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Dear all,
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<p style="margin: 0px 0px 8px; font-stretch: normal; line-height: normal;" class="">
<span style="font-kerning: none;" class="">We are looking for a post-doctoral fellow for a 2.5-year project (possible extension for up to 1 year) in my group at the Faculty of Biochemistry and Molecular Medicine (FBMM), University of Oulu, Finland. Alternatively,
an exceptionally highly-qualified PhD student could be considered. The overall aim of my group is to understand the molecular mechanism of malaria parasite gliding motility. To reach this goal, we use a wide variety of structural biology and biochemical/biophysical
methods. Our ongoing work is focused on (i) the polymerization and ATPase mechanism of actin, (ii) parasite actomyosin complexes, (iii) the structure and function of the glideosome-associated linker protein, and (iv) reconstructing the entire membrane-delimited
motor complex <i class="">in vitro</i> for structural and functional studies. The exact project will be agreed upon based on the experience and interests of the successful candidate.</span></p>
<p style="margin: 0px 0px 8px; font-stretch: normal; line-height: normal;" class="">
<span style="font-kerning: none;" class="">The candidate should have a PhD (or MSc if applying for a graduate student position) in a relevant field of science and have experience, or at least a keen interest, in all or several of the following:</span></p>
<p style="margin: 0px 0px 8px; font-stretch: normal; line-height: normal;" class="">
<span style="font-kerning: none;" class="">- molecular biology and protein expression and purification</span></p>
<p style="margin: 0px 0px 8px; font-stretch: normal; line-height: normal;" class="">
<span style="font-kerning: none;" class="">- biophysical and biochemical characterization of proteins and their complexes</span></p>
<p style="margin: 0px 0px 8px; font-stretch: normal; line-height: normal;" class="">
<span style="font-kerning: none;" class="">- protein crystallography and/or cryo-EM</span></p>
<p style="margin: 0px 0px 8px; font-stretch: normal; line-height: normal;" class="">
<span style="font-kerning: none;" class="">- light and/or electron microscopy</span></p>
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<span style="font-kerning: none;" class="">We welcome applications particularly from candidates willing and eligible to apply for competitive funding from national, European, and international sources.</span></p>
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<span style="font-kerning: none;" class="">Our research group is split between the FBMM in Oulu and the Department of Biomedicine, University of Bergen, Norway. Our laboratories and the available core facilities available have state-of-the-art equipment for
molecular biology, protein biochemistry/biophysics, and electron and light microscopy. We have active collaborations for cryo-EM and cell biology/parasitology.</span></p>
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<span style="font-kerning: none;" class="">The project is funded by the Sigrid Jusélius foundation, and the candidate will receive a personal stipend (tax-exempt up to the limit defined by the Finnish tax authorities and subject to a compulsory pension insurance).</span></p>
<p style="margin: 0px 0px 8px; font-stretch: normal; line-height: normal;" class="">
<span style="font-kerning: none;" class="">Informal inquiries and applications including a motivation letter, a CV with publication list, and contact information for 2-3 referees are to be sent to <a href="mailto:inari.kursula@oulu.fi" class=""><span style="font-kerning: none;" class="">inari.kursula@oulu.fi</span></a>.
