<html><head><meta http-equiv="Content-Type" content="text/html; charset=utf-8"></head><body style="word-wrap: break-word; -webkit-nbsp-mode: space; line-break: after-white-space;" class=""><p class="MsoHeader" style="line-height: 14pt;"><img apple-inline="yes" id="D6730253-CBB8-4AC8-9AC1-E983D6918A84" class="" src="cid:EBCBD178-83EE-44FA-BAFD-F31D3BA2C48B@ucsf.edu"></p><p class="MsoHeader" style="line-height: 14pt;"><b class=""><span class="" style="font-size: 14pt; font-family: Arial, sans-serif;"><br class=""></span></b></p><p class="MsoHeader" style="line-height: 14pt;"><b class=""><span class="" style="font-size: 14pt; font-family: Arial, sans-serif;">Postdoctoral Positions in:<o:p class=""></o:p></span></b></p><p class="MsoHeader" style="margin-left: 0.5in; text-indent: -0.25in; line-height: 14pt;"><b class=""><span class="" style="font-size: 14pt; font-family: Arial, sans-serif;">1)<span class="" style="font-weight: normal; font-stretch: normal; font-size: 7pt; line-height: normal; font-family: "Times New Roman";"> </span></span></b><b class=""><span class="" style="font-size: 14pt; font-family: Arial, sans-serif;">Structural biology of ion channel assembly mechanisms<o:p class=""></o:p></span></b></p><p class="MsoHeader" style="margin: 0in 0in 6pt 0.5in; text-indent: -0.25in; line-height: 14pt;"><b class=""><span class="" style="font-size: 14pt; font-family: Arial, sans-serif;">2)<span class="" style="font-weight: normal; font-stretch: normal; font-size: 7pt; line-height: normal; font-family: "Times New Roman";"> </span></span></b><b class=""><span class="" style="font-size: 14pt; font-family: Arial, sans-serif;">Structural studies and protein design of toxin sponge proteins<o:p class=""></o:p></span></b></p><p class="MsoNormal" style="margin-bottom: 6pt; text-align: justify;"><b class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">MINOR LAB </span></b><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">UCSF - Cardiovascular Research Institute<o:p class=""></o:p></span></p><p class="MsoNormal" style="margin-bottom: 6pt; text-align: justify;"><b class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">Multiple</span></b><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;"> postdoctoral positions are available immediately for highly motivated individuals with strong backgrounds in biophysics, biochemistry, structural biology, or computational methods, and an interest in <b class="">structural biology of ion channel assembly mechanisms </b>or <b class="">structural studies and protein design of toxin sponge proteins</b> in the lab of <b class="">Prof. Dan Minor</b> at the <b class="">University of California, San Francisco</b> (<b class="">UCSF</b>). The Minor Lab merges structural, biochemical, chemical biology, genetic, and electrophysiological methods to dissect mechanisms of complex protein machines involved in electrical signaling and to uncover mechanisms of toxin resistance in poison organisms.<b class=""><o:p class=""></o:p></b></span></p><p class="MsoHeader" style="margin: 0in 0in 3pt 0.25in; text-indent: -0.25in;"><b class=""><span class="" style="font-family: Arial, sans-serif;">1)<span class="" style="font-weight: normal; font-stretch: normal; font-size: 7pt; line-height: normal; font-family: "Times New Roman";"> </span></span></b><b class=""><span class="" style="font-family: Arial, sans-serif;">Structural biology of ion channel assembly<o:p class=""></o:p></span></b></p><p class="MsoNormal" style="margin-bottom: 3pt; text-align: justify;"><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">Projects focus on cryo-EM and other approaches to study the structural principles of ion channel assembly and interactions with chaperones. Candidates should have (or expect) an Ph.D. or M.D. and should have demonstrated achievements in<u class=""> protein biochemistry or biophysics, X-ray crystallography, cryo‑electronmicroscopy, or electrophysiology</u>. Computational skills are also highly desired.