Jeppe Kari

1.1k total citations
30 papers, 827 citations indexed

About

Jeppe Kari is a scholar working on Biomedical Engineering, Molecular Biology and Biomaterials. According to data from OpenAlex, Jeppe Kari has authored 30 papers receiving a total of 827 indexed citations (citations by other indexed papers that have themselves been cited), including 24 papers in Biomedical Engineering, 18 papers in Molecular Biology and 10 papers in Biomaterials. Recurrent topics in Jeppe Kari's work include Biofuel production and bioconversion (24 papers), Enzyme Catalysis and Immobilization (12 papers) and Enzyme Production and Characterization (10 papers). Jeppe Kari is often cited by papers focused on Biofuel production and bioconversion (24 papers), Enzyme Catalysis and Immobilization (12 papers) and Enzyme Production and Characterization (10 papers). Jeppe Kari collaborates with scholars based in Denmark, Estonia and Sweden. Jeppe Kari's co-authors include Peter Westh, Kim Borch, Kenneth Jensen, Johan P. Olsen, Silke Flindt Badino, Morten Andersen, Trine Holst Sørensen, Kristian B. R. M. Krogh, Nicolaj Cruys‐Bagger and Jenny Arnling Bååth and has published in prestigious journals such as Journal of Biological Chemistry, Nature Communications and Biochemistry.

In The Last Decade

Jeppe Kari

30 papers receiving 818 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Jeppe Kari Denmark 16 472 358 255 207 122 30 827
Silke Flindt Badino Denmark 15 326 0.7× 231 0.6× 148 0.6× 136 0.7× 93 0.8× 22 550
Aftab Ahamed Canada 11 675 1.4× 455 1.3× 98 0.4× 285 1.4× 184 1.5× 14 955
Alankar A. Vaidya New Zealand 21 591 1.3× 282 0.8× 398 1.6× 140 0.7× 140 1.1× 43 1.1k
Fumihiko Hasegawa Japan 12 159 0.3× 287 0.8× 192 0.8× 88 0.4× 117 1.0× 22 696
Shuangyan Han China 14 260 0.6× 217 0.6× 473 1.9× 103 0.5× 153 1.3× 36 936
Mingren Liu China 15 610 1.3× 156 0.4× 203 0.8× 125 0.6× 150 1.2× 25 951
Takamitsu Arai Japan 20 684 1.4× 385 1.1× 330 1.3× 263 1.3× 183 1.5× 45 1.1k
Ya‐Shan Cheng Taiwan 14 371 0.8× 393 1.1× 294 1.2× 275 1.3× 185 1.5× 21 949
Yi Tong China 16 164 0.3× 228 0.6× 301 1.2× 92 0.4× 47 0.4× 39 707