Applications will be considered until a suitable candidate has been identified. The starting date is as soon as possible.</span></p>
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<span style="font-kerning: none;" class="">Publications most relevant for the project:</span></p>
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<span style="font-kerning: none;" class="">Pires I, Hung YF, Bergmann U, Molloy JE & Kursula I (2022) Analysis of <i class="">Plasmodium falciparum</i> myosin B ATPase activity and structure in complex with the calmodulin-like domain of its light chain MLC-B. <b class=""><i class="">J
Biol Chem </i></b>in press, <a href="https://urldefense.com/v3/__https://doi.org/10.1016/j.jbc.2022.102634__;!!Mih3wA!Fbd0sTrwUjzxaZaM-7y81Jm4b6fAcLeYcMtONcSvqzuDIyUkUjotXL5k6GkQg9JzVwsAGOB2bX0ClV7qyjWNf_k72w$" class=""><span style="font-kerning: none;" class="">https://doi.org/10.1016/j.jbc.2022.102634</span></a></span></p>
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<span style="font-kerning: none;" class="">Vahokoski J, Calder L, Lopez AJ, Molloy JE, Kursula I & Rosenthal PB (2022) High-resolution structures of malaria parasite actomyosin and actin filaments. <b class=""><i class="">PLoS Pathog</i></b> 18: e1010408.</span></p>
<p style="margin: 0px 0px 8px; font-stretch: normal; line-height: normal;" class="">
<span style="font-kerning: none;" class="">Kumpula EP, Lopez AJ, Tajedin L, Han H & Kursula I (2020) Atomic view into <i class="">Plasmodium</i> actin polymerization, ATP hydrolysis, and fragmentation.<b class=""><i class=""> PLoS Biol </i></b>17: e3000315.</span></p>
<p style="margin: 0px 0px 8px; font-stretch: normal; line-height: normal;" class="">
<span style="font-kerning: none;" class="">Kumpula EP, Pires IP, Lasiwa D, Piirainen H, Bergmann U, Vahokoski J & Kursula I (2017) Apicomplexan actin polymerization depends on nucleation. <b class=""><i class="">Sci Rep</i></b> 7: 12137.</span></p>
<p style="margin: 0px 0px 8px; font-stretch: normal; line-height: normal;" class="">
<span style="font-kerning: none;" class="">Pospich S, Kumpula EP, von der Ecken J, Vahokoski J, Kursula I & Raunser S (2017) Near-atomic structure of jasplakinolide-stabilized malaria parasite F-actin reveals the structural basis of filament instability. <b class=""><i class="">Proc
Natl Acad Sci USA</i></b> 114: 10636-10641.</span></p>
<p style="margin: 0px 0px 8px; font-stretch: normal; line-height: normal;" class="">
<span style="font-kerning: none;" class="">Jacot D, Tosetti N, Pires IP, Stock J, Graindorge A, Hung YF, Han H, Tewari R, Kursula I & Soldati-Favre D (2016) An apicomplexan actin-binding protein serves as a connector and lipid sensor to coordinate motility
and invasion. <b class=""><i class="">Cell Host Microbe</i></b> 20: 731-743.</span></p>
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<span style="font-kerning: none;" class=""><b class="">More info:</b></span></p>
