Wim Nerinckx

2.4k total citations
42 papers, 1.8k citations indexed

About

Wim Nerinckx is a scholar working on Biotechnology, Molecular Biology and Biomedical Engineering. According to data from OpenAlex, Wim Nerinckx has authored 42 papers receiving a total of 1.8k indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Biotechnology, 22 papers in Molecular Biology and 19 papers in Biomedical Engineering. Recurrent topics in Wim Nerinckx's work include Enzyme Production and Characterization (25 papers), Biofuel production and bioconversion (19 papers) and Carbohydrate Chemistry and Synthesis (11 papers). Wim Nerinckx is often cited by papers focused on Enzyme Production and Characterization (25 papers), Biofuel production and bioconversion (19 papers) and Carbohydrate Chemistry and Synthesis (11 papers). Wim Nerinckx collaborates with scholars based in Belgium, Greece and Sweden. Wim Nerinckx's co-authors include Marc Claeyssens, Paul Christakopoulos, Peter Vandenabeele, Ria Roelandt, Tom Desmet, Nico Callewaert, Nozomi Takahashi, M. Vandewalle, Vera Goossens and Koen Augustyns and has published in prestigious journals such as Journal of Biological Chemistry, Nature Communications and Nature Biotechnology.

In The Last Decade

Wim Nerinckx

41 papers receiving 1.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Wim Nerinckx Belgium 21 1.0k 695 662 278 258 42 1.8k
Elena Catanzaro Italy 21 738 0.7× 235 0.3× 136 0.2× 156 0.6× 144 0.6× 39 1.7k
Sankar Mohan Canada 23 842 0.8× 69 0.1× 259 0.4× 95 0.3× 499 1.9× 43 1.9k
Takuo Yamamoto Japan 16 637 0.6× 100 0.1× 237 0.4× 142 0.5× 45 0.2× 38 1.1k
Jun‐yong Choe United States 25 1.1k 1.0× 137 0.2× 67 0.1× 257 0.9× 156 0.6× 52 1.6k
Donald Wojciechowicz United States 19 713 0.7× 60 0.1× 113 0.2× 100 0.4× 284 1.1× 31 1.5k
Ling Fu China 19 917 0.9× 71 0.1× 71 0.1× 391 1.4× 182 0.7× 31 1.7k
Alessia Garufi Italy 20 1.3k 1.3× 79 0.1× 73 0.1× 94 0.3× 198 0.8× 38 2.2k
Rama Rao Malla India 18 750 0.7× 194 0.3× 55 0.1× 92 0.3× 105 0.4× 65 1.4k
Margherita Eufemi Italy 23 820 0.8× 42 0.1× 121 0.2× 157 0.6× 60 0.2× 59 1.3k
Jana Jakubı́ková Slovakia 28 1.4k 1.4× 69 0.1× 56 0.1× 197 0.7× 191 0.7× 78 2.2k

