Sylvie Lachkar

5.4k total citations · 1 hit paper
36 papers, 3.6k citations indexed

About

Sylvie Lachkar is a scholar working on Molecular Biology, Cell Biology and Epidemiology. According to data from OpenAlex, Sylvie Lachkar has authored 36 papers receiving a total of 3.6k indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 19 papers in Cell Biology and 7 papers in Epidemiology. Recurrent topics in Sylvie Lachkar's work include Microtubule and mitosis dynamics (14 papers), Cellular transport and secretion (8 papers) and Cellular Mechanics and Interactions (8 papers). Sylvie Lachkar is often cited by papers focused on Microtubule and mitosis dynamics (14 papers), Cellular transport and secretion (8 papers) and Cellular Mechanics and Interactions (8 papers). Sylvie Lachkar collaborates with scholars based in France, Sweden and Spain. Sylvie Lachkar's co-authors include Patrick A. Curmi, André Sobel, M. Knossow, Benoı̂t Gigant, Isabelle Jourdain, Raimond B. G. Ravelli, Guido Kroemer, Elodie Charbaut, Maria Chiara Maiuri and Guillermo Mariño and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Sylvie Lachkar

35 papers receiving 3.5k citations

Hit Papers

Insight into tubulin regulation from a complex with colch... 2004 2026 2011 2018 2004 400 800 1.2k

Peers

Sylvie Lachkar
Robert Z. Qi Hong Kong
Pradipta Ghosh United States
Deborah Defeo-Jones United States
Frank W. Hobbs United States
Huilin Zhou United States
Asher Zilberstein United States
Robert Z. Qi Hong Kong
Sylvie Lachkar
Citations per year, relative to Sylvie Lachkar Sylvie Lachkar (= 1×) peers Robert Z. Qi

Countries citing papers authored by Sylvie Lachkar

Since Specialization
Citations

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

Fields of papers citing papers by Sylvie Lachkar

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Sylvie Lachkar

This figure shows the co-authorship network connecting the top 25 collaborators of Sylvie Lachkar. A scholar is included among the top collaborators of Sylvie Lachkar 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 Sylvie Lachkar. Sylvie Lachkar 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.
Nogueira-Recalde, Uxía, Flavia Lambertucci, Léa Montégut, et al.. (2025). Neutralization of acyl CoA binding protein (ACBP) for the experimental treatment of osteoarthritis. Cell Death and Differentiation. 32(8). 1484–1498. 2 indexed citations
2.
Campanacci, Valérie, Agathe Urvoas, Magali Aumont‐Nicaise, et al.. (2022). Structural convergence for tubulin binding of CPAP and vinca domain microtubule inhibitors. Proceedings of the National Academy of Sciences. 119(19). e2120098119–e2120098119. 4 indexed citations
3.
Liu, Peng, Liwei Zhao, Friedemann Loos, et al.. (2019). Immunosuppression by Mutated Calreticulin Released from Malignant Cells. Molecular Cell. 77(4). 748–760.e9. 73 indexed citations
4.
Loos, Friedemann, Wei Xie, Valentina Sica, et al.. (2019). Artificial tethering of LC3 or p62 to organelles is not sufficient to trigger autophagy. Cell Death and Disease. 10(10). 771–771. 15 indexed citations
5.
Liu, Peng, Liwei Zhao, Friedemann Loos, et al.. (2017). Identification of pharmacological agents that induce HMGB1 release. Scientific Reports. 7(1). 14915–14915. 39 indexed citations
6.
Niso‐Santano, Mireia, Shensi Shen, Sandy Adjemian, et al.. (2012). Direct interaction between STAT3 and EIF2AK2 controls fatty acid-induced autophagy. Autophagy. 9(3). 415–417. 47 indexed citations
7.
Poulain, Fabienne E., et al.. (2012). Specific Serine-Proline Phosphorylation and Glycogen Synthase Kinase 3β-directed Subcellular Targeting of Stathmin 3/Sclip in Neurons. Journal of Biological Chemistry. 287(26). 22341–22353. 11 indexed citations
8.
Shen, Shensi, Mireia Niso‐Santano, Sandy Adjemian, et al.. (2012). Cytoplasmic STAT3 Represses Autophagy by Inhibiting PKR Activity. Molecular Cell. 48(5). 667–680. 219 indexed citations
9.
Criollo, Alfredo, Mireia Niso‐Santano, Shoaib Ahmad Malik, et al.. (2011). Inhibition of autophagy by TAB2 and TAB3. The EMBO Journal. 30(24). 4908–4920. 80 indexed citations
10.
Cifuentes-Díaz, Carmen, O. Dubourg, Théano Irinopoulou, et al.. (2011). Nodes of Ranvier and Paranodes in Chronic Acquired Neuropathies. PLoS ONE. 6(1). e14533–e14533. 56 indexed citations
11.
Lachkar, Sylvie, Marion Lebois, Michel O. Steinmetz, et al.. (2010). Drosophila Stathmins Bind Tubulin Heterodimers with High and Variable Stoichiometries. Journal of Biological Chemistry. 285(15). 11667–11680. 15 indexed citations
12.
Cormier, Anthony, Marie‐Jeanne Clément, M. Knossow, et al.. (2009). The PN2-3 Domain of Centrosomal P4.1-associated Protein Implements a Novel Mechanism for Tubulin Sequestration. Journal of Biological Chemistry. 284(11). 6909–6917. 41 indexed citations
13.
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 →
14.
Bièche, Ivan, Alexandre Maucuer, Ingrid Laurendeau, et al.. (2003). Expression of stathmin family genes in human tissues: non-neural-restricted expression for SCLIP. Genomics. 81(4). 400–410. 53 indexed citations
15.
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
16.
Curmi, Patrick A., Catherine Noguès, Sylvie Lachkar, et al.. (2000). Overexpression of stathmin in breast carcinomas points out to highly proliferative tumours. British Journal of Cancer. 82(1). 142–150. 112 indexed citations
17.
Redeker, Virginie, Sylvie Lachkar, S. Siavoshian, et al.. (2000). Probing the Native Structure of Stathmin and Its Interaction Domains with Tubulin. Journal of Biological Chemistry. 275(10). 6841–6849. 36 indexed citations
18.
Bièche, Ivan, Sylvie Lachkar, Véronique Becette, et al.. (1998). Overexpression of the stathmin gene in a subset of human breast cancer. British Journal of Cancer. 78(6). 701–709. 86 indexed citations
19.
Akaaboune, Mohammed, et al.. (1998). Developmental regulation of the serpin, protease nexin I, localization during activity-dependent polyneuronal synapse elimination in mouse skeletal muscle. The Journal of Comparative Neurology. 397(4). 572–579. 26 indexed citations
20.
Lorenzo, Hans Kristian, Maurice Geuskens, Antonio Macho, et al.. (1996). Alpha-Fetoprotein Binding and Uptake by Primary Cultures of Human Skeletal Muscle. Tumor Biology. 17(4). 251–260. 15 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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