<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=""><div><div class=""><div class="" style="word-wrap:break-word; line-break:after-white-space"><p class="x_MsoNormal" style="margin-bottom:.1in; text-align:justify; text-autospace:none"><span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif"><b class="">Multiple </b>postdoctoral positions are available immediately for highly motivated individuals with
strong backgrounds in biophysics and an interest in <b class="">structural and chemical biology studies of ion channels</b> or
<b class="">mechanisms of</b> <b class="">toxin recognition and resistance</b> in the lab of Prof. Dan Minor at the University of California, San Francisco (UCSF). 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 poisonous organisms.<b class=""></b></span></p><p class="x_MsoHeader" style="margin-top:0in; margin-right:0in; margin-bottom:3.0pt; margin-left:.25in; text-indent:-.25in">
<span class="" style="font-size:15px"><b class=""><span class="" style="font-family:"Arial",sans-serif">1)<span class="" style="font-weight:normal; font-stretch:normal; line-height:normal; font-family:"Times New Roman"">
</span></span></b><b class=""><span class="" style="font-family:"Arial",sans-serif">Ion channel structure, function, and chemical biology</span></b></span></p><p class="x_MsoNormal" style="margin-bottom:3.0pt; text-align:justify; text-autospace:none">
<span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif">Projects focus on structural approaches to study ion channel function and development of chemical biology tools for a wide range of channel types. Candidates should have (or expect) an
Ph.D. or M.D. and should have demonstrated achievements with <u class="">X-ray crystallography, cryo‑electronmicroscopy, or electrophysiology</u>.<b class=""></b></span></p><p class="x_MsoNormal" style="margin-bottom:3.0pt; text-align:justify"><i class=""><span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif">Ongoing projects focus on mechanisms of voltage-gated, thermosensitive, and mechanosensitive channels
and efforts develop new agents to control and image ion channels involved in pain represented by:
</span></i></p><p class="x_MsoNormal" style="margin-top:0in; margin-right:0in; margin-bottom:3.0pt; margin-left:.25in; text-align:justify; line-height:12.0pt">
<span lang="IT" class="" style="font-size:11.0pt; font-family:"Arial",sans-serif; color:#333333; background:white">Lolicato, M., Natale, A., Abderemane-Ali, F., Crottès, D. Capponi, S., Duman, R., Wagner, A., Rosenberg, J.M., Grabe.
</span><span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif; color:#333333; background:white">M., and </span><strong class="" style="outline:0px; font-variant-ligatures:normal; orphans:2; widows:2"><span class="" style="font-family:"Arial",sans-serif; border:none windowtext 1.0pt; padding:0in; font-weight:normal">Minor,
D.L., Jr</span></strong><strong class=""><span class="" style="font-family:"Arial",sans-serif; border:none windowtext 1.0pt; padding:0in">.</span></strong><span class="" style="font-variant-ligatures:normal; orphans:2; widows:2"> ’</span><em class="" style="outline:0px; font-variant-ligatures:normal; orphans:2; widows:2"><span class="" style="font-family:"Arial",sans-serif; border:none windowtext 1.0pt; padding:0in">K<sub class="">2P</sub>2.1
channel C-type gating involves asymmetric selectivity filter order-disorder transitions</span></em><span class="" style="font-variant-ligatures:normal; orphans:2; widows:2">’ </span><em class="" style="outline:0px; font-variant-ligatures:normal; orphans:2; widows:2"><span class="" style="font-family:"Arial",sans-serif; border:none windowtext 1.0pt; padding:0in">Science
Advances</span></em><span class="" style="font-variant-ligatures:normal; orphans:2; widows:2"> </span><strong class="" style="outline:0px; font-variant-ligatures:normal; orphans:2; widows:2"><span class="" style="font-family:"Arial",sans-serif; border:none windowtext 1.0pt; padding:0in">6</span></strong><span class="" style="font-variant-ligatures:normal; orphans:2; widows:2"> eabc9174
(2020)</span><i class=""><span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif"></span></i></p><p class="x_MsoNormal" style="margin-top:0in; margin-right:0in; margin-bottom:3.0pt; margin-left:.25in; text-align:justify; line-height:12.0pt">
<span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif">Pope, L., Lolicato, M., Minor, D.L., Jr., ‘Polynuclear ruthenium amines inhibit K<sub class="">2P</sub> channels via a “Finger in the dam” mechanism’ <i class="">Cell Chemical Biology </i><b class="">27</b> 511-524
(2020) </span></p><p class="x_MsoNormal" style="margin-top:0in; margin-right:0in; margin-bottom:3.0pt; margin-left:.25in; text-align:justify; line-height:12.0pt">
<span lang="IT" class="" style="font-size:11.0pt; font-family:"Arial",sans-serif">Lolicato, M., Arrigoni, C., Mori, T., Sekioka, Y., Bryant, C., Clark, K.A., Minor, D.L., Jr.
