Per Jemth

6.0k total citations
130 papers, 4.6k citations indexed

About

Per Jemth is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Per Jemth has authored 130 papers receiving a total of 4.6k indexed citations (citations by other indexed papers that have themselves been cited), including 115 papers in Molecular Biology, 60 papers in Materials Chemistry and 26 papers in Cell Biology. Recurrent topics in Per Jemth's work include Protein Structure and Dynamics (67 papers), Enzyme Structure and Function (57 papers) and RNA and protein synthesis mechanisms (20 papers). Per Jemth is often cited by papers focused on Protein Structure and Dynamics (67 papers), Enzyme Structure and Function (57 papers) and RNA and protein synthesis mechanisms (20 papers). Per Jemth collaborates with scholars based in Sweden, Italy and United Kingdom. Per Jemth's co-authors include Stefano Gianni, Jakob Dogan, Åke Engström, N. Celestine, Bengt Mannervik, Kristian Strømgaard, Ylva Ivarsson, Carlo Travaglini‐Allocatelli, Anders Bach and Maurizio Brunori 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 Jemth

129 papers receiving 4.6k 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 Jemth Sweden 43 3.7k 1.3k 889 373 324 130 4.6k
Volkhard Helms Germany 41 4.2k 1.1× 658 0.5× 821 0.9× 393 1.1× 704 2.2× 219 5.8k
Tsjerk A. Wassenaar Netherlands 24 4.3k 1.2× 555 0.4× 501 0.6× 505 1.4× 439 1.4× 52 5.3k
Grzegorz Nawrocki United States 13 3.7k 1.0× 779 0.6× 372 0.4× 291 0.8× 401 1.2× 17 5.1k
Birthe B. Kragelund Denmark 49 5.2k 1.4× 1.4k 1.1× 671 0.8× 152 0.4× 275 0.8× 179 6.9k
Michael H. Hecht United States 44 5.3k 1.4× 1.6k 1.3× 571 0.6× 178 0.5× 262 0.8× 104 6.5k
Jesús Zurdo United Kingdom 28 5.6k 1.5× 1.1k 0.9× 668 0.8× 126 0.3× 379 1.2× 35 7.2k
Neil A. Farrow United States 30 3.8k 1.0× 1.1k 0.9× 463 0.5× 353 0.9× 260 0.8× 51 5.6k
Homme W. Hellinga United States 44 4.5k 1.2× 1.3k 1.0× 402 0.5× 394 1.1× 230 0.7× 82 5.6k
Alemayehu A. Gorfe United States 41 4.4k 1.2× 738 0.6× 996 1.1× 168 0.5× 228 0.7× 113 5.0k
Jill Trewhella United States 44 4.4k 1.2× 1.9k 1.5× 554 0.6× 133 0.4× 320 1.0× 158 5.7k