<b class=""><o:p class=""></o:p></b></span></p><p class="MsoNormal" style="margin-bottom: 3pt; text-align: justify;"><i class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">Ongoing work is represented by: <o:p class=""></o:p></span></i></p><p class="MsoNormal" style="margin: 0in 0in 2pt 13.5pt; text-align: justify; line-height: 12pt;"><span class="" style="font-size: 11pt; font-family: Arial, sans-serif; color: rgb(51, 51, 51); background-color: white; background-position: initial initial; background-repeat: initial initial;">Arrigoni, C., Lolicato, M., Shaya, D., Rohaim, A., Findeisen, F., Fong, L.-K., Colleran, C.M., Dominik, P., Kim, S.S., Schuermann, J., DeGrado, W.F., Grabe, M., Kossiakoff, A.A., and <strong class=""><span class="" style="border: 1pt none windowtext; padding: 0in;">Minor, D.L., Jr.</span></strong></span><o:p class=""></o:p></p><p class="MsoNormal" style="margin-left: 13.5pt; text-align: justify; line-height: 12pt;"><span class="" style="font-size: 11pt; font-family: Arial, sans-serif; color: rgb(51, 51, 51); background-color: white; background-position: initial initial; background-repeat: initial initial;">'<em class=""><span class="" style="border: 1pt none windowtext; padding: 0in;">Quaternary structure independent folding of voltage-gated ion channel pore domain subunits'</span></em> <o:p class=""></o:p></span></p><p class="MsoNormal" style="margin: 0in 0in 6pt 13.5pt; text-align: justify; line-height: 12pt;"><em class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif; color: rgb(51, 51, 51); border: 1pt none windowtext; padding: 0in; background-color: white; background-position: initial initial; background-repeat: initial initial;">Nature Structural and Molecular Biology</span></em><span class="" style="font-size: 11pt; font-family: Arial, sans-serif; color: rgb(51, 51, 51); background-color: white; background-position: initial initial; background-repeat: initial initial;"> <strong class=""><span class="" style="border: 1pt none windowtext; padding: 0in;">29</span></strong> 537-548 (2022) </span><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;"><a href="https://www.nature.com/articles/s41594-022-00775-x" class=""><span class="" style="background-color: white; background-position: initial initial; background-repeat: initial initial;">https://wsww.nature.com/articles/s41594-022-00775-x</span></a><span class="" style="color: rgb(51, 51, 51); background-color: white; background-position: initial initial; background-repeat: initial initial;"> <strong class=""><o:p class=""></o:p></strong></span></span></p><p class="MsoNormal" style="margin: 0in 0in 2pt 13.5pt; text-align: justify; line-height: 12pt;"><span lang="IT" class="" style="font-size: 11pt; font-family: Arial, sans-serif;">Chen, Z., Mondal, A., Abderemane-Ali, F., Montano, J., Zaro, B., and Minor, D.L., Jr.,</span><b class=""><span lang="IT" class="" style="font-size: 11pt; font-family: Arial, sans-serif; color: rgb(51, 51, 51); background-color: white; background-position: initial initial; background-repeat: initial initial;"><o:p class=""></o:p></span></b></p><p class="MsoNormal" style="margin: 0in 0in 6pt 13.5pt; text-align: justify; line-height: 12pt;"><i class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">’EMC holdase:Ca<sub class="">V</sub>1.2/Ca<sub class="">V</sub>β<sub class="">3</sub> complex and Ca<sub class="">V</sub>1.2 channel structures reveal Ca<sub class="">V</sub> assembly and drug binding mechanisms</span></i><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">’ </span><b class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">bioRxiv</span></b><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;"> </span><a href="https://www.biorxiv.org/content/10.1101/2022.10.03.510667v1" class=""><i class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">https://www.biorxiv.org/content/10.1101/2022.10.03.510667v1</span></i></a><i class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;"><o:p class=""></o:p></span></i></p><p class="MsoHeader" style="margin: 0in 0in 3pt 0.25in; text-indent: -0.25in;"><b class=""><span class="" style="font-family: Arial, sans-serif;">2)<span class="" style="font-weight: normal; font-stretch: normal; font-size: 7pt; line-height: normal; font-family: "Times New Roman";"> </span></span></b><b class=""><span class="" style="font-family: Arial, sans-serif;">Structural studies and protein design of toxin sponge proteins<o:p class=""></o:p></span></b></p><p class="MsoNormal" style="margin-bottom: 3pt; text-align: justify;"><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">This project focuses on using structural biology, protein engineering, computational design, and molecular evolution to characterize and develop new toxin sponge proteins. Candidates should have (or expect) an Ph.D. or M.D. and should have demonstrated achievements in <u class="">protein structure analysis, protein biophysics, computational methods, or selection methods</u>. Computational skills are highly desired.