Countries citing papers authored by Jeppe Kari

Since Specialization
Citations

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

Fields of papers citing papers by Jeppe Kari

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Jeppe Kari

This figure shows the co-authorship network connecting the top 25 collaborators of Jeppe Kari. A scholar is included among the top collaborators of Jeppe Kari 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 Jeppe Kari. Jeppe Kari 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.
Westh, Peter, et al.. (2024). Are cellulases slow? Kinetic and thermodynamic limitations for enzymatic breakdown of cellulose. PubMed. 7. 100128–100128. 1 indexed citations
2.
Kari, Jeppe, et al.. (2022). The Sabatier principle as a tool for discovery and engineering of industrial enzymes. Current Opinion in Biotechnology. 78. 102843–102843. 11 indexed citations
3.
Badino, Silke Flindt, Trine Holst Sørensen, Jeppe Kari, et al.. (2021). A comparative biochemical investigation of the impeding effect of C1-oxidizing LPMOs on cellobiohydrolases. Journal of Biological Chemistry. 296. 100504–100504. 14 indexed citations
4.
Kari, Jeppe, Kay Schaller, Silke Flindt Badino, et al.. (2021). Physical constraints and functional plasticity of cellulases. Nature Communications. 12(1). 3847–3847. 31 indexed citations
5.
Kari, Jeppe, et al.. (2019). A practical approach to steady-state kinetic analysis of cellulases acting on their natural insoluble substrate. Analytical Biochemistry. 586. 113411–113411. 12 indexed citations
6.
Olsen, Johan P., Jeppe Kari, Michael Skovbo Windahl, Kim Borch, & Peter Westh. (2019). Molecular recognition in the product site of cellobiohydrolase Cel7A regulates processive step length. Biochemical Journal. 477(1). 99–110. 5 indexed citations
7.
Kari, Jeppe, Trine Holst Sørensen, Silke Flindt Badino, et al.. (2019). Substrate binding in the processive cellulase Cel7A: Transition state of complexation and roles of conserved tryptophan residues. Journal of Biological Chemistry. 295(6). 1454–1463. 21 indexed citations
8.
Kari, Jeppe, Johan P. Olsen, Kenneth Jensen, et al.. (2018). Sabatier Principle for Interfacial (Heterogeneous) Enzyme Catalysis. ACS Catalysis. 8(12). 11966–11972. 160 indexed citations
9.
Jensen, Kenneth, et al.. (2018). Systematic deletions in the cellobiohydrolase (CBH) Cel7A from the fungus Trichoderma reesei reveal flexible loops critical for CBH activity. Journal of Biological Chemistry. 294(6). 1807–1815. 39 indexed citations
10.
Borisova, Anna S., Elena V. Eneyskaya, Silke Flindt Badino, et al.. (2018). Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases from Trichoderma atroviride, T. reesei and T. harzianum. Biotechnology for Biofuels. 11(1). 5–5. 22 indexed citations
11.
Badino, Silke Flindt, et al.. (2017). Direct kinetic comparison of the two cellobiohydrolases Cel6A and Cel7A from Hypocrea jecorina Proteins and proteomics. Biochimica et Biophysica Acta. 1 indexed citations
12.
Westh, Peter, et al.. (2017). Thermoactivation of a cellobiohydrolase. Biotechnology and Bioengineering. 115(4). 831–838. 12 indexed citations
13.
Olsen, Johan P., Jeppe Kari, Kim Borch, & Peter Westh. (2017). A quenched-flow system for measuring heterogeneous enzyme kinetics with sub-second time resolution. Enzyme and Microbial Technology. 105. 45–50. 6 indexed citations
14.
Badino, Silke Flindt, et al.. (2017). Direct kinetic comparison of the two cellobiohydrolases Cel6A and Cel7A from Hypocrea jecorina. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1865(12). 1739–1745. 15 indexed citations
15.
Andersen, Morten, Jeppe Kari, Kim Borch, & Peter Westh. (2017). Michaelis–Menten equation for degradation of insoluble substrate. Mathematical Biosciences. 296. 93–97. 37 indexed citations
16.
Badino, Silke Flindt, Jeppe Kari, Michael Skovbo Windahl, et al.. (2017). Exo‐exo synergy between Cel6A and Cel7A from Hypocrea jecorina: Role of carbohydrate binding module and the endo‐lytic character of the enzymes. Biotechnology and Bioengineering. 114(8). 1639–1647. 27 indexed citations
17.
Kont, Riin, Jeppe Kari, Kim Borch, Peter Westh, & Priit Väljamäe. (2016). Inter-domain Synergism Is Required for Efficient Feeding of Cellulose Chain into Active Site of Cellobiohydrolase Cel7A. Journal of Biological Chemistry. 291(50). 26013–26023. 33 indexed citations
18.
Kari, Jeppe, Riin Kont, Kim Borch, et al.. (2016). Anomeric Selectivity and Product Profile of a Processive Cellulase. Biochemistry. 56(1). 167–178. 11 indexed citations
19.
Colussi, Francieli, Trine Holst Sørensen, Jeppe Kari, et al.. (2014). Probing Substrate Interactions in the Active Tunnel of a Catalytically Deficient Cellobiohydrolase (Cel7). Journal of Biological Chemistry. 290(4). 2444–2454. 34 indexed citations
20.
Kari, Jeppe, Johan P. Olsen, Kim Borch, et al.. (2014). Kinetics of Cellobiohydrolase (Cel7A) Variants with Lowered Substrate Affinity. Journal of Biological Chemistry. 289(47). 32459–32468. 59 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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