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<!--StartFragment--><p class="MsoHeader" style="line-height:14.0pt;mso-line-height-rule:exactly;
tab-stops:3.0in"><b style="text-align: justify;" class=""><span style="font-size:11.0pt;
font-family:"Arial",sans-serif" class="">MINOR LAB </span></b><span style="text-align: justify; font-size: 11pt; font-family: Arial, sans-serif;" class="">UCSF - Cardiovascular Research Institute</span></p><p class="MsoNormal" style="margin-bottom:.1in;mso-para-margin-bottom:.6gd;
text-align:justify;mso-pagination:none;mso-layout-grid-align:none;text-autospace:
none"><b class=""><span style="font-size:11.0pt;font-family:"Arial",sans-serif" class="">Multiple</span></b><span style="font-size:11.0pt;font-family:"Arial",sans-serif" class=""> 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 poison organisms.<b class=""><o:p class=""></o:p></b></span></p><p class="MsoHeader" style="margin-top:0in;margin-right:0in;margin-bottom:3.0pt;
margin-left:.25in;text-indent:-.25in;mso-list:l0 level1 lfo2;tab-stops:3.0in"><!--[if !supportLists]--><b class=""><span style="font-family:"Arial",sans-serif;
mso-fareast-font-family:Arial" class="">1)<span style="font-weight: normal; font-stretch: normal; font-size: 7pt; line-height: normal; font-family: "Times New Roman";" class=""> </span></span></b><!--[endif]--><b class=""><span style="font-family:"Arial",sans-serif" class="">Ion
channel structure, function, and chemical biology<o:p class=""></o:p></span></b></p><p class="MsoNormal" style="margin-bottom:3.0pt;text-align:justify;mso-pagination:
none;mso-layout-grid-align:none;text-autospace:none"><span style="font-size:
11.0pt;font-family:"Arial",sans-serif" class="">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=""><o:p class=""></o:p></b></span></p><p class="MsoNormal" style="margin-bottom:6.0pt;text-align:justify"><i class=""><span style="font-size:11.0pt;font-family:
"Arial",sans-serif" class="">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: <o:p class=""></o:p></span></i></p><p class="MsoNormal" style="margin-top:0in;margin-right:0in;margin-bottom:3.0pt;
margin-left:.25in;text-align:justify;line-height:12.0pt;mso-line-height-rule:
exactly"><span style="font-size:11.0pt;font-family:"Arial",sans-serif;
color:#333333;background:white" class="">Arrigoni, C, Lolicato, M., <i class="">et a</i>l.
, ‘Quaternary structure independent folding of voltage-gated ion channel
pore domain subunits’ <i class="">Nature Structural and Molecular Biology <b class=""> </b></i><b class="">2022
Jun 2. doi: 10.1038/s41594-022-00775-x. Online ahead of print.</b><o:p class=""></o:p></span></p><p class="MsoNormal" style="margin-top:0in;margin-right:0in;margin-bottom:3.0pt;
margin-left:.25in;text-align:justify;line-height:12.0pt;mso-line-height-rule:
exactly"><span lang="IT" style="font-size:11.0pt;font-family:"Arial",sans-serif;
color:#333333;background:white;mso-ansi-language:IT" class="">Lolicato, M., Natale, A.,
Abderemane-Ali, F., Crottès, D. Capponi, S., Duman, R., Wagner, A., Rosenberg,
J.M., Grabe. </span><span style="font-size:11.0pt;font-family:"Arial",sans-serif;
color:#333333;background:white" class="">M., and <strong class=""><span style="border: 1pt none windowtext; padding: 0in;" class="">Minor, D.L., Jr.</span></strong> ’<em class=""><span style="border: 1pt none windowtext; padding: 0in;" class="">K<sub class="">2P</sub>2.1 channel C-type gating involves asymmetric
selectivity filter order-disorder transitions</span></em>’ <em class=""><span style="border: 1pt none windowtext; padding: 0in;" class="">Science Advances</span></em> <strong class=""><span style="border: 1pt none windowtext; padding: 0in;" class="">6</span></strong> eabc9174 (2020)</span><i class=""><span style="font-size:11.0pt;font-family:
"Arial",sans-serif;mso-bidi-language:EN-US" class=""><o:p class=""></o:p></span></i></p><p class="MsoNormal" style="margin-top:0in;margin-right:0in;margin-bottom:3.0pt;
margin-left:.25in;text-align:justify;line-height:12.0pt;mso-line-height-rule:
exactly"><span lang="IT" style="font-size:11.0pt;font-family:"Arial",sans-serif;
mso-ansi-language:IT;mso-bidi-language:EN-US" class="">Lolicato, M., Arrigoni, C., Mori,
T., Sekioka, Y., Bryant, C., Clark, K.A., Minor, D.L., Jr. </span><span style="font-size:11.0pt;font-family:"Arial",sans-serif;mso-bidi-language:EN-US" class="">’<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="">)<o:p class=""></o:p></i></span></p><div style="margin: 0in 0in 0.1in 0.25in; text-align: justify; line-height: 12pt;" class=""><span style="font-size:11.0pt;font-family:"Arial",sans-serif;
mso-bidi-language:EN-US;mso-bidi-font-weight:bold" class="">Arrigoni, C., Rohaim, A.,
Shaya, D., Findeisen ,F., Stein, R.A. Nurva, S.R., Mishra, S., Mchaourab, H.S.,
and </span><span style="font-size:11.0pt;font-family:"Arial",sans-serif;
mso-bidi-language:EN-US" class="">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=""><o:p class=""></o:p></b></span></div><p class="MsoHeader" style="margin-top:0in;margin-right:0in;margin-bottom:3.0pt;
margin-left:.25in;text-indent:-.25in;mso-list:l0 level1 lfo2;tab-stops:3.0in"><!--[if !supportLists]--><b class=""><span style="font-family:"Arial",sans-serif;