<b class=""><o:p class=""></o:p></b></span></p><p class="MsoNormal" style="margin-bottom: 3pt; text-align: justify;"><i class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">Ongoing work is represented by: </span></i><b class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;"><o:p class=""></o:p></span></b></p><p class="MsoNormal" style="margin-left: 13.5pt; text-align: justify; line-height: 12pt;"><span class="" style="font-size: 11pt; font-family: Arial, sans-serif; background-color: white;">Yen, T.-J., Lolicato, M., Thomas-Tran, R., Du Bois, J., and <strong class=""><span class="" style="border: 1pt none windowtext; padding: 0in;">Minor, D.L., Jr.</span></strong>, </span><b class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif; color: rgb(51, 51, 51); background-color: white; background-position: initial initial; background-repeat: initial initial;"><o:p class=""></o:p></span></b></p><div class="" style="margin: 0in 0in 0.1in 13.5pt; text-align: justify; line-height: 12pt;"><span class="" style="font-size: 11pt; font-family: Arial, sans-serif; background-color: white;">'<em class=""><span class="" style="border: 1pt none windowtext; padding: 0in;">Structure of the Saxiphilin:saxitoxin (STX) complex reveals a convergent molecular recognition strategy for paralytic toxins</span></em>' <em class=""><span class="" style="border: 1pt none windowtext; padding: 0in;">Science Advances </span></em><strong class=""><span class="" style="border: 1pt none windowtext; padding: 0in;">5</span></strong>,<strong class=""><span class="" style="border: 1pt none windowtext; padding: 0in;"> </span></strong>eaax2650 (2019)</span> <a href="https://www.science.org/doi/10.1126/sciadv.aax2650" class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif; background-color: white; background-position: initial initial; background-repeat: initial initial;">aax2650</span></a><strong class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif; color: rgb(51, 51, 51); background-color: white; background-position: initial initial; background-repeat: initial initial;"><o:p class=""></o:p></span></strong></div><p class="MsoNormal" style="margin: 0in 0in 3pt 13.5pt; text-align: justify; line-height: 12pt;"><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">Chen, Z., Zakrzewska, S., Hajare, H., Alvarez-Bullya, A., Abderemane-Ali, F., Bogan, M., Ramirez, D., O’Connell, L.A., Du Bois, J., and<b class=""> </b>Minor, D.L., Jr.</span><b class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif; color: rgb(51, 51, 51); background-color: white; background-position: initial initial; background-repeat: initial initial;"><o:p class=""></o:p></span></b></p><p class="MsoNormal" style="margin: 0in 0in 3pt 13.5pt; text-align: justify; line-height: 12pt;"><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">'<i class="">Definition of a saxitoxin (STX) binding code enables discovery and characterization of the Anuran saxiphilin family</i>’ <i class="">Proceedings of the National Academy of Sciences, USA (in press) </i>and <b class="">bioRxiv</b> </span><a href="https://www.biorxiv.org/content/10.1101/2022.06.09.495489v1" class=""><i class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">https://www.biorxiv.org/content/10.1101/2022.06.09.495489v1</span></i></a><i class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;"><o:p class=""></o:p></span></i></p><p class="MsoNormal" style="margin-bottom: 3pt; text-align: justify; line-height: 12pt;"><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">More information is available at the lab website </span><a href="http://www.cvri.ucsf.edu/~dminor/" class=""><b class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">http://www.cvri.ucsf.edu/~dminor/</span></b></a><b class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;"><o:p class=""></o:p></span></b></p><p class="MsoNormal" style="margin-bottom: 3pt; text-align: justify; line-height: 12pt;"><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">Fellows will benefit from both the outstanding lab environment and the highly collaborative UCSF community.