Christine Kellenberger

610 total citations
18 papers, 498 citations indexed

About

Christine Kellenberger is a scholar working on Immunology, Molecular Biology and Immunology and Allergy. According to data from OpenAlex, Christine Kellenberger has authored 18 papers receiving a total of 498 indexed citations (citations by other indexed papers that have themselves been cited), including 10 papers in Immunology, 5 papers in Molecular Biology and 5 papers in Immunology and Allergy. Recurrent topics in Christine Kellenberger's work include Insect symbiosis and bacterial influences (4 papers), Invertebrate Immune Response Mechanisms (4 papers) and Neurobiology and Insect Physiology Research (4 papers). Christine Kellenberger is often cited by papers focused on Insect symbiosis and bacterial influences (4 papers), Invertebrate Immune Response Mechanisms (4 papers) and Neurobiology and Insect Physiology Research (4 papers). Christine Kellenberger collaborates with scholars based in France, Switzerland and United States. Christine Kellenberger's co-authors include Alain Roussel, Philippe Leone, Renaud Vincentelli, F Coste, Bang Luu, Hélène Hietter, Onya Opota, Bruno Lemaître, Christian Boudier and Isabel Bermúdez and has published in prestigious journals such as Journal of Biological Chemistry, The Journal of Immunology and Biochemistry.

In The Last Decade

Christine Kellenberger

18 papers receiving 496 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Christine Kellenberger France 12 264 208 190 125 45 18 498
David Kuttenkeuler Germany 5 288 1.1× 128 0.6× 343 1.8× 87 0.7× 51 1.1× 5 613
Tamara Zoranovic United States 9 217 0.8× 126 0.6× 221 1.2× 93 0.7× 20 0.4× 11 479
Candace Swimmer United States 14 377 1.4× 247 1.2× 539 2.8× 119 1.0× 30 0.7× 16 959
Young-Lan Song South Korea 6 156 0.6× 59 0.3× 250 1.3× 43 0.3× 31 0.7× 7 436
Steven Rodems United States 11 176 0.7× 122 0.6× 549 2.9× 41 0.3× 27 0.6× 20 836
Kate Senger United States 15 465 1.8× 94 0.5× 781 4.1× 80 0.6× 137 3.0× 19 1.2k
Siegfried Bialojan Germany 8 65 0.2× 89 0.4× 257 1.4× 40 0.3× 16 0.4× 9 429
Ursula Wiedemann Australia 7 107 0.4× 33 0.2× 376 2.0× 67 0.5× 6 0.1× 8 718
Joseph A. D’Alessio United States 10 50 0.2× 68 0.3× 350 1.8× 19 0.2× 22 0.5× 12 569
Vasantha Kumar United States 8 138 0.5× 118 0.6× 219 1.2× 30 0.2× 34 0.8× 8 361

