Per Rogne

1.4k total citations
26 papers, 1.0k citations indexed

About

Per Rogne is a scholar working on Molecular Biology, Materials Chemistry and Food Science. According to data from OpenAlex, Per Rogne has authored 26 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Molecular Biology, 11 papers in Materials Chemistry and 7 papers in Food Science. Recurrent topics in Per Rogne's work include Protein Structure and Dynamics (12 papers), Enzyme Structure and Function (11 papers) and Probiotics and Fermented Foods (7 papers). Per Rogne is often cited by papers focused on Protein Structure and Dynamics (12 papers), Enzyme Structure and Function (11 papers) and Probiotics and Fermented Foods (7 papers). Per Rogne collaborates with scholars based in Sweden, Norway and United States. Per Rogne's co-authors include Per Eugen Kristiansen, Camilla Oppegård, Magnus Wolf‐Watz, Gunnar Fimland, Michael Kovermann, Håvard Jostein Haugen, Christin Grundström, Uwe H. Sauer, Lars T. Kuhn and Christian Hedberg and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Per Rogne

24 papers receiving 999 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Per Rogne Sweden 15 776 511 164 153 134 26 1.0k
Filip V. Toukach Russia 24 1.1k 1.5× 249 0.5× 291 1.8× 56 0.4× 115 0.9× 91 2.0k
F.J.M. van de Ven Netherlands 23 1.0k 1.3× 299 0.6× 88 0.5× 150 1.0× 156 1.2× 36 1.4k
Henno W. van den Hooven Netherlands 15 607 0.8× 444 0.9× 125 0.8× 193 1.3× 17 0.1× 21 1.0k
Vince Pozsgay United States 30 1.5k 2.0× 107 0.2× 191 1.2× 120 0.8× 46 0.3× 88 2.2k
Richard J. Bingham United Kingdom 17 467 0.6× 209 0.4× 79 0.5× 31 0.2× 78 0.6× 21 1.0k
Karen E. Kawulka Canada 6 346 0.4× 206 0.4× 34 0.2× 122 0.8× 27 0.2× 6 490
Kai Wen China 24 947 1.2× 107 0.2× 25 0.2× 68 0.4× 137 1.0× 80 1.5k
Micheline Guinand France 18 530 0.7× 137 0.3× 47 0.3× 120 0.8× 83 0.6× 50 911
Vassiliy N. Bavro United Kingdom 25 941 1.2× 89 0.2× 80 0.5× 86 0.6× 86 0.6× 47 1.9k

Countries citing papers authored by Per Rogne

Since Specialization
Citations

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

Fields of papers citing papers by Per Rogne

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Per Rogne

This figure shows the co-authorship network connecting the top 25 collaborators of Per Rogne. A scholar is included among the top collaborators of Per Rogne 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 Per Rogne. Per Rogne 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.
2.
Nam, Kwangho, Jörgen Ådén, Per Rogne, et al.. (2024). Magnesium induced structural reorganization in the active site of adenylate kinase. Science Advances. 10(32). eado5504–eado5504. 9 indexed citations
3.
Rogne, Per, et al.. (2023). Insights into Enzymatic Catalysis from Binding and Hydrolysis of Diadenosine Tetraphosphate by E. coli Adenylate Kinase. Biochemistry. 62(15). 2238–2243. 3 indexed citations
4.
Sparrman, Tobias, Ameeq Ul Mushtaq, Per Rogne, et al.. (2022). Insights into the evolution of enzymatic specificity and catalysis: From Asgard archaea to human adenylate kinases. Science Advances. 8(44). eabm4089–eabm4089. 14 indexed citations
5.
Mushtaq, Ameeq Ul, et al.. (2021). Milligram scale expression, refolding, and purification of Bombyx mori cocoonase using a recombinant E. coli system. Protein Expression and Purification. 186. 105919–105919. 10 indexed citations
6.
Mushtaq, Ameeq Ul, Per Rogne, Victor Ovchinnikov, et al.. (2021). Dynamic Connection between Enzymatic Catalysis and Collective Protein Motions. Biochemistry. 60(28). 2246–2258. 37 indexed citations
7.
Rogne, Per, David Andersson, Christin Grundström, et al.. (2019). Nucleation of an Activating Conformational Change by a Cation−π Interaction. Biochemistry. 58(32). 3408–3412. 8 indexed citations
8.
Rogne, Per, et al.. (2019). Dynamic pH‐induced conformational changes of the PsbO protein in the fluctuating acidity of the thylakoid lumen. Physiologia Plantarum. 166(1). 288–299. 11 indexed citations
9.
Rogne, Per, Marie Rosselin, Christin Grundström, et al.. (2018). Molecular mechanism of ATP versus GTP selectivity of adenylate kinase. Proceedings of the National Academy of Sciences. 115(12). 3012–3017. 38 indexed citations
10.
Rogne, Per & Magnus Wolf‐Watz. (2016). Urea-Dependent Adenylate Kinase Activation following Redistribution of Structural States. Biophysical Journal. 111(7). 1385–1395. 11 indexed citations
11.
Tükenmez, Hasan, et al.. (2016). Bridging in Vitro with in Vivo Enzymology. Biophysical Journal. 110(3). 223a–223a.
12.
Kovermann, Michael, Per Rogne, & Magnus Wolf‐Watz. (2016). Protein dynamics and function from solution state NMR spectroscopy. Quarterly Reviews of Biophysics. 49. e6–e6. 131 indexed citations
13.
Rogne, Per, et al.. (2016). Characterization of the Ruler Protein Interaction Interface on the Substrate Specificity Switch Protein in the Yersinia Type III Secretion System. Journal of Biological Chemistry. 292(8). 3299–3311. 19 indexed citations
14.
Rogne, Per, et al.. (2012). Atomic-Level Structure Characterization of an Ultrafast Folding Mini-Protein Denatured State. PLoS ONE. 7(7). e41301–e41301. 15 indexed citations
15.
Rogne, Per, et al.. (2009). Structure-Function Relationships of the Non-Lanthionine-Containing Peptide (class II) Bacteriocins Produced by Gram-Positive Bacteria. Current Pharmaceutical Biotechnology. 10(1). 19–37. 203 indexed citations
16.
Oppegård, Camilla, et al.. (2009). Structure and Mode-of-Action of the Two-Peptide (Class-IIb) Bacteriocins. Probiotics and Antimicrobial Proteins. 2(1). 52–60. 143 indexed citations
17.
Rogne, Per, et al.. (2009). Three-dimensional structure of the two-peptide bacteriocin plantaricin JK. Peptides. 30(9). 1613–1621. 33 indexed citations
18.
Rogne, Per, et al.. (2008). Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin plantaricin EF. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1784(11). 1711–1719. 40 indexed citations
19.
Rogne, Per, et al.. (2008). Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin lactococcin G. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1784(3). 543–554. 65 indexed citations
20.
Oppegård, Camilla, et al.. (2007). The Two-Peptide Class II Bacteriocins: Structure, Production, and Mode of Action. Microbial Physiology. 13(4). 210–219. 118 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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