Thijs Kaper

1.7k total citations
29 papers, 1.3k citations indexed

About

Thijs Kaper is a scholar working on Biotechnology, Molecular Biology and Biomedical Engineering. According to data from OpenAlex, Thijs Kaper has authored 29 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Biotechnology, 18 papers in Molecular Biology and 12 papers in Biomedical Engineering. Recurrent topics in Thijs Kaper's work include Enzyme Production and Characterization (20 papers), Enzyme Catalysis and Immobilization (15 papers) and Biofuel production and bioconversion (12 papers). Thijs Kaper is often cited by papers focused on Enzyme Production and Characterization (20 papers), Enzyme Catalysis and Immobilization (15 papers) and Biofuel production and bioconversion (12 papers). Thijs Kaper collaborates with scholars based in Netherlands, United States and Sweden. Thijs Kaper's co-authors include John van der Oost, Marc J. E. C. van der Maarel, Willem M. de Vos, Lubbert Dijkhuizen, Joyce H.G. Lebbink, Saeid Karkehabadi, Mats Sandgren, Henrik Hansson, Loren L. Looger and Wolf B. Frommer and has published in prestigious journals such as Chemical Reviews, Journal of Biological Chemistry and Applied and Environmental Microbiology.

In The Last Decade

Thijs Kaper

29 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Thijs Kaper Netherlands 22 750 719 499 372 245 29 1.3k
Julia Marín‐Navarro Spain 20 874 1.2× 401 0.6× 367 0.7× 219 0.6× 232 0.9× 39 1.3k
Nicolas Lenfant France 13 636 0.8× 369 0.5× 495 1.0× 85 0.2× 396 1.6× 20 1.2k
Josep López-Santı́n Spain 19 694 0.9× 284 0.4× 287 0.6× 77 0.2× 194 0.8× 62 1.0k
Noshi Minamiura Japan 19 592 0.8× 522 0.7× 161 0.3× 379 1.0× 234 1.0× 81 1.2k
Masafumi Hidaka Japan 17 555 0.7× 484 0.7× 190 0.4× 264 0.7× 108 0.4× 49 928
Toshio Fukui Japan 26 1.0k 1.4× 450 0.6× 120 0.2× 355 1.0× 493 2.0× 109 1.7k
Kuniki Kino Japan 22 706 0.9× 169 0.2× 186 0.4× 69 0.2× 101 0.4× 62 1.1k
Kazutoshi Fujii Japan 15 418 0.6× 695 1.0× 216 0.4× 468 1.3× 257 1.0× 24 1.0k
Nancy A. Da Silva United States 27 1.7k 2.3× 328 0.5× 805 1.6× 38 0.1× 151 0.6× 59 2.3k
Jindřich Volc Czechia 26 967 1.3× 355 0.5× 347 0.7× 35 0.1× 1.0k 4.1× 52 1.7k

