�ݺ�ߣshows by User: sbliven

�ݺ�ߣshows by User: sbliven / http://www.slideshare.net/images/logo.gif �ݺ�ߣshows by User: sbliven / Fri, 01 Jun 2018 14:16:34 GMT �ݺ�ߣShare feed for �ݺ�ߣshows by User: sbliven 2018-05-24 Research update on Armadillo Repeat Proteins: Evolution and Design potential /slideshow/20180524-research-update-on-armadillo-repeat-proteins-evolution-and-design-potential/99934823 2018-05-24acgt-180601141634
Presented to the ZHAW Anisimova Group on 2018-05-24]]>
Presented to the ZHAW Anisimova Group on 2018-05-24]]> Fri, 01 Jun 2018 14:16:34 GMT /slideshow/20180524-research-update-on-armadillo-repeat-proteins-evolution-and-design-potential/99934823 sbliven@slideshare.net(sbliven) 2018-05-24 Research update on Armadillo Repeat Proteins: Evolution and Design potential sbliven Presented to the ZHAW Anisimova Group on 2018-05-24 <img style="border:1px solid #C3E6D8;float:right;" alt="" src="https://cdn.slidesharecdn.com/ss_thumbnails/2018-05-24acgt-180601141634-thumbnail.jpg?width=120&height=120&fit=bounds" /> Presented to the ZHAW Anisimova Group on 2018-05-24

2018-05-24 Research update on Armadillo Repeat Proteins: Evolution and Design potential from Spencer Bliven

]]> 249 4 https://cdn.slidesharecdn.com/ss_thumbnails/2018-05-24acgt-180601141634-thumbnail.jpg?width=120&height=120&fit=bounds presentation White http://activitystrea.ms/schema/1.0/post

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0 3DSIG 2016 Presentation: Exploring Internal Symmetry and Structural Repeats with CE-Symm /slideshow/3dsig-2016-presentaion-exploring-internal-symmetry-and-structural-repeats-with-cesymm/63917370 3dsig16bliven-160711163347
Understanding the role and evolution of internal symmetry in protein structure is a fundamental question in structural biology. We present here CE-Symm 2.0, a key tool to address that question, which is able to detect all types of protein internal symmetry and provides a robust and intuitive sequence-to-structure analysis of all repeats. Notable features compared to the previous version include an optimized multiple alignment between repeats, determination of the full point group, and identification of multiple symmetry axes. We expect CE-Symm to find ample use in evolutionary studies, functional annotation, and structural classification of proteins. This work was presented at the 3DSIG 2016 conference in Orlando, FL, on July 8, 2016. See also the poster form: http://www.slideshare.net/sbliven/3dsig-2016-poster-exploring-internal-symmetry-and-structural-repeats-with-cesymm ]]>
Understanding the role and evolution of internal symmetry in protein structure is a fundamental question in structural biology. We present here CE-Symm 2.0, a key tool to address that question, which is able to detect all types of protein internal symmetry and provides a robust and intuitive sequence-to-structure analysis of all repeats. Notable features compared to the previous version include an optimized multiple alignment between repeats, determination of the full point group, and identification of multiple symmetry axes. We expect CE-Symm to find ample use in evolutionary studies, functional annotation, and structural classification of proteins. This work was presented at the 3DSIG 2016 conference in Orlando, FL, on July 8, 2016. See also the poster form: http://www.slideshare.net/sbliven/3dsig-2016-poster-exploring-internal-symmetry-and-structural-repeats-with-cesymm ]]> Mon, 11 Jul 2016 16:33:47 GMT /slideshow/3dsig-2016-presentaion-exploring-internal-symmetry-and-structural-repeats-with-cesymm/63917370 sbliven@slideshare.net(sbliven) 3DSIG 2016 Presentation: Exploring Internal Symmetry and Structural Repeats with CE-Symm sbliven Understanding the role and evolution of internal symmetry in protein structure is a fundamental question in structural biology. We present here CE-Symm 2.0, a key tool to address that question, which is able to detect all types of protein internal symmetry and provides a robust and intuitive sequence-to-structure analysis of all repeats. Notable features compared to the previous version include an optimized multiple alignment between repeats, determination of the full point group, and identification of multiple symmetry axes. We expect CE-Symm to find ample use in evolutionary studies, functional annotation, and structural classification of proteins. This work was presented at the 3DSIG 2016 conference in Orlando, FL, on July 8, 2016. See also the poster form: http://www.slideshare.net/sbliven/3dsig-2016-poster-exploring-internal-symmetry-and-structural-repeats-with-cesymm <img style="border:1px solid #C3E6D8;float:right;" alt="" src="https://cdn.slidesharecdn.com/ss_thumbnails/3dsig16bliven-160711163347-thumbnail.jpg?width=120&height=120&fit=bounds" /> Understanding the role and evolution of internal symmetry in protein structure is a fundamental question in structural biology. We present here CE-Symm 2.0, a key tool to address that question, which is able to detect all types of protein internal symmetry and provides a robust and intuitive sequence-to-structure analysis of all repeats. Notable features compared to the previous version include an optimized multiple alignment between repeats, determination of the full point group, and identification of multiple symmetry axes. We expect CE-Symm to find ample use in evolutionary studies, functional annotation, and structural classification of proteins. This work was presented at the 3DSIG 2016 conference in Orlando, FL, on July 8, 2016. See also the poster form: http://www.slideshare.net/sbliven/3dsig-2016-poster-exploring-internal-symmetry-and-structural-repeats-with-cesymm

