyme Structure and Function (13 papers) and Heat shock proteins research (11 papers). Dieter Perl is often cited by papers focused on Protein Structure and Dynamics (16 papers), Enzyme Structure and Function (13 papers) and Heat shock proteins research (11 papers). Dieter Perl collaborates with scholars based in Germany, Switzerland and United States. Dieter Perl's co-authors include Franz X. Schmid, Udo Heinemann, U. Müeller, Thomas H. Schindler, Mohamed A. Marahiel, Franz X. Schmid, Brian N. Dominy, Charles L. Brooks, Christine Welker and Rainer Jaenicke and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Biochemistry.

In The Last Decade

Dieter Perl

16 papers receiving 1.2k citations

Peers

Dieter Perl
Beatriz Ibarra‐Molero Spain
Kevin L. Shaw United States
Vakhtang V. Loladze United States
Vladimir V. Filimonov Russia
Patrick Alexander United States
Brian W. Matthews United States
Bertrand García‐Moreno United States
Sanbo Qin United States
Sergiy O. Garbuzynskiy Russia
H. Nicholson United States
Beatriz Ibarra‐Molero Spain
Dieter Perl
Citations per year, relative to Dieter Perl Dieter Perl (= 1×) peers Beatriz Ibarra‐Molero

Countries citing papers authored by Dieter Perl

Since Specialization
Citations

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

Fields of papers citing papers by Dieter Perl

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Dieter Perl

This figure shows the co-authorship network connecting the top 25 collaborators of Dieter Perl. A scholar is included among the top collaborators of Dieter Perl 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 Dieter Perl. Dieter Perl is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

16 of 16 papers shown
1.
Szyperski, Thomas, Jeffrey Mills, Dieter Perl, & Jochen Balbach. (2005). Combined NMR-observation of cold denaturation in supercooled water and heat denaturation enables accurate measurement of ΔC p of protein unfolding. European Biophysics Journal. 35(4). 363–366. 40 indexed citations
2.
Jacob, Maik H., C Saudan, Georg Holtermann, et al.. (2002). Water Contributes Actively to the Rapid Crossing of a Protein Unfolding Barrier. Journal of Molecular Biology. 318(3). 837–845. 40 indexed citations
3.
Perl, Dieter, et al.. (2002). Thermodynamics of a diffusional protein folding reaction. Biophysical Chemistry. 96(2-3). 173–190. 38 indexed citations
4.
Dominy, Brian N., Dieter Perl, Franz X. Schmid, & Charles L. Brooks. (2002). The Effects of Ionic Strength on Protein Stability: The Cold Shock Protein Family. Journal of Molecular Biology. 319(2). 541–554. 154 indexed citations
5.
Perl, Dieter & Franz X. Schmid. (2002). Some Like It Hot: The Molecular Determinants of Protein Thermostability. ChemBioChem. 3(1). 39–44. 34 indexed citations
6.
Perl, Dieter & Franz X. Schmid. (2002). ChemInform Abstract: Some Like It Hot: The Molecular Determinants of Protein Thermostability. ChemInform. 33(16). 1 indexed citations
7.
Perl, Dieter & Franz X. Schmid. (2001). Electrostatic stabilization of a thermophilic cold shock protein. Journal of Molecular Biology. 313(2). 343–357. 107 indexed citations
8.
Delbrück, Heinrich, U. Müeller, Dieter Perl, Franz X. Schmid, & Udo Heinemann. (2001). Crystal structures of mutant forms of the Bacillus caldolyticus cold shock protein differing in thermal stability. Journal of Molecular Biology. 313(2). 359–369. 38 indexed citations
9.
Perl, Dieter, Georg Holtermann, & Franz X. Schmid. (2001). Role of the Chain Termini for the Folding Transition State of the Cold Shock Protein. Biochemistry. 40(51). 15501–15511. 33 indexed citations
10.
Schmid, Franz X., Dieter Perl, U. Müeller, & Udo Heinemann. (2000). Two exposed amino acid residues confer thermostability on a cold shock protein.. Nature Structural Biology. 7(5). 380–383. 264 indexed citations
11.
Müeller, U., Dieter Perl, Franz X. Schmid, & Udo Heinemann. (2000). Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock protein 1 1Edited by D. C. Rees. Journal of Molecular Biology. 297(4). 975–988. 103 indexed citations
12.
Schindler, Thomas H., et al.. (1999). The Family of Cold Shock Proteins of Bacillus subtilis. Journal of Biological Chemistry. 274(6). 3407–3413. 58 indexed citations
13.
Jacob, Maik H., Georg Holtermann, Dieter Perl, et al.. (1999). Microsecond Folding of the Cold Shock Protein Measured by a Pressure-Jump Technique. Biochemistry. 38(10). 2882–2891. 56 indexed citations
14.
Schindler, Thomas H., et al.. (1998). Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB fromBacillus subtilis. Proteins Structure Function and Bioinformatics. 30(4). 401–406. 49 indexed citations
15.
Schindler, Thomas H., Dieter Perl, Peter L. Graumann, et al.. (1998). Surface‐exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold‐shock protein CspB from Bacillus subtilis. Proteins Structure Function and Bioinformatics. 30(4). 401–406. 2 indexed citations
16.
Perl, Dieter, Christine Welker, Thomas H. Schindler, et al.. (1998). Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nature Structural Biology. 5(3). 229–235. 255 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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