</span><span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif">’<i class="">K<sub class="">2P</sub>2.1(TREK‑1):activator complexes reveal a cryptic selectivity filter binding site’ Nature </i><b class="">547<i class=""> </i></b>364-368 (2017<i class="">)</i></span></p>
<div class="" style="margin:0in 0in 0.1in 0.25in; text-align:justify; line-height:12pt">
<span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif">Arrigoni, C., Rohaim, A., Shaya, D., Findeisen ,F., Stein, R.A. Nurva, S.R., Mishra, S., Mchaourab, H.S., and </span><span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif">Minor,
D.L., Jr., ‘Unfolding of a temperature-sensitive domain controls voltage-gated channel activation’ <i class="">Cell</i> <b class="">164</b> 922-936 (2016) <b class=""></b></span></div><p class="x_MsoHeader" style="margin-top:0in; margin-right:0in; margin-bottom:3.0pt; margin-left:.25in; text-indent:-.25in">
<span class="" style="font-size:15px"><b class=""><span class="" style="font-family:"Arial",sans-serif">2)<span class="" style="font-weight:normal; font-stretch:normal; line-height:normal; font-family:"Times New Roman"">
</span></span></b></span><b class=""><span class="" style="font-family:"Arial",sans-serif"><span class="" style="font-size:15px">Mechanisms of toxin resistance in poison animals</span></span></b></p><p class="x_MsoNormal" style="margin-bottom:3.0pt; text-align:justify; text-autospace:none">
<span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif">This project focus on using protein engineering and molecular evolution methods to develop new classes of toxin binding 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, or selection methods and have a willingness to work with animals</u>.<b class=""></b></span></p><p class="x_MsoNormal" style="margin-bottom:3.0pt; text-align:justify; text-autospace:none">
<i class=""><span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif">Ongoing projects in this area are represented by:
</span></i><b class=""><span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif"></span></b></p><p class="x_MsoNormal" style="margin-top:0in; margin-right:0in; margin-bottom:3.0pt; margin-left:.25in; text-align:justify; line-height:12.0pt">
<span class="" style="font-size:11pt; font-family:Arial,sans-serif; background-color:white; background-position:initial initial; background-repeat:initial initial">Yen, T.-J., Lolicato, M., Thomas-Tran, R., Du Bois, J., and </span><strong class="" style="outline:0px; font-variant-ligatures:none; orphans:2; widows:2"><span class="" style="font-family:"Arial",sans-serif; border:none windowtext 1.0pt; padding:0in; font-weight:normal">Minor,
D.L., Jr.</span></strong><b class=""><span class="" style="font-variant-ligatures:none; orphans:2; widows:2">,</span></b> '<em class="" style="outline:0px; font-variant-ligatures:none; orphans:2; widows:2"><span class="" style="font-family:"Arial",sans-serif; border:none windowtext 1.0pt; padding:0in">Structure
of the Saxiphilin:saxitoxin (STX) complex reveals a convergent molecular recognition strategy for paralytic toxins</span></em><span class="" style="font-variant-ligatures:none; orphans:2; widows:2">' </span><em class="" style="outline:0px; font-variant-ligatures:none; orphans:2; widows:2"><span class="" style="font-family:"Arial",sans-serif; border:none windowtext 1.0pt; padding:0in">Science