3DSIG 2016 Presentation: Exploring Internal Symmetry and Structural Repeats with CE-Symm from Spencer Bliven

]]> 298 5 https://cdn.slidesharecdn.com/ss_thumbnails/3dsig16bliven-160711163347-thumbnail.jpg?width=120&height=120&fit=bounds presentation Black http://activitystrea.ms/schema/1.0/post

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0 Aligning Subunits of Internally Symmetric Proteins with CE-Symm /slideshow/bliven3-dsig13/40497928 bliven3dsig13-141020112106-conversion-gate01
Poster from 3DSIG 2013 on CE-Symm. For a more recent version, see http://www.slideshare.net/sbliven/3dsig-2014-systematic-detection-of-internal-symmetry-in-proteins]]>
Poster from 3DSIG 2013 on CE-Symm. For a more recent version, see http://www.slideshare.net/sbliven/3dsig-2014-systematic-detection-of-internal-symmetry-in-proteins]]> Mon, 20 Oct 2014 11:21:06 GMT /slideshow/bliven3-dsig13/40497928 sbliven@slideshare.net(sbliven) Aligning Subunits of Internally Symmetric Proteins with CE-Symm sbliven Poster from 3DSIG 2013 on CE-Symm. For a more recent version, see http://www.slideshare.net/sbliven/3dsig-2014-systematic-detection-of-internal-symmetry-in-proteins <img style="border:1px solid #C3E6D8;float:right;" alt="" src="https://cdn.slidesharecdn.com/ss_thumbnails/bliven3dsig13-141020112106-conversion-gate01-thumbnail.jpg?width=120&height=120&fit=bounds" /> Poster from 3DSIG 2013 on CE-Symm. For a more recent version, see http://www.slideshare.net/sbliven/3dsig-2014-systematic-detection-of-internal-symmetry-in-proteins

Aligning Subunits of Internally Symmetric Proteins with CE-Symm from Spencer Bliven

]]> 301 2 https://cdn.slidesharecdn.com/ss_thumbnails/bliven3dsig13-141020112106-conversion-gate01-thumbnail.jpg?width=120&height=120&fit=bounds document White http://activitystrea.ms/schema/1.0/post

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0 CE-Symm jLBR talk /slideshow/cesymm-jlbr-talk/39742350 blivenjlbr2014-141001042325-phpapp02
�ݺ�ߣs from my talk describing CE-Symm and my research on internal symmetry. It was given for jLBR, the weekly seminar series for our department at PSI.]]>
�ݺ�ߣs from my talk describing CE-Symm and my research on internal symmetry. It was given for jLBR, the weekly seminar series for our department at PSI.]]> Wed, 01 Oct 2014 04:23:24 GMT /slideshow/cesymm-jlbr-talk/39742350 sbliven@slideshare.net(sbliven) CE-Symm jLBR talk sbliven �ݺ�ߣs from my talk describing CE-Symm and my research on internal symmetry. It was given for jLBR, the weekly seminar series for our department at PSI. <img style="border:1px solid #C3E6D8;float:right;" alt="" src="https://cdn.slidesharecdn.com/ss_thumbnails/blivenjlbr2014-141001042325-phpapp02-thumbnail.jpg?width=120&height=120&fit=bounds" /> �ݺ�ߣs from my talk describing CE-Symm and my research on internal symmetry. It was given for jLBR, the weekly seminar series for our department at PSI.

