Job opening for a structural biologist to join the Structural Motility team at the Curie Institute Paris, France. We are looking for a post-doctoral fellow to join the Structural Motility team at the Curie Institute (Paris Center) directed by Anne Houdusse. The Structural Motility team at the Institut Curie has gathered important structural insights on how force generated by molecular motors can power cellular processes in human health and disease. We develop chemical biology and cell biology approaches to test these insights and understand how molecular motors produce force, how their activity is regulated and how they are recruited to their cellular targets. One of our goals is to develop specific modulators of the force they can produce. Many of these motors are also involved in human pathologies and their modulation could lead to new therapies. We are looking for an expert in biochemical, crystallogenesis and structural determination studies. The post-doctoral fellow will also gain expertise in functional and cellular studies. Energy and a strong will to quickly gain autonomy in the lead of exciting scientific projects are essential. Experience in cryo-electron microscopy or cell biology, is a plus. Experience in cloning, expression and purification of recombinant proteins, protein biophysics and/or biochemical assays are also welcome, and we are ready to train a dynamic and motivated candidate. If you are interested, please send a CV and a letter of motivation as well as letters of recommendation of your previous employers. Contact : Anne Houdusse (anne.houdu...@curie.fr<mailto:anne.houdu...@curie.fr>) https://science.institut-curie.org/research/multiscale-physics-biology-chemistry/umr144-subcellular-structure-and-cellular-dynamics/team-houdusse/ Key publications Julien Robert-Paganin, Olena Pylypenko, Carlos Kikuti, H Lee Sweeney, Anne Houdusse (2019 Nov 6) Force Generation by Myosin Motors: A Structural Perspective. Chemical reviews : 5-35 : DOI : 10.1021/acs.chemrev.9b00264<http://dx.doi.org/10.1021/acs.chemrev.9b00264>
Julien Robert-Paganin, Daniel Auguin, Anne Houdusse (2018 Oct 3) Hypertrophic cardiomyopathy disease results from disparate impairments of cardiac myosin function and auto-inhibition. Nature communications : 4019 : DOI : 10.1038/s41467-018-06191-4<http://dx.doi.org/10.1038/s41467-018-06191-4> Florian Blanc, Tatiana Isabet, Hannah Benisty, H Lee Sweeney, Marco Cecchini, Anne Houdusse (2018 May 31) An intermediate along the recovery stroke of myosin VI revealed by X-ray crystallography and molecular dynamics. Proceedings of the National Academy of Sciences of the United States of America : 6213-6218 : DOI : 10.1073/pnas.1711512115<http://dx.doi.org/10.1073/pnas.1711512115> Vicente J Planelles-Herrero, James J Hartman, Julien Robert-Paganin, Fady I Malik, Anne Houdusse (2017 Aug 5) Mechanistic and structural basis for activation of cardiac myosin force production by omecamtiv mecarbil. Nature communications : 190 : DOI : 10.1038/s41467-017-00176-5<http://dx.doi.org/10.1038/s41467-017-00176-5> I-Mei Yu, Vicente J Planelles-Herrero, Yannick Sourigues, Dihia Moussaoui, Helena Sirkia, Carlos Kikuti, David Stroebel, Margaret A Titus, Anne Houdusse (2017 Jun 30) Myosin 7 and its adaptors link cadherins to actin. Nature communications : 15864 : DOI : 10.1038/ncomms15864<http://dx.doi.org/10.1038/ncomms15864> Sirigu S, Hartman J, Planelles-Herrero VJ, Ropars V, Clancy S, Wang X, Chuang G, Qian X, Lu P-P, Barrett E, Rudolph K, Royer C, Morgan B, Stura EA, Malik FI, Houdusse A (2016 Nov 4) Highly selective inhibition of myosin motors provides the basis of potential therapeutic application. Proceedings of the National Academy of Sciences of the United States of America : 201609342 : DOI : 10.1073/pnas.1609342113<http://dx.doi.org/10.1073/pnas.1609342113> ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 This message was issued to members of www.jiscmail.ac.uk/CCP4BB, a mailing list hosted by www.jiscmail.ac.uk, terms & conditions are available at https://www.jiscmail.ac.uk/policyandsecurity/