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<span style="font-kerning: none;" class="">Group webpages in <span style="font-kerning: none;" class=""><a href="https://urldefense.com/v3/__https://www.oulu.fi/en/research-groups/molecular-mechanisms-parasite-motility__;!!Mih3wA!Fbd0sTrwUjzxaZaM-7y81Jm4b6fAcLeYcMtONcSvqzuDIyUkUjotXL5k6GkQg9JzVwsAGOB2bX0ClV7qyjXw1VW7pg$" class="">Oulu</a>: <a href="https://urldefense.com/v3/__https://www.oulu.fi/en/research-groups/molecular-mechanisms-parasite-motility__;!!Mih3wA!Fbd0sTrwUjzxaZaM-7y81Jm4b6fAcLeYcMtONcSvqzuDIyUkUjotXL5k6GkQg9JzVwsAGOB2bX0ClV7qyjXw1VW7pg$" class="">https://www.oulu.fi/en/research-groups/molecular-mechanisms-parasite-motility</a></span> and <span style="font-kerning: none;" class=""><a href="https://urldefense.com/v3/__https://www.uib.no/en/rg/inari__;!!Mih3wA!Fbd0sTrwUjzxaZaM-7y81Jm4b6fAcLeYcMtONcSvqzuDIyUkUjotXL5k6GkQg9JzVwsAGOB2bX0ClV7qyjX7Xg3gvw$" class="">Bergen</a>: <a href="https://urldefense.com/v3/__https://www.uib.no/en/rg/inari__;!!Mih3wA!Fbd0sTrwUjzxaZaM-7y81Jm4b6fAcLeYcMtONcSvqzuDIyUkUjotXL5k6GkQg9JzVwsAGOB2bX0ClV7qyjX7Xg3gvw$" class="">https://www.uib.no/en/rg/inari</a></span></span></p>
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<span style="text-decoration: underline; font-kerning: none;" class=""><a href="https://urldefense.com/v3/__https://www.uib.no/en/rg/inari/149298/our-publications__;!!Mih3wA!Fbd0sTrwUjzxaZaM-7y81Jm4b6fAcLeYcMtONcSvqzuDIyUkUjotXL5k6GkQg9JzVwsAGOB2bX0ClV7qyjWWebSTqQ$" class="">Selected publications</a>: <a href="https://urldefense.com/v3/__https://www.uib.no/en/rg/inari/149298/our-publications__;!!Mih3wA!Fbd0sTrwUjzxaZaM-7y81Jm4b6fAcLeYcMtONcSvqzuDIyUkUjotXL5k6GkQg9JzVwsAGOB2bX0ClV7qyjWWebSTqQ$" class="">https://www.uib.no/en/rg/inari/149298/our-publications</a></span></p>
<p style="margin: 0px 0px 8px; font-stretch: normal; line-height: normal;" class="">
<span style="text-decoration: underline; font-kerning: none;" class=""><a href="https://urldefense.com/v3/__https://www.oulu.fi/en/university/faculties-and-units/faculty-biochemistry-and-molecular-medicine__;!!Mih3wA!Fbd0sTrwUjzxaZaM-7y81Jm4b6fAcLeYcMtONcSvqzuDIyUkUjotXL5k6GkQg9JzVwsAGOB2bX0ClV7qyjWH2Oondw$" class="">FBMM Oulu</a>: <a href="https://urldefense.com/v3/__https://www.oulu.fi/en/university/faculties-and-units/faculty-biochemistry-and-molecular-medicine__;!!Mih3wA!Fbd0sTrwUjzxaZaM-7y81Jm4b6fAcLeYcMtONcSvqzuDIyUkUjotXL5k6GkQg9JzVwsAGOB2bX0ClV7qyjWH2Oondw$" class="">https://www.oulu.fi/en/university/faculties-and-units/faculty-biochemistry-and-molecular-medicine</a></span></p>
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<div class="">Kind regards,</div>
<div class="">Inari </div>
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Prof. Inari Kursula<br class="">
<br class="">
Department of Biomedicine<br class="">
University of Bergen<br class="">
Jonas Lies vei 91<br class="">
5009 Bergen<br class="">
Norway<br class="">
<br class="">
Faculty of Biochemistry and Molecular Medicine<br class="">
University of Oulu<br class="">
Aapistie 7<br class="">
90220 Oulu<br class="">
Finland<br class="">
<br class="">
<a href="https://urldefense.com/v3/__https://www.uib.no/rg/inari__;!!Mih3wA!Fbd0sTrwUjzxaZaM-7y81Jm4b6fAcLeYcMtONcSvqzuDIyUkUjotXL5k6GkQg9JzVwsAGOB2bX0ClV7qyjU8oCFafw$" class="">https://www.uib.no/rg/inari</a><br class="">
<a href="https://urldefense.com/v3/__https://www.oulu.fi/en/research-groups/molecular-mechanisms-parasite-motility__;!!Mih3wA!Fbd0sTrwUjzxaZaM-7y81Jm4b6fAcLeYcMtONcSvqzuDIyUkUjotXL5k6GkQg9JzVwsAGOB2bX0ClV7qyjXw1VW7pg$">https://www.oulu.fi/en/research-groups/molecular-mechanisms-parasite-motility</a><br class="">
inari.kursula@uib.no, inari.kursula@oulu.fi<br class="">
<br class="">
Office in Bergen: https://link.mazemap.com/OtQ8q8bm<br class="">
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