CE-Symm jLBR talk from Spencer Bliven

]]> 1837 3 https://cdn.slidesharecdn.com/ss_thumbnails/blivenjlbr2014-141001042325-phpapp02-thumbnail.jpg?width=120&height=120&fit=bounds presentation White http://activitystrea.ms/schema/1.0/post

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0 Systematic detection of internal symmetry in proteins - Rheinknie Regiomeeting 2014 /slideshow/rheinknie-regiomeeting/39375695 blivenrheinknie14-140922084416-phpapp02
My talk for the 28th Rhine-Knee Regional Meeting on Biocrystallography]]>
My talk for the 28th Rhine-Knee Regional Meeting on Biocrystallography]]> Mon, 22 Sep 2014 08:44:16 GMT /slideshow/rheinknie-regiomeeting/39375695 sbliven@slideshare.net(sbliven) Systematic detection of internal symmetry in proteins - Rheinknie Regiomeeting 2014 sbliven My talk for the 28th Rhine-Knee Regional Meeting on Biocrystallography <img style="border:1px solid #C3E6D8;float:right;" alt="" src="https://cdn.slidesharecdn.com/ss_thumbnails/blivenrheinknie14-140922084416-phpapp02-thumbnail.jpg?width=120&height=120&fit=bounds" /> My talk for the 28th Rhine-Knee Regional Meeting on Biocrystallography

Systematic detection of internal symmetry in proteins - Rheinknie Regiomeeting 2014 from Spencer Bliven

]]> 1056 4 https://cdn.slidesharecdn.com/ss_thumbnails/blivenrheinknie14-140922084416-phpapp02-thumbnail.jpg?width=120&height=120&fit=bounds presentation White http://activitystrea.ms/schema/1.0/post

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0 3DSIG 2014 Presentation: Systematic detection of internal symmetry in proteins /slideshow/bliven-3-dsig14-blue/36911524 bliven3dsig14blue-140712165847-phpapp02
These slides are from 3DSIG 2014, presented on July 11. I describe our investigation of internal symmetry in protein structures. This is quite common (24% of domains), and has many implications for function, folding, and evolution. I introduce the CE-Symm method, described in Myers-Turnbull, D., Bliven, S. E., Rose, P. W., Aziz, Z. K., Youkharibache, P., Bourne, P. E., & Prlić, A. (2014). Systematic Detection of Internal Symmetry in Proteins Using CE-Symm. Journal of Molecular Biology, 426(11), 2255–2268. doi:10.1016/j.jmb.2014.03.010 I discuss the results from running CE-Symm across the PDB, as well as some particularly compelling examples. See also my poster by the same title for more details. ]]>
These slides are from 3DSIG 2014, presented on July 11. I describe our investigation of internal symmetry in protein structures. This is quite common (24% of domains), and has many implications for function, folding, and evolution. I introduce the CE-Symm method, described in Myers-Turnbull, D., Bliven, S. E., Rose, P. W., Aziz, Z. K., Youkharibache, P., Bourne, P. E., & Prlić, A. (2014). Systematic Detection of Internal Symmetry in Proteins Using CE-Symm. Journal of Molecular Biology, 426(11), 2255–2268. doi:10.1016/j.jmb.2014.03.010 I discuss the results from running CE-Symm across the PDB, as well as some particularly compelling examples. See also my poster by the same title for more details. ]]> Sat, 12 Jul 2014 16:58:47 GMT /slideshow/bliven-3-dsig14-blue/36911524 sbliven@slideshare.net(sbliven) 3DSIG 2014 Presentation: Systematic detection of internal symmetry in proteins sbliven These slides are from 3DSIG 2014, presented on July 11. I describe our investigation of internal symmetry in protein structures. This is quite common (24% of domains), and has many implications for function, folding, and evolution. I introduce the CE-Symm method, described in Myers-Turnbull, D., Bliven, S. E., Rose, P. W., Aziz, Z. K., Youkharibache, P., Bourne, P. E., & Prlić, A. (2014). Systematic Detection of Internal Symmetry in Proteins Using CE-Symm. Journal of Molecular Biology, 426(11), 2255–2268. doi:10.1016/j.jmb.2014.03.010 I discuss the results from running CE-Symm across the PDB, as well as some particularly compelling examples. See also my poster by the same title for more details. <img style="border:1px solid #C3E6D8;float:right;" alt="" src="https://cdn.slidesharecdn.com/ss_thumbnails/bliven3dsig14blue-140712165847-phpapp02-thumbnail.jpg?width=120&height=120&fit=bounds" /> These slides are from 3DSIG 2014, presented on July 11. I describe our investigation of internal symmetry in protein structures. This is quite common (24% of domains), and has many implications for function, folding, and evolution. I introduce the CE-Symm method, described in Myers-Turnbull, D., Bliven, S. E., Rose, P. W., Aziz, Z. K., Youkharibache, P., Bourne, P. E., & Prlić, A. (2014). Systematic Detection of Internal Symmetry in Proteins Using CE-Symm. Journal of Molecular Biology, 426(11), 2255–2268. doi:10.1016/j.jmb.2014.03.010 I discuss the results from running CE-Symm across the PDB, as well as some particularly compelling examples. See also my poster by the same title for more details.