Countries citing papers authored by Thijs Kaper

Since Specialization
Citations

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

Fields of papers citing papers by Thijs Kaper

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Thijs Kaper

This figure shows the co-authorship network connecting the top 25 collaborators of Thijs Kaper. A scholar is included among the top collaborators of Thijs Kaper 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 Thijs Kaper. Thijs Kaper 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.
Karkehabadi, Saeid, Henrik Hansson, Nils Mikkelsen, et al.. (2018). Structural studies of a glycoside hydrolase family 3 β-glucosidase from the model fungusNeurospora crassa. Acta Crystallographica Section F Structural Biology Communications. 74(12). 787–796. 14 indexed citations
2.
Hansson, Henrik, Saeid Karkehabadi, Nils Mikkelsen, et al.. (2017). High-resolution structure of a lytic polysaccharide monooxygenase from Hypocrea jecorina reveals a predicted linker as an integral part of the catalytic domain. Journal of Biological Chemistry. 292(46). 19099–19109. 58 indexed citations
3.
Gudmundsson, Mikael, Henrik Hansson, Saeid Karkehabadi, et al.. (2016). Structural and functional studies of the glycoside hydrolase family 3 β-glucosidase Cel3A from the moderately thermophilic fungusRasamsonia emersonii. Acta Crystallographica Section D Structural Biology. 72(7). 860–870. 29 indexed citations
4.
Karkehabadi, Saeid, K.E. Helmich, Thijs Kaper, et al.. (2014). Biochemical Characterization and Crystal Structures of a Fungal Family 3 β-Glucosidase, Cel3A from Hypocrea jecorina. Journal of Biological Chemistry. 289(45). 31624–31637. 69 indexed citations
5.
Lantz, Suzanne E., Frits Goedegebuur, R. W. J. Hommes, et al.. (2010). Hypocrea jecorina CEL6A protein engineering. Biotechnology for Biofuels. 3(1). 20–20. 54 indexed citations
6.
Kaper, Thijs, et al.. (2009). Improving low‐temperature activity of Sulfolobus acidocaldarius 2‐keto‐3‐deoxygluconate aldolase. Archaea. 2(4). 233–239. 11 indexed citations
7.
Wallace, Louise, et al.. (2009). Determination of Product Inhibition of CBH1, CBH2, and EG1 Using a Novel Cellulase Activity Assay. Applied Biochemistry and Biotechnology. 161(1-8). 313–317. 29 indexed citations
8.
Kaper, Thijs, et al.. (2008). Fluorescence resonance energy transfer sensors for quantitative monitoring of pentose and disaccharide accumulation in bacteria. Biotechnology for Biofuels. 1(1). 11–11. 54 indexed citations
9.
Kaper, Thijs, Loren L. Looger, Hitomi Takanaga, et al.. (2007). Nanosensor Detection of an Immunoregulatory Tryptophan Influx/Kynurenine Efflux Cycle. PLoS Biology. 5(10). e257–e257. 98 indexed citations
10.
Barends, T.R.M., Jelle B. Bultema, Thijs Kaper, et al.. (2007). Three-way Stabilization of the Covalent Intermediate in Amylomaltase, an α-Amylase-like Transglycosylase. Journal of Biological Chemistry. 282(23). 17242–17249. 64 indexed citations
11.
Ozimek, Łukasz, Slavko Kralj, Thijs Kaper, Marc J. E. C. van der Maarel, & Lubbert Dijkhuizen. (2006). Single amino acid residue changes in subsite − 1 of inulosucrase from Lactobacillus reuteri 121 strongly influence the size of products synthesized. FEBS Journal. 273(17). 4104–4113. 40 indexed citations
12.
Maarel, Marc J. E. C. van der, et al.. (2005). A Novel Thermoreversible Gelling Product Made by Enzymatic Modification of Starch. Starch - Stärke. 57(12). 634–634. 1 indexed citations
13.
Kaper, Thijs, Stan J. J. Brouns, Ans C. M. Geerling, Willem M. de Vos, & John van der Oost. (2002). DNA family shuffling of hyperthermostable β-glycosidases. Biochemical Journal. 368(2). 461–470. 31 indexed citations
14.
Chiaraluce, Roberta, John van der Oost, Joyce H.G. Lebbink, Thijs Kaper, & Valerio Consalvi. (2002). Persistence of Tertiary Structure in 7.9 M Guanidinium Chloride:  The Case of Endo-β-1,3-glucanase from Pyrococcus furiosus. Biochemistry. 41(49). 14624–14632. 14 indexed citations
15.
Lebbink, Joyce H.G., Thijs Kaper, Servé W. M. Kengen, John van der Oost, & Willem M. de Vos. (2001). β-glucosidase CelB from Pyrococcus furiosus: Production by Escherichia coli, purification, and in vitro evolution. Methods in enzymology on CD-ROM/Methods in enzymology. 330. 364–379. 24 indexed citations
16.
Kaper, Thijs, Joyce H.G. Lebbink, Leon Kluskens, et al.. (2001). Characterization of β-glycosylhydrolases from Pyrococcus furiosus. Methods in enzymology on CD-ROM/Methods in enzymology. 330. 329–346. 16 indexed citations
17.
Hansson, Therése, Thijs Kaper, John van der Oost, Willem M. de Vos, & Patrick Adlercreutz. (2001). Improved oligosaccharide synthesis by protein engineering of β‐glucosidase CelB from hyperthermophilic Pyrococcus furiosus. Biotechnology and Bioengineering. 73(3). 203–210. 67 indexed citations
18.
Kaper, Thijs, et al.. (2001). The catalytic potency of β-glucosidase from Pyrococcus furiosus in the direct glucosylation reaction. Enzyme and Microbial Technology. 29(10). 621–624. 7 indexed citations
19.
Pouwels, Jeroen, Marco Moracci, Beatrice Cobucci‐Ponzano, et al.. (2000). Activity and stability of hyperthermophilic enzymes: a comparative study on two archaeal β-glycosidases. Extremophiles. 4(3). 157–164. 29 indexed citations
20.
Kaper, Thijs, Joyce H.G. Lebbink, Jeroen Pouwels, et al.. (2000). Comparative Structural Analysis and Substrate Specificity Engineering of the Hyperthermostable β-Glucosidase CelB from Pyrococcus furiosus. Biochemistry. 39(17). 4963–4970. 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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