Kathleen Piens

2.2k total citations
31 papers, 1.2k citations indexed

About

Kathleen Piens is a scholar working on Biomedical Engineering, Biotechnology and Molecular Biology. According to data from OpenAlex, Kathleen Piens has authored 31 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Biomedical Engineering, 20 papers in Biotechnology and 17 papers in Molecular Biology. Recurrent topics in Kathleen Piens's work include Biofuel production and bioconversion (22 papers), Enzyme Production and Characterization (19 papers) and Polysaccharides and Plant Cell Walls (10 papers). Kathleen Piens is often cited by papers focused on Biofuel production and bioconversion (22 papers), Enzyme Production and Characterization (19 papers) and Polysaccharides and Plant Cell Walls (10 papers). Kathleen Piens collaborates with scholars based in Belgium, Sweden and United States. Kathleen Piens's co-authors include Tuula T. Teeri, Mats Sandgren, Marc Claeyssens, Henrik Hansson, Harry Brumer, Saeid Karkehabadi, Colin Mitchinson, Steve Kim, Jerry Ståhlberg and Rebecca Van Acker 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

Kathleen Piens

31 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Kathleen Piens Belgium 18 721 719 492 439 165 31 1.2k
Farid M. Ibatullin Russia 20 502 0.7× 372 0.5× 331 0.7× 509 1.2× 256 1.6× 28 1.0k
Ingeborg Stals Belgium 18 718 1.0× 661 0.9× 567 1.2× 253 0.6× 90 0.5× 27 1.2k
Kazuhide Totani Japan 16 469 0.7× 296 0.4× 207 0.4× 137 0.3× 163 1.0× 39 870
Markus Alahuhta United States 15 527 0.7× 525 0.7× 318 0.6× 202 0.5× 38 0.2× 38 886
Emilio Margolles‐Clark United States 17 571 0.8× 494 0.7× 393 0.8× 300 0.7× 39 0.2× 21 972
C.M. Bianchetti United States 15 313 0.4× 402 0.6× 200 0.4× 209 0.5× 30 0.2× 20 807
Naoto Tonouchi Japan 19 374 0.5× 412 0.6× 283 0.6× 306 0.7× 26 0.2× 36 995
Takashi Kawaguchi Japan 21 829 1.1× 592 0.8× 744 1.5× 279 0.6× 39 0.2× 46 1.2k
Katsuya Ozaki Japan 25 1.1k 1.6× 502 0.7× 1.1k 2.2× 415 0.9× 19 0.1× 67 1.8k
Andrea Strazzulli Italy 16 525 0.7× 168 0.2× 305 0.6× 74 0.2× 158 1.0× 36 783