<b class=""><o:p class=""></o:p></b></span></p><p class="MsoNormal" style="margin-bottom: 3pt; text-align: justify; line-height: 12pt;"><b class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">TO APPLY: </span></b><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;">Interested individuals should send a current CV to Prof. Daniel Minor at </span><a href="mailto:daniel.minor@ucsf.edu" class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif; color: rgb(56, 110, 255);">daniel.minor@ucsf.edu</span></a><u class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif; color: rgb(56, 110, 255);"><o:p class=""></o:p></span></u></p><p class="MsoNormal" style="margin-bottom: 0.1in; text-align: justify;"><b class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif; color: rgb(56, 110, 255);"><img border="0" v:shapes="Picture_x0020_2" apple-inline="yes" id="A9B40AFF-84B1-418F-A1C9-7A394D778E49" class="" width="22" height="16" src="cid:clip_image001.png"></span></b><b class=""><span class="" style="font-size: 11pt; font-family: Arial, sans-serif;"> @ElectrosomeUCSF<o:p class=""></o:p></span></b></p><div class=""><br class=""></div><div class=""><div class="" style="word-wrap: break-word; -webkit-nbsp-mode: space; line-break: after-white-space;">Dan Minor, Ph.D.<br class="">Professor<br class="">Cardiovascular Research Institute<br class="">Departments of Biochemistry & Biophysics,<br class="">and Cellular & Molecular Pharmacology<br class="">California Institute for Quantitative Biomedical Research<br class="">Kavli Institute for Fundamental Neuroscience<br class="">University of California, San Francisco<br class=""><br class=""><br class="">FEDEX/UPS address:<br class=""><br class="">Cardiovascular Research Institute<br class="">Box 3122<br class="">University of California San Francisco<br class="">555 Mission Bay Blvd. South. Rm 452Z<br class="">San Francisco, CA 94158-9001<br class=""><br class=""><a href="mailto:daniel.minor@ucsf.edu" class="">Email: daniel.minor@ucsf.edu</a><br class="">Phone: 415-514-2551<br class="">Fax: 415-476-8173<br class="">Web: <a href="http://www.cvri.ucsf.edu/~dminor" class="">http://www.cvri.ucsf.edu/~dminor</a></div><div class="" style="word-wrap: break-word; -webkit-nbsp-mode: space; line-break: after-white-space;">Twitter:<a href="http://twitter.com/ElectrosomeUCSF" class="">http://twitter.com/ElectrosomeUCSF</a></div></div><div class="">
<div style="color: rgb(0, 0, 0); letter-spacing: normal; text-align: start; text-indent: 0px; text-transform: none; white-space: normal; word-spacing: 0px; -webkit-text-stroke-width: 0px; word-wrap: break-word; -webkit-nbsp-mode: space; line-break: after-white-space;" class="">Dan Minor, Ph.D.<br class="">Professor<br class="">Cardiovascular Research Institute<br class="">Departments of Biochemistry & Biophysics,<br class="">and Cellular & Molecular Pharmacology<br class="">California Institute for Quantitative Biomedical Research<br class="">Kavli Institute for Fundamental Neuroscience<br class="">University of California, San Francisco<br class=""><br class=""><br class="">FEDEX/UPS address:<br class=""><br class="">Cardiovascular Research Institute<br class="">Box 3122<br class="">University of California San Francisco<br class="">555 Mission Bay Blvd. South. Rm 452Z<br class="">San Francisco, CA 94158-9001<br class=""><br class=""><a href="mailto:daniel.minor@ucsf.edu" class="">Email: daniel.minor@ucsf.edu</a><br class="">Phone: 415-514-2551<br class="">Fax: 415-476-8173<br class="">Web: http://www.cvri.ucsf.edu/~dminor</div><div style="color: rgb(0, 0, 0); letter-spacing: normal; text-align: start; text-indent: 0px; text-transform: none; white-space: normal; word-spacing: 0px; -webkit-text-stroke-width: 0px; word-wrap: break-word; -webkit-nbsp-mode: space; line-break: after-white-space;" class="">Twitter:<a href="http://twitter.com/ElectrosomeUCSF" class="">http://twitter.com/ElectrosomeUCSF</a><br class=""><br class=""><br class=""></div>
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