mso-fareast-font-family:Arial" class="">2)<span style="font-weight: normal; font-stretch: normal; font-size: 7pt; line-height: normal; font-family: "Times New Roman";" class=""> </span></span></b><!--[endif]--><b class=""><span style="font-family:"Arial",sans-serif" class="">Mechanisms
of toxin resistance in poison animals<o:p class=""></o:p></span></b></p><p class="MsoNormal" style="margin-bottom:3.0pt;text-align:justify;mso-pagination:
none;mso-layout-grid-align:none;text-autospace:none"><span style="font-size:
11.0pt;font-family:"Arial",sans-serif" class="">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</u>.<b class=""><o:p class=""></o:p></b></span></p><p class="MsoNormal" style="margin-bottom:3.0pt;text-align:justify;mso-pagination:
none;mso-layout-grid-align:none;text-autospace:none"><i class=""><span style="font-size:11.0pt;font-family:"Arial",sans-serif" class="">Ongoing
projects in this area are represented by: </span></i><b class=""><span style="font-size:11.0pt;font-family:"Arial",sans-serif" class=""><o:p class=""></o:p></span></b></p><p class="MsoNormal" style="margin-top:0in;margin-right:0in;margin-bottom:3.0pt;
margin-left:.25in;text-align:justify;line-height:12.0pt;mso-line-height-rule:
exactly"><span style="font-size: 11pt; font-family: Arial, sans-serif; background-color: white; background-position: initial initial; background-repeat: initial initial;" class="">Yen, T.-J., Lolicato, M., Thomas-Tran, R., Du
Bois, J., and <strong class=""><span style="border: 1pt none windowtext; padding: 0in;" class="">Minor,
D.L., Jr.</span></strong><b class="">,</b> '<em class=""><span style="border: 1pt none windowtext; padding: 0in;" class="">Structure
of the Saxiphilin:saxitoxin (STX) complex reveals a convergent molecular
recognition strategy for paralytic toxins</span></em>' <em class=""><span style="border: 1pt none windowtext; padding: 0in;" class="">Science Advances </span></em><strong class=""><span style="border: 1pt none windowtext; padding: 0in;" class="">5</span></strong>,<strong class=""><span style="border: 1pt none windowtext; padding: 0in;" class=""> </span></strong>eaax2650 (2019)</span><i class=""><span style="font-size:11.0pt;font-family:
"Arial",sans-serif;mso-bidi-language:EN-US" class=""><o:p class=""></o:p></span></i></p><p class="MsoNormal" style="margin-top:0in;margin-right:0in;margin-bottom:3.0pt;
margin-left:.25in;text-align:justify;line-height:12.0pt;mso-line-height-rule:
exactly"><span style="font-size: 11pt; font-family: Arial, sans-serif;" class="">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 style="border:none windowtext 1.0pt;mso-border-alt:none windowtext 0in;
padding:0in" class="">Minor, D.L., Jr.</span> '<i class=""><span style="border:none windowtext 1.0pt;
mso-border-alt:none windowtext 0in;padding:0in" class="">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 style="border:none windowtext 1.0pt;
mso-border-alt:none windowtext 0in;padding:0in" class="">J. Gen. Physiol </span></i><b class=""><span style="border:none windowtext 1.0pt;mso-border-alt:none windowtext 0in;
padding:0in" class="">153:</span></b>e202112872<b class=""><span style="border:none windowtext 1.0pt;
mso-border-alt:none windowtext 0in;padding:0in" class=""> </span></b>(2021) </span><i class=""><span style="font-size:11.0pt;font-family:
"Arial",sans-serif;mso-bidi-language:EN-US" class=""><o:p class=""></o:p></span></i></p><p class="MsoNormal" style="margin-bottom:3.0pt;text-align:justify;line-height:
12.0pt;mso-line-height-rule:exactly"><span style="font-size:11.0pt;font-family:
"Arial",sans-serif" class="">More information is available at the lab website </span><a href="http://www.cvri.ucsf.edu/~dminor/" class=""><b class=""><span style="font-size:11.0pt;font-family:"Arial",sans-serif" class="">http://www.cvri.ucsf.edu/~dminor/</span></b></a><b class=""><span style="font-size:11.0pt;font-family:
"Arial",sans-serif" class=""><o:p class=""></o:p></span></b></p><p class="MsoNormal" style="margin-bottom:3.0pt;text-align:justify;line-height:
12.0pt;mso-line-height-rule:exactly;mso-pagination:none;mso-layout-grid-align:
none;text-autospace:none"><span style="font-size:11.0pt;font-family:"Arial",sans-serif" class="">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:3.0pt;text-align:justify;line-height:
12.0pt;mso-line-height-rule:exactly"><b class=""><span style="font-size:11.0pt;font-family:"Arial",sans-serif" class="">TO APPLY:<o:p class=""></o:p></span></b></p><p class="MsoNormal" style="margin-bottom:.1in;mso-para-margin-bottom:.6gd;
text-align:justify;mso-pagination:none;mso-layout-grid-align:none;text-autospace:
none"><span style="font-size:11.0pt;font-family:"Arial",sans-serif" class="">Interested
individuals should send a current CV to Prof. Daniel Minor at </span><a href="mailto:daniel.minor@ucsf.edu" class=""><span style="font-size:11.0pt;font-family:
"Arial",sans-serif;color:#386EFF" class="">daniel.minor@ucsf.edu</span></a><span style="font-size:11.0pt;font-family:"Arial",sans-serif" class=""><o:p class=""></o:p></span></p>
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