Natalie De Jonge

614 total citations
17 papers, 459 citations indexed

About

Natalie De Jonge is a scholar working on Molecular Biology, Molecular Medicine and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, Natalie De Jonge has authored 17 papers receiving a total of 459 indexed citations (citations by other indexed papers that have themselves been cited), including 9 papers in Molecular Biology, 6 papers in Molecular Medicine and 5 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in Natalie De Jonge's work include Antibiotic Resistance in Bacteria (6 papers), Bacterial Genetics and Biotechnology (5 papers) and Monoclonal and Polyclonal Antibodies Research (4 papers). Natalie De Jonge is often cited by papers focused on Antibiotic Resistance in Bacteria (6 papers), Bacterial Genetics and Biotechnology (5 papers) and Monoclonal and Polyclonal Antibodies Research (4 papers). Natalie De Jonge collaborates with scholars based in Belgium, Slovenia and France. Natalie De Jonge's co-authors include Remy Loris, Sarah Haesaerts, Abel Garcia‐Pino, Henri De Greve, Jurij Lah, L. Buts, Klaus Zangger, Lode Wyns, Daniël Charlier and Christophe Blanchetot and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Journal of Clinical Investigation.

In The Last Decade

Natalie De Jonge

17 papers receiving 455 citations

Peers

Natalie De Jonge
Silke R. Vedelaar Netherlands
Linda Foit United States
Wesley Martin United States
David Shultis United States
Sandrine Guillard United Kingdom
S Lepage Belgium
Justin R. Klesmith United States
Silke R. Vedelaar Netherlands
Natalie De Jonge
Citations per year, relative to Natalie De Jonge Natalie De Jonge (= 1×) peers Silke R. Vedelaar

Countries citing papers authored by Natalie De Jonge

Since Specialization
Citations

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

Fields of papers citing papers by Natalie De Jonge

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Natalie De Jonge. 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 Natalie De Jonge. The network helps show where Natalie De Jonge may publish in the future.

Co-authorship network of co-authors of Natalie De Jonge

This figure shows the co-authorship network connecting the top 25 collaborators of Natalie De Jonge. A scholar is included among the top collaborators of Natalie De Jonge 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 Natalie De Jonge. Natalie De Jonge is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

17 of 17 papers shown
1.
Verma, Mayank, Nan Liu, Brian K. Miller, et al.. (2021). VEGFR-1/Flt-1 inhibition increases angiogenesis and improves muscle function in a mouse model of Duchenne muscular dystrophy. Molecular Therapy — Methods & Clinical Development. 21. 369–381. 12 indexed citations
2.
Zorzini, Valentina, Jurij Lah, Yann G.‐J. Sterckx, et al.. (2016). Substrate Recognition and Activity Regulation of the Escherichia coli mRNA Endonuclease MazF. Journal of Biological Chemistry. 291(21). 10950–10960. 42 indexed citations
3.
Godar, Marie, Virginia Morello, Anna Hultberg, et al.. (2016). Dual anti-idiotypic purification of a novel, native-format biparatopic anti-MET antibody with improved in vitro and in vivo efficacy. Scientific Reports. 6(1). 31621–31621. 13 indexed citations
4.
Blanchetot, Christophe, Natalie De Jonge, Aline Desmyter, et al.. (2016). Structural Mimicry of Receptor Interaction by Antagonistic Interleukin-6 (IL-6) Antibodies. Journal of Biological Chemistry. 291(26). 13846–13854. 28 indexed citations
5.
Rolfo, Christian, Philippe Aftimos, Jean‐René Pallandre, et al.. (2016). ARGX-111 shows activity in MET-amplified patients in a phase-I study and in preclinical models of myeloid-derived suppressor cell (MDSC) depletion in the tumor microenvironment.. Journal of Clinical Oncology. 34(15_suppl). e14016–e14016. 1 indexed citations
6.
Klarenbeek, A., Aline Desmyter, Christophe Blanchetot, et al.. (2015). Camelid Ig V genes reveal significant human homology not seen in therapeutic target genes, providing for a powerful therapeutic antibody platform. mAbs. 7(4). 693–706. 74 indexed citations
7.
Hanssens, Valérie, Natalie De Jonge, Anna Hultberg, et al.. (2015). The clinical potential of ARGX-111, an afucosylated anti-MET antibody, in hematological malignancies and suppression of metastasis. Annals of Oncology. 26. ii31–ii31. 3 indexed citations
8.
Aftimos, Philippe, Philippe Barthélémy, Christian Rolfo, et al.. (2015). A phase I, first-in-human study of argx-111, a monoclonal antibody targeting c-met in patients with solid tumors.. Journal of Clinical Oncology. 33(15_suppl). 2580–2580. 15 indexed citations
9.
Basilico, Cristina, Anna Hultberg, Christophe Blanchetot, et al.. (2014). Four individually druggable MET hotspots mediate HGF-driven tumor progression. Journal of Clinical Investigation. 124(7). 3172–3186. 41 indexed citations
10.
Drobnak, Igor, Natalie De Jonge, Sarah Haesaerts, et al.. (2013). Energetic Basis of Uncoupling Folding from Binding for an Intrinsically Disordered Protein. Journal of the American Chemical Society. 135(4). 1288–1294. 40 indexed citations
11.
Jonge, Natalie De, L. Buts, Sarah Haesaerts, et al.. (2012). Alternative interactions define gyrase specificity in the CcdB family. Molecular Microbiology. 84(5). 965–978. 13 indexed citations
12.
Jonge, Natalie De, W Hohlweg, Abel Garcia‐Pino, et al.. (2009). Structural and Thermodynamic Characterization of Vibrio fischeri CcdB. Journal of Biological Chemistry. 285(8). 5606–5613. 15 indexed citations
13.
Jonge, Natalie De, Abel Garcia‐Pino, L. Buts, et al.. (2009). Rejuvenation of CcdB-Poisoned Gyrase by an Intrinsically Disordered Protein Domain. Molecular Cell. 35(2). 154–163. 128 indexed citations
14.
Respondek, Michal, L. Buts, Natalie De Jonge, et al.. (2009). Sequence-specific 1H, 15N and 13C resonance assignments of the 23.7-kDa homodimeric toxin CcdB from Vibrio fischeri. Biomolecular NMR Assignments. 3(1). 145–147. 1 indexed citations
15.
Jonge, Natalie De, et al.. (2009). Driving Forces of Gyrase Recognition by the Addiction Toxin CcdB. Journal of Biological Chemistry. 284(30). 20002–20010. 22 indexed citations
16.
Jonge, Natalie De, L. Buts, Natacha Mine, et al.. (2007). Purification and crystallization ofVibrio fischeriCcdB and its complexes with fragments of gyrase and CcdA. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63(4). 356–360. 7 indexed citations
17.
Buts, L., Natalie De Jonge, Remy Loris, Lode Wyns, & Minh‐Hoa Dao‐Thi. (2005). Crystallization of the C-terminal domain of the addiction antidote CcdA in complex with its toxin CcdB. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(10). 949–952. 4 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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