Countries citing papers authored by Christine Kellenberger

Since Specialization
Citations

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

Fields of papers citing papers by Christine Kellenberger

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Christine Kellenberger

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

All Works

18 of 18 papers shown
1.
Brier, Sébastien, Maxime Le Mignon, K. Jain, et al.. (2017). Characterization of epitope specificities of reference antibodies used for the quantification of the birch pollen allergen Bet v 1. Allergy. 73(5). 1032–1040. 16 indexed citations
2.
Korkmaz, Brice, Adam Lesner, Magdalena Wysocka, et al.. (2016). Inhibitors and Antibody Fragments as Potential Anti-Inflammatory Therapeutics Targeting Neutrophil Proteinase 3 in Human Disease. Pharmacological Reviews. 68(3). 603–630. 26 indexed citations
3.
Bouley, Julien, K. Jain, Sonia Luce, et al.. (2016). Sialylated Fetuin-A as a candidate predictive biomarker for successful grass pollen allergen immunotherapy. Journal of Allergy and Clinical Immunology. 140(3). 759–770.e13. 8 indexed citations
4.
Leone, Philippe, Cecilia Bebeacua, Onya Opota, et al.. (2015). X-ray and Cryo-electron Microscopy Structures of Monalysin Pore-forming Toxin Reveal Multimerization of the Pro-form. Journal of Biological Chemistry. 290(21). 13191–13201. 24 indexed citations
5.
Kellenberger, Christine, Sandrine Dallet‐Choisy, Marcin Sieńczyk, et al.. (2014). New Selective Peptidyl Di(chlorophenyl) Phosphonate Esters for Visualizing and Blocking Neutrophil Proteinase 3 in Human Diseases. Journal of Biological Chemistry. 289(46). 31777–31791. 34 indexed citations
6.
Kellenberger, Christine, et al.. (2013). Crystallization and preliminary X-ray analysis of monalysin, a novel β-pore-forming toxin from the entomopathogenPseudomonas entomophila. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 69(8). 930–933. 6 indexed citations
7.
Opota, Onya, Isabelle Vallet-Gély, Renaud Vincentelli, et al.. (2011). Monalysin, a Novel ß-Pore-Forming Toxin from the Drosophila Pathogen Pseudomonas entomophila, Contributes to Host Intestinal Damage and Lethality. PLoS Pathogens. 7(9). e1002259–e1002259. 84 indexed citations
8.
Coste, F, Philippe Leone, Renaud Vincentelli, et al.. (2011). The Drosophila peptidoglycan‐recognition protein LF interacts with peptidoglycan‐recognition protein LC to downregulate the Imd pathway. EMBO Reports. 12(4). 327–333. 67 indexed citations
9.
Kellenberger, Christine, Philippe Leone, Laurent Coquet, et al.. (2011). Structure-Function Analysis of Grass Clip Serine Protease Involved in Drosophila Toll Pathway Activation. Journal of Biological Chemistry. 286(14). 12300–12307. 29 indexed citations
10.
Castella, Sandrine, Hichem Lahouassa, M Jourdan, et al.. (2011). A substrate‐based approach to convert SerpinB1 into a specific inhibitor of proteinase 3, the Wegener's granulomatosis autoantigen. The FASEB Journal. 25(9). 3019–3031. 13 indexed citations
11.
Mishima, Yumiko, et al.. (2009). Expression, purification, crystallization and preliminary X-ray analysis of the N-terminal domain of GNBP3 fromDrosophila melanogaster. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65(9). 870–873. 4 indexed citations
12.
Mishima, Yumiko, Jessica Quintin, Vishukumar Aimanianda, et al.. (2009). The N-terminal Domain of Drosophila Gram-negative Binding Protein 3 (GNBP3) Defines a Novel Family of Fungal Pattern Recognition Receptors. Journal of Biological Chemistry. 284(42). 28687–28697. 49 indexed citations
13.
Leone, Philippe, Alain Roussel, & Christine Kellenberger. (2008). Structure ofLocusta migratoriaprotease inhibitor 3 (LMPI-3) in complex withFusarium oxysporumtrypsin. Acta Crystallographica Section D Biological Crystallography. 64(11). 1165–1171. 3 indexed citations
14.
Kellenberger, Christine, Alain Roussel, & Bernard Malissen. (2005). The H-2Kk MHC Peptide-Binding Groove Anchors the Backbone of an Octameric Antigenic Peptide in an Unprecedented Mode. The Journal of Immunology. 175(6). 3819–3825. 7 indexed citations
15.
Kellenberger, Christine, et al.. (2004). Expression, refolding, crystallization and preliminary crystallographic study of MHC H-2Kkcomplexed with octapeptides and nonapeptides. Acta Crystallographica Section D Biological Crystallography. 60(7). 1278–1280. 3 indexed citations
16.
Kellenberger, Christine, Gilles Ferrat, Philippe Leone, H. Darbon, & Alain Roussel. (2003). Selective Inhibition of Trypsins by Insect Peptides: Role of P6−P10 Loop. Biochemistry. 42(46). 13605–13612. 19 indexed citations
17.
Kellenberger, Christine, Christian Boudier, Isabel Bermúdez, et al.. (1995). Serine Protease Inhibition by Insect Peptides Containing a Cysteine Knot and a Triple-stranded β-Sheet. Journal of Biological Chemistry. 270(43). 25514–25519. 65 indexed citations
18.
Mer, Georges, Christine Kellenberger, Patrice Koehl, et al.. (1994). Solution Structure of PMP-D2, a 35-Residue Peptide Isolated from the Insect Locusta migratoria. Biochemistry. 33(51). 15397–15407. 41 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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