Countries citing papers authored by Kathleen Piens

Since Specialization
Citations

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

Fields of papers citing papers by Kathleen Piens

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kathleen Piens

This figure shows the co-authorship network connecting the top 25 collaborators of Kathleen Piens. A scholar is included among the top collaborators of Kathleen Piens 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 Kathleen Piens. Kathleen Piens 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.
Costain, Willard J., Arsalan S. Haqqani, Greg Hussack, et al.. (2025). In vivo brain delivery of BBB-enabled iduronate 2-sulfatase in rats. Fluids and Barriers of the CNS. 22(1). 7–7. 2 indexed citations
2.
Geronimo, Inacrist, Kathleen Piens, Mikael Gudmundsson, et al.. (2019). Kinetic and molecular dynamics study of inhibition and transglycosylation in Hypocrea jecorina family 3 β-glucosidases. Journal of Biological Chemistry. 294(9). 3169–3180. 9 indexed citations
3.
Acker, Rebecca Van, Ruben Vanholme, Kathleen Piens, & Wout Boerjan. (2016). Saccharification Protocol for Small-scale Lignocellulosic Biomass Samples to Test Processing of Cellulose into Glucose. BIO-PROTOCOL. 6(1). 26 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.
Acker, Rebecca Van, Jean‐Charles Leplé, Dirk Aerts, et al.. (2013). Improved saccharification and ethanol yield from field-grown transgenic poplar deficient in cinnamoyl-CoA reductase. Proceedings of the National Academy of Sciences. 111(2). 845–850. 155 indexed citations
6.
Karkehabadi, Saeid, Henrik Hansson, Frits Goedegebuur, et al.. (2013). The Crystal Structure of the Core Domain of a Cellulose Induced Protein (Cip1) from Hypocrea jecorina, at 1.5 Å Resolution. PLoS ONE. 8(9). e70562–e70562. 11 indexed citations
7.
Tiels, Petra, E.V. Baranova, Kathleen Piens, et al.. (2012). A bacterial glycosidase enables mannose-6-phosphate modification and improved cellular uptake of yeast-produced recombinant human lysosomal enzymes. Nature Biotechnology. 30(12). 1225–1231. 82 indexed citations
8.
Wu, Miao, Wim Nerinckx, Kathleen Piens, et al.. (2012). Rational design, synthesis, evaluation and enzyme–substrate structures of improved fluorogenic substrates for family 6 glycoside hydrolases. FEBS Journal. 280(1). 184–198. 11 indexed citations
9.
Desmet, Tom, Marc Claeyssens, Kathleen Piens, & Wim Nerinckx. (2010). Synthesis and Evaluation of 2-Deoxy-2-amino-β-cellobiosides as Cellulase Inhibitors. Journal of Carbohydrate Chemistry. 29(4). 164–180. 1 indexed citations
10.
Piens, Kathleen, Régis Fauré, Martin Baumann, et al.. (2008). Mechanism-based Labeling Defines the Free Energy Change for Formation of the Covalent Glycosyl-enzyme Intermediate in a Xyloglucan endo-Transglycosylase. Journal of Biological Chemistry. 283(32). 21864–21872. 16 indexed citations
11.
Sandström, Corine, Kathleen Piens, Emma R. Master, et al.. (2008). Comparative NMR Analysis of Cellooligosaccharide Hydrolysis by GH9 Bacterial and Plant Endo-1,4-β-glucanases. Biochemistry. 47(18). 5235–5241. 9 indexed citations
12.
Karkehabadi, Saeid, Henrik Hansson, Steve Kim, et al.. (2008). The First Structure of a Glycoside Hydrolase Family 61 Member, Cel61B from Hypocrea jecorina, at 1.6 Å Resolution. Journal of Molecular Biology. 383(1). 144–154. 158 indexed citations
13.
Desmet, Tom, Tineke Cantaert, Peter Gualfetti, et al.. (2006). An investigation of the substrate specificity of the xyloglucanase Cel74A from Hypocrea jecorina. FEBS Journal. 274(2). 356–363. 38 indexed citations
14.
Kallas, Åsa, Kathleen Piens, Stuart E. Denman, et al.. (2005). Enzymatic properties of native and deglycosylated hybrid aspen (Populus tremula×tremuloides) xyloglucan endotransglycosylase 16A expressed in Pichia pastoris. Biochemical Journal. 390(1). 105–113. 72 indexed citations
15.
Ossowski, Ingemar von, Jerry Ståhlberg, Anu Koivula, et al.. (2003). Engineering the Exo-loop of Cellobiohydrolase, Cel7A. A comparison with Cel7D. University of Huddersfield Repository (University of Huddersfield). 2 indexed citations
16.
Becker, D. E., Harry Brumer, Marc Claeyssens, et al.. (2001). Engineering of a glycosidase Family 7 cellobiohydrolase to more alkaline pH optimum: the pH behaviour of Trichoderma reesei Cel7A and its E223S/ A224H/L225V/T226A/D262G mutant. Biochemical Journal. 356(1). 19–19. 54 indexed citations
17.
Maras, Marleen, Nico Callewaert, Kathleen Piens, et al.. (2000). Molecular cloning and enzymatic characterization of a Trichoderma reesei 1,2-α-d-mannosidase. Journal of Biotechnology. 77(2-3). 255–263. 49 indexed citations
18.
19.
Claeyssens, Marc, et al.. (1998). Carbohydrates [i.e. Carbohydrases] from Trichoderma reesei and other microorganisms : structures, biochemistry, genetics and applications. 5 indexed citations
20.
Maras, Marleen, Xavier Saelens, Wouter Laroy, et al.. (1997). In vitro Conversion of the Carbohydrate Moiety of Fungal Glycoproteins to Mammalian‐type Oligosaccharides. European Journal of Biochemistry. 249(3). 701–707. 16 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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