M. Knossow

8.2k total citations · 2 hit papers
81 papers, 6.7k citations indexed

About

M. Knossow is a scholar working on Molecular Biology, Cell Biology and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, M. Knossow has authored 81 papers receiving a total of 6.7k indexed citations (citations by other indexed papers that have themselves been cited), including 51 papers in Molecular Biology, 31 papers in Cell Biology and 28 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in M. Knossow's work include Microtubule and mitosis dynamics (30 papers), Monoclonal and Polyclonal Antibodies Research (28 papers) and Influenza Virus Research Studies (18 papers). M. Knossow is often cited by papers focused on Microtubule and mitosis dynamics (30 papers), Monoclonal and Polyclonal Antibodies Research (28 papers) and Influenza Virus Research Studies (18 papers). M. Knossow collaborates with scholars based in France, Israel and United Kingdom. M. Knossow's co-authors include Benoı̂t Gigant, Raimond B. G. Ravelli, Patrick A. Curmi, André Sobel, J.J. Skehel, Sylvie Lachkar, Isabelle Jourdain, Chunguang Wang, Thierry Bizebard and Yves Gaudin and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

M. Knossow

81 papers receiving 6.5k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain

2004 1.4k citations Raimond B. G. Ravelli, Benoı̂t Gigant et al. Nature profile →
Structural basis for the regulation of tubulin by vinblastine

2005 594 citations Benoı̂t Gigant, Chunguang Wang et al. Nature profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
M. Knossow France	38	3.8k	2.0k	1.4k	1.4k	767	81	6.7k
Nicholas K. Sauter United States	28	5.7k 1.5×	740 0.4×	555 0.4×	864 0.6×	394 0.5×	75	8.9k
Fred Naider United States	42	5.4k 1.4×	616 0.3×	907 0.6×	289 0.2×	612 0.8×	269	7.2k
Benoı̂t Gigant France	32	3.2k 0.8×	2.0k 1.0×	1.5k 1.1×	476 0.3×	409 0.5×	63	5.1k
Stefan M.V. Freund United Kingdom	61	9.3k 2.5×	1.2k 0.6×	458 0.3×	1.1k 0.8×	406 0.5×	153	11.3k
Deborah Fass Israel	39	3.8k 1.0×	1.5k 0.7×	318 0.2×	908 0.7×	545 0.7×	84	6.8k
Ben Webb United States	12	6.9k 1.8×	607 0.3×	373 0.3×	595 0.4×	518 0.7×	13	9.5k
Jens Schneider‐Mergener Germany	47	5.2k 1.4×	666 0.3×	357 0.2×	593 0.4×	1.4k 1.8×	124	7.5k
Daisuke Kohda Japan	47	4.6k 1.2×	629 0.3×	481 0.3×	521 0.4×	343 0.4×	150	6.7k
Stewart R. Durell United States	44	5.8k 1.5×	492 0.2×	655 0.5×	394 0.3×	349 0.5×	96	7.9k
Tim Elliott United Kingdom	52	4.0k 1.1×	613 0.3×	909 0.6×	797 0.6×	1.0k 1.3×	178	9.4k

Countries citing papers authored by M. Knossow

Since Specialization

Citations

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

Fields of papers citing papers by M. Knossow

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of M. Knossow

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

All Works

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20 of 20 papers shown

Cao, Luyan, Weiyi Wang, Qiyang Jiang, et al.. (2014). The structure of apo-kinesin bound to tubulin links the nucleotide cycle to movement. Nature Communications. 5(1). 5364–5364. 104 indexed citations

Gigant, Benoı̂t, Weiyi Wang, Birgit Dreier, et al.. (2013). Structure of a kinesin–tubulin complex and implications for kinesin motility. Nature Structural & Molecular Biology. 20(8). 1001–1007. 130 indexed citations

Wang, Weiyi, Qiyang Jiang, Manuela Argentini, et al.. (2012). Kif2C Minimal Functional Domain Has Unusual Nucleotide Binding Properties That Are Adapted to Microtubule Depolymerization. Journal of Biological Chemistry. 287(18). 15143–15153. 27 indexed citations