Countries citing papers authored by Per Jemth

Since Specialization
Citations

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

Fields of papers citing papers by Per Jemth

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Per Jemth

This figure shows the co-authorship network connecting the top 25 collaborators of Per Jemth. A scholar is included among the top collaborators of Per Jemth 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 Jemth. Per Jemth 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.
Jemth, Per. (2025). Protein binding and folding through an evolutionary lens. Current Opinion in Structural Biology. 90. 102980–102980. 2 indexed citations
2.
Arcila, Dahiana, Mats E. Pettersson, Eva Andersson, et al.. (2024). Conservation of Affinity Rather Than Sequence Underlies a Dynamic Evolution of the Motif-Mediated p53/MDM2 Interaction in Ray-Finned Fishes. Molecular Biology and Evolution. 41(2). 4 indexed citations
3.
Lindqvist, Richard, Leandro Simonetti, Eva Andersson, et al.. (2023). Identification of motif-based interactions between SARS-CoV-2 protein domains and human peptide ligands pinpoint antiviral targets. Nature Communications. 14(1). 5636–5636. 15 indexed citations
4.
Babina, Arianne M., Jon Jerlström-Hultqvist, Mårten Larsson, et al.. (2023). Rescue of Escherichia coli auxotrophy by de novo small proteins. eLife. 12. 12 indexed citations
5.
Frykholm, Carina, Cecilia Gunnarsson, Sanna Gudmundsson, et al.. (2023). Gustavson syndrome is caused by an in-frame deletion in RBMX associated with potentially disturbed SH3 domain interactions. European Journal of Human Genetics. 32(3). 333–341. 5 indexed citations
6.
Teyra, Joan, Shane Miersch, Lia Cardarelli, et al.. (2022). Development of Monoclonal Antibodies to Detect for SARS-CoV-2 Proteins. Journal of Molecular Biology. 434(10). 167583–167583. 4 indexed citations
7.
Laursen, Louise, et al.. (2022). Determinants of affinity, specificity, and phase separation in a supramodule from Post-synaptic density protein 95. iScience. 25(10). 105069–105069. 2 indexed citations
8.
Haugaard‐Kedström, Linda M., et al.. (2021). Molecular Details of a Coupled Binding and Folding Reaction between the Amyloid Precursor Protein and a Folded Domain. ACS Chemical Biology. 16(7). 1191–1200. 5 indexed citations
9.
Laursen, Louise, Jelena Čalyševa, Toby J. Gibson, & Per Jemth. (2020). Divergent Evolution of a Protein–Protein Interaction Revealed through Ancestral Sequence Reconstruction and Resurrection. Molecular Biology and Evolution. 38(1). 152–167. 7 indexed citations
10.
Laursen, Louise, Johanna Kliche, Stefano Gianni, & Per Jemth. (2020). Supertertiary protein structure affects an allosteric network. Proceedings of the National Academy of Sciences. 117(39). 24294–24304. 26 indexed citations
11.
Gustafsson, Robert, Ulrich Eckhard, Erik D. Enbody, et al.. (2020). Structure and Characterization of Phosphoglucomutase 5 from Atlantic and Baltic Herring—An Inactive Enzyme with Intact Substrate Binding. Biomolecules. 10(12). 1631–1631. 3 indexed citations
12.
Schwochow, Doreen, Elisabeth Sundström, Xiaofang Cao, et al.. (2017). The evolution of Sex-linked barring alleles in chickens involves both regulatory and coding changes in CDKN2A. PLoS Genetics. 13(4). e1006665–e1006665. 29 indexed citations
13.
Toto, Angelo, Eva Andersson, N. Celestine, et al.. (2016). Ligand binding to the PDZ domains of postsynaptic density protein 95. Protein Engineering Design and Selection. 29(5). 169–175. 10 indexed citations
14.
Iešmantavičius, Vytautas, Jakob Dogan, Per Jemth, Kaare Teilum, & Magnus Kjærgaard. (2014). Helical Propensity in an Intrinsically Disordered Protein Accelerates Ligand Binding. Angewandte Chemie International Edition. 53(6). 1548–1551. 137 indexed citations
15.
Bach, Anders, N. Celestine, Lars Olsen, et al.. (2009). Design and Synthesis of Highly Potent and Plasma‐Stable Dimeric Inhibitors of the PSD‐95–NMDA Receptor Interaction. Angewandte Chemie. 121(51). 9865–9869. 15 indexed citations
16.
Celestine, N., et al.. (2008). Reassessing a sparse energetic network within a single protein domain. Proceedings of the National Academy of Sciences. 105(12). 4679–4684. 85 indexed citations
17.
Calosci, Nicoletta, N. Celestine, Barbara Richter, et al.. (2008). Comparison of successive transition states for folding reveals alternative early folding pathways of two homologous proteins. Proceedings of the National Academy of Sciences. 105(49). 19241–19246. 57 indexed citations
18.
Kreuger, Johan, Per Jemth, Dina Ron, et al.. (2005). Fibroblast growth factors share binding sites in heparan sulphate. Biochemical Journal. 389(1). 145–150. 74 indexed citations
19.
White, George, Stefano Gianni, J. Günter Grossmann, et al.. (2005). Simulation and Experiment Conspire to Reveal Cryptic Intermediates and a Slide from the Nucleation-condensation to Framework Mechanism of Folding. Journal of Molecular Biology. 350(4). 757–775. 60 indexed citations
20.
Jemth, Per, Johan Kreuger, Marion Kusche‐Gullberg, et al.. (2002). Biosynthetic Oligosaccharide Libraries for Identification of Protein-binding Heparan Sulfate Motifs. Journal of Biological Chemistry. 277(34). 30567–30573. 86 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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