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        1. 您的位置:中國(guó)博士人才網(wǎng) > 博士后招收 > 海外博士后招收 > 美國(guó)俄勒岡大學(xué)招收細(xì)胞骨架調(diào)控的分子基礎(chǔ)方向博士后研究員

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          美國(guó)俄勒岡大學(xué)招收細(xì)胞骨架調(diào)控的分子基礎(chǔ)方向博士后研究員

          時(shí)間:2020-09-02來(lái)源:中國(guó)博士人才網(wǎng) 作者:佚名

          美國(guó)俄勒岡大學(xué)招收細(xì)胞骨架調(diào)控的分子基礎(chǔ)方向博士后研究員

          The Nolen laboratory at the University of Oregon (https://blogs.uoregon.edu/nolenlab/) seeks a highly motivated postdoctoral researcher to join our lab full time on a flexible start date. Our interest is in understanding the molecular basis for the regulation of the actin cytoskeleton. We apply a broad range of techniques to understand the structure-function relationships of actin regulatory proteins and how their molecular mechanisms dictate cellular function. Example of current projects include:

          1. Dissection of the mechanism and regulation of the WISH/DIP/SPIN90 (WDS) family proteins.

          Approaches used in this project include (but are not limited to) single molecule TIRF microscopy and ensemble methods to determine biochemical mechanism of WDS proteins, x-ray crystallography to determine high resolution structures of WDS family proteins bound to Arp2/3 complex, yeast genetics and live cell imaging combined with structure-function analyses to understand how WDS proteins function in assembly of branched actin networks during endocytosis, and biochemical reconstitution of branched actin network initiation and propagation.

          2. Mechanism of Arp2/3 complex regulation.

          Approaches used in this project include (but are not limited to) x-ray or electron microscopy to determine high-resolution structures of Arp2/3 complex with bound regulators, single molecule TIRF microscopy and ensemble methods to determine mechanisms of branching nucleation, development of new biochemical/biophysical/optogenetic tools to explore the conformational and kinetic pathway to branching nucleation, and structure-based mutational analysis to test biochemical mechanisms in vitro and in yeast.

          Successful candidates will have a Ph.D. in biochemistry, biophysics, structural or cellular biology or a related field, a published record of accomplishment, and good written and oral communication skills.

          Eugene, Oregon is an ideal place to work and live, and is an outdoor enthusiast’s paradise. In addition to a mild climate with access to the ocean and mountains, Eugene has affordable housing, bike-friendly streets, and a strong community feel. The University of Oregon is an Equal Opportunity/Affirmative Action Institution committed to cultural diversity and compliance with the Americans with Disabilities Act.

          For further information, please see:

          Luan Q., Liu S-L., Helgeson L.A., and Nolen B.J., Structure of the nucleation promoting factor

          SPIN90 bound to the actin filament nucleator Arp2/3 complex. (2018) EMBO J. 37(22).

          Rodnick-Smith, M., Luan, Q., Liu, S.-L., & Nolen, B. J. (2016). Role and structural mechanism of WASP-triggered conformational changes in branched actin filament nucleation by Arp2/3 complex. Proceedings of the National Academy of Sciences, 113(27), E3834–E3843. http://doi.org/10.1073/pnas.1517798113

          Balzer C.J., Wagner A.R., Helgeson L.A., and Nolen B.J. (2019) Single-Turnover Activation of Arp2/3 Complex by Dip1 May Balance Nucleation of Linear versus Branched Actin Filaments.Curr. Bio., pii: S0960-9822(19)31039-5

          Wagner, A. R., Luan, Q., Liu, S.-L., & Nolen, B. J. (2013). Dip1 Defines a Class of Arp2/3 Complex Activators that Function without Preformed Actin Filaments. Current Biology : CB, 23(20), 1990–8. doi:10.1016/j.cub.2013.08.029

          To apply, please upload a cover letter, curriculum vitae, and contact information for three references to http://careers.uoregon.edu/cw/en-us/job/524303/postdoctoral-scholar. The position will remain open until filled.

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