Cormier, Anthony, M. Knossow, Chunguang Wang, & Benoı̂t Gigant. (2010). The Binding of Vinca Domain Agents to Tubulin. Methods in cell biology. 95. 373–390. 21 indexed citations

Barbier, Pascale, Audrey Dorléans, François Devred, et al.. (2010). Stathmin and Interfacial Microtubule Inhibitors Recognize a Naturally Curved Conformation of Tubulin Dimers. Journal of Biological Chemistry. 285(41). 31672–31681. 85 indexed citations

Dorléans, Audrey, Benoı̂t Gigant, Raimond B. G. Ravelli, et al.. (2009). Variations in the colchicine-binding domain provide insight into the structural switch of tubulin. Proceedings of the National Academy of Sciences. 106(33). 13775–13779. 216 indexed citations

Knossow, M. & J.J. Skehel. (2006). Variation and infectivity neutralization in influenza. Immunology. 119(1). 1–7. 113 indexed citations

Hertzog, Maud, Carine van Heijenoort, Dominique Didry, et al.. (2004). The β-Thymosin/WH2 Domain. Cell. 117(5). 611–623. 170 indexed citations

Ravelli, Raimond B. G., Benoı̂t Gigant, Patrick A. Curmi, et al.. (2004). Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature. 428(6979). 198–202. 1360 indexed citations breakdown →

10.

Knossow, M., Thierry Bizebard, Benoı̂t Gigant, et al.. (2002). The mechanism of neutralization of influenza virus infectivity by antibodies. Acta Crystallographica Section A Foundations of Crystallography. 58(s1). c281–c281. 9 indexed citations

11.

Knossow, M., Martin Gaudier, A. R. Douglas, et al.. (2002). Mechanism of Neutralization of Influenza Virus Infectivity by Antibodies. Virology. 302(2). 294–298. 120 indexed citations

12.

Gigant, Benoı̂t, Patrick A. Curmi, Elodie Charbaut, et al.. (2000). The 4 Å X-Ray Structure of a Tubulin:Stathmin-like Domain Complex. Cell. 102(6). 809–816. 211 indexed citations

13.

Gigant, Benoı̂t, Takeshi Tsumuraya, Ikuo Fujii, & M. Knossow. (1999). Diverse structural solutions to catalysis in a family of antibodies. Structure. 7(11). 1385–1393. 17 indexed citations

14.

Fleury, Damien, Steve A. Wharton, J.J. Skehel, M. Knossow, & Thierry Bizebard. (1998). Antigen distortion allows influenza virus to escape neutralization. Nature Structural Biology. 5(2). 119–123. 106 indexed citations

15.

Gigant, Benoı̂t, et al.. (1998). Crossreactivity, efficiency and catalytic specificity of an esterase-like antibody. Journal of Molecular Biology. 284(3). 741–750. 9 indexed citations

16.

Gigant, Benoı̂t, Jean‐Baptiste Charbonnier, Béatrice Golinelli‐Pimpaneau, et al.. (1997). Mechanism of Inactivation of a Catalytic Antibody by P‐Nitrophenyl Esters. European Journal of Biochemistry. 246(2). 471–476. 9 indexed citations

17.

Gigant, Benoı̂t, Damien Fleury, Thierry Bizebard, J.J. Skehel, & M. Knossow. (1995). Crystallization and preliminary X‐ray diffraction studies of complexes between an influenza hemagglutinin and fab fragments of two different monoclonal antibodies. Proteins Structure Function and Bioinformatics. 23(1). 115–117. 15 indexed citations

18.

Golinelli‐Pimpaneau, Béatrice, Benoı̂t Gigant, Thierry Bizebard, et al.. (1994). Crystal structure of a catalytic antibody Fab with esterase- like activity. Structure. 2(3). 175–183. 52 indexed citations

19.

Bizebard, Thierry, et al.. (1990). Crystallization and preliminary X-ray diffraction studies of a monoclonal antibody Fab fragment specific for an influenza virus haemagglutinin and of an escape mutant of that haemagglutinin. Journal of Molecular Biology. 216(3). 513–514. 8 indexed citations

20.

Tsoucaris, G., et al.. (1983). Clathrates and Intercalates. Molecular crystals and liquid crystals. 96(1). 181–195. 3 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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