Advances </span></em><strong class="" style="outline:0px; font-variant-ligatures:none; orphans:2; widows:2"><span class="" style="font-family:"Arial",sans-serif; border:none windowtext 1.0pt; padding:0in">5</span></strong><span class="" style="font-variant-ligatures:none; orphans:2; widows:2">,</span><strong class="" style="outline:0px; font-variant-ligatures:none; orphans:2; widows:2"><span class="" style="font-family:"Arial",sans-serif; border:none windowtext 1.0pt; padding:0in"> </span></strong><span class="" style="font-variant-ligatures:none; orphans:2; widows:2">eaax2650
(2019)</span><i class=""><span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif"></span></i></p><p class="x_MsoNormal" style="margin-top:0in; margin-right:0in; margin-bottom:3.0pt; margin-left:.25in; text-align:justify; line-height:12.0pt">
<span class="" style="font-size:11pt; font-family:Arial,sans-serif">Abderemane-Ali, F., Rossen, N.D., Kobiela, M.E., Craig, R.A.II, Garrison, C.E., Chen, Z., O'Connell, L.A., Du Bois, J., Dumbacher, J.P., and <span class="" style="border:none windowtext 1.0pt; padding:0in">Minor,
D.L., Jr.</span> '<i class=""><span class="" style="border:none windowtext 1.0pt; padding:0in">Evidence that toxin resistance in poison birds and frogs is not rooted in sodium channel mutations and relies on ‘toxin sponge’ proteins</span></i>', <i class=""><span class="" style="border:none windowtext 1.0pt; padding:0in">J.
Gen. Physiol </span></i><b class=""><span class="" style="border:none windowtext 1.0pt; padding:0in">153:</span></b>e202112872<b class=""><span class="" style="border:none windowtext 1.0pt; padding:0in"> </span></b>(2021) </span><i class=""><span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif"></span></i></p><p class="x_MsoNormal" style="margin-bottom:3.0pt; text-align:justify; line-height:12.0pt">
<span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif">More information is available at the lab website
</span><span class="" style="font-size:11.0pt"><a href="http://www.cvri.ucsf.edu/~dminor/" class=""><b class=""><span class="" style="font-family:"Arial",sans-serif">http://www.cvri.ucsf.edu/~dminor/</span></b></a></span><b class=""><span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif"></span></b></p><p class="x_MsoNormal" style="margin-bottom:3.0pt; text-align:justify; line-height:12.0pt; text-autospace:none">
<span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif">Fellows will benefit from both the outstanding lab environment and the highly collaborative UCSF community.<b class=""></b></span></p><p class="x_MsoNormal" style="margin-bottom:3.0pt; text-align:justify; line-height:12.0pt">
<b class=""><span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif">TO APPLY:</span></b></p><p class="x_MsoNormal" style="margin-bottom:.1in; text-align:justify; text-autospace:none">
<span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif">Interested individuals should send a current CV to Prof. Daniel Minor at </span><span class="" style="font-size:11.0pt"><span class="" style="font-family:"Arial",sans-serif; color:#386EFF"><a href="mailto:daniel.minor@ucsf.edu" class="">daniel.minor@ucsf.edu</a></span></span><span class="" style="font-size:11.0pt; font-family:"Arial",sans-serif"></span></p><p class="x_MsoNormal" style="margin-bottom:.1in; text-align:justify; text-autospace:none">
<span class="" style="font-size:11.0pt"><img apple-inline="yes" id="438E4EBE-94A3-4B59-91EA-D80AF08D459C" src="cid:4D512922-5233-4269-85CD-43F4A0459D83@ucsf.edu" class="">
</span></p><div style="margin-bottom: 0.1in; text-align: justify;" class=""><br class=""></div></div></div></div><br class=""><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>
</div>
<br class=""></body></html>