Countries citing papers authored by Wim Nerinckx

Since Specialization
Citations

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

Fields of papers citing papers by Wim Nerinckx

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Wim Nerinckx

This figure shows the co-authorship network connecting the top 25 collaborators of Wim Nerinckx. A scholar is included among the top collaborators of Wim Nerinckx 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 Wim Nerinckx. Wim Nerinckx 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.
Félix, Jan, João Paulo Portela Catani, Kenny Roose, et al.. (2025). Single-domain antibodies directed against hemagglutinin and neuraminidase protect against influenza B viruses. Nature Communications. 16(1). 5831–5831.
2.
Schie, Loes van, Wander Van Breedam, Bert Schepens, et al.. (2023). GlycoVHH: optimal sites for introducing N-glycans on the camelid VHH antibody scaffold and use for macrophage delivery. mAbs. 15(1). 2210709–2210709. 6 indexed citations
3.
Vlieger, Dorien De, Inge Van Molle, Wim Nerinckx, et al.. (2019). Selective Engagement of FcγRIV by a M2e-Specific Single Domain Antibody Construct Protects Against Influenza A Virus Infection. Frontiers in Immunology. 10. 2920–2920. 16 indexed citations
4.
Takahashi, Nozomi, Linde Duprez, Sasker Grootjans, et al.. (2012). Necrostatin-1 analogues: critical issues on the specificity, activity and in vivo use in experimental disease models. Cell Death and Disease. 3(11). e437–e437. 369 indexed citations
5.
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
6.
Rougé, Pierre, Wim Nerinckx, Clare Gough, Jean‐Jacques Bono, & Annick Barre. (2011). Docking of Chitin Oligomers and Nod Factors on Lectin Domains of the LysM-RLK Receptors in the Medicago-Rhizobium Symbiosis. Advances in experimental medicine and biology. 705. 511–521. 1 indexed citations
7.
Lobsanov, Yuri D., Takashi Yoshida, Tom Desmet, et al.. (2008). Modulation of activity by Arg407: structure of a fungal α-1,2-mannosidase in complex with a substrate analogue. Acta Crystallographica Section D Biological Crystallography. 64(3). 227–236. 3 indexed citations
8.
Cantu, David C., Wim Nerinckx, & Peter J. Reilly. (2008). Theory and computation show that Asp463 is the catalytic proton donor in human endoplasmic reticulum α-(1→2)-mannosidase I. Carbohydrate Research. 343(13). 2235–2242. 6 indexed citations
9.
Nerinckx, Wim, et al.. (2006). The fate of β-d-mannopyranose after its formation by endoplasmic reticulum α-(1→2)-mannosidase I catalysis. Carbohydrate Research. 342(2). 163–169. 9 indexed citations
10.
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
11.
Sandra, Koen, et al.. (2004). Evaluation of automated nano‐electrospray mass spectrometry in the determination of non‐covalent protein–ligand complexes. Rapid Communications in Mass Spectrometry. 18(24). 3061–3067. 26 indexed citations
12.
Hägglund, Per, et al.. (2003). A cellulose-binding module of the Trichoderma reesei β-mannanase Man5A increases the mannan-hydrolysis of complex substrates. Journal of Biotechnology. 101(1). 37–48. 82 indexed citations
13.
Katapodis, Petros, Mária Vršanská, Dimitris Kekos, et al.. (2003). Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Sporotrichum thermophile. Carbohydrate Research. 338(18). 1881–1890. 43 indexed citations
14.
Nerinckx, Wim, Tom Desmet, & Marc Claeyssens. (2003). A hydrophobic platform as a mechanistically relevant transition state stabilising factor appears to be present in the active centre of all glycoside hydrolases. FEBS Letters. 538(1-3). 1–7. 43 indexed citations
15.
Parry, Neil, D. E. Beever, E. Owen, et al.. (2002). Biochemical characterization and mode of action of a thermostable endoglucanase purified from Thermoascus aurantiacus. Archives of Biochemistry and Biophysics. 404(2). 243–253. 57 indexed citations
16.
Desmet, Tom, Wim Nerinckx, Ingeborg Stals, et al.. (2002). Novel tools for the study of class I α-mannosidases: a chromogenic substrate and a substrate-analog inhibitor. Analytical Biochemistry. 307(2). 361–367. 8 indexed citations
17.
Andrews, Simon, Simon J. Charnock, Jeremy H. Lakey, et al.. (2000). Substrate Specificity in Glycoside Hydrolase Family 10. Journal of Biological Chemistry. 275(30). 23027–23033. 55 indexed citations
18.
Zou, Jinyu, Gerard J. Kleywegt, Jerry Ståhlberg, et al.. (1999). Crystallographic evidence for substrate ring distortion and protein conformational changes during catalysis in cellobiohydrolase Ce16A from Trichoderma reesei. Structure. 7(9). 1035–1045. 137 indexed citations
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.
Ryan, James W., Peter Biely, Mária Vršanská, et al.. (1998). Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Thermomyces lanuginosus ATCC 46882. Carbohydrate Research. 306(3). 445–455. 75 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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