3DSIG 2014 Presentation: Systematic detection of internal symmetry in proteins from Spencer Bliven

]]> 2235 5 https://cdn.slidesharecdn.com/ss_thumbnails/bliven3dsig14blue-140712165847-phpapp02-thumbnail.jpg?width=120&height=120&fit=bounds presentation White http://activitystrea.ms/schema/1.0/post

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0 Journal Club 2013-09-10: Pandya et al /slideshow/journal-club-20130910-rossmann-sf/26076190 2013-09-10rossmannsf-130910155654-phpapp01
Journal club presentation on: Pandya, C., Brown, S., Pieper, U., Šali, A., Dunaway-Mariano, D., Babbitt, P. C., et al. (2013). Consequences of domain insertion on sequence-structure divergence in a superfold. Proceedings of the National Academy of Sciences of the United States of America, 110(36), E3381–7. doi:10.1073/pnas.1305519110]]>
Journal club presentation on: Pandya, C., Brown, S., Pieper, U., Šali, A., Dunaway-Mariano, D., Babbitt, P. C., et al. (2013). Consequences of domain insertion on sequence-structure divergence in a superfold. Proceedings of the National Academy of Sciences of the United States of America, 110(36), E3381–7. doi:10.1073/pnas.1305519110]]> Tue, 10 Sep 2013 15:56:54 GMT /slideshow/journal-club-20130910-rossmann-sf/26076190 sbliven@slideshare.net(sbliven) Journal Club 2013-09-10: Pandya et al sbliven Journal club presentation on: Pandya, C., Brown, S., Pieper, U., Šali, A., Dunaway-Mariano, D., Babbitt, P. C., et al. (2013). Consequences of domain insertion on sequence-structure divergence in a superfold. Proceedings of the National Academy of Sciences of the United States of America, 110(36), E3381–7. doi:10.1073/pnas.1305519110 <img style="border:1px solid #C3E6D8;float:right;" alt="" src="https://cdn.slidesharecdn.com/ss_thumbnails/2013-09-10rossmannsf-130910155654-phpapp01-thumbnail.jpg?width=120&height=120&fit=bounds" /> Journal club presentation on: Pandya, C., Brown, S., Pieper, U., Šali, A., Dunaway-Mariano, D., Babbitt, P. C., et al. (2013). Consequences of domain insertion on sequence-structure divergence in a superfold. Proceedings of the National Academy of Sciences of the United States of America, 110(36), E3381–7. doi:10.1073/pnas.1305519110

Journal Club 2013-09-10: Pandya et al from Spencer Bliven

]]> 2867 3 https://cdn.slidesharecdn.com/ss_thumbnails/2013-09-10rossmannsf-130910155654-phpapp01-thumbnail.jpg?width=120&height=120&fit=bounds presentation White http://activitystrea.ms/schema/1.0/post

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0 Following the Evolution of New Protein Folds via Protodomains [Report] /sbliven/following-the-evolution-of-new-protein-folds-via-protodomains-report blivencandidacyexam-130129194914-phpapp02
Protein evolution proceeds through genetic mechanisms, but selection acts on biological assemblies. I define a protodomain as a minimal independently evolving unit with conserved structure. Protodomain rearrangements have minimal impact on biological assemblies, so they represent a valid evolutionary path through fold space. This report is the written portion of my Candidacy Exam at University of California, San Diego. It discusses my current research in Philip Bourne's lab, as well as proposes research for my thesis over the next two years. �ݺ�ߣs for the oral presentation are available at http://www.slideshare.net/sbliven/following-the-evolution-of-new-protein-folds-via-protodomains]]>
Protein evolution proceeds through genetic mechanisms, but selection acts on biological assemblies. I define a protodomain as a minimal independently evolving unit with conserved structure. Protodomain rearrangements have minimal impact on biological assemblies, so they represent a valid evolutionary path through fold space. This report is the written portion of my Candidacy Exam at University of California, San Diego. It discusses my current research in Philip Bourne's lab, as well as proposes research for my thesis over the next two years. �ݺ�ߣs for the oral presentation are available at http://www.slideshare.net/sbliven/following-the-evolution-of-new-protein-folds-via-protodomains]]> Tue, 29 Jan 2013 19:49:14 GMT /sbliven/following-the-evolution-of-new-protein-folds-via-protodomains-report sbliven@slideshare.net(sbliven) Following the Evolution of New Protein Folds via Protodomains [Report] sbliven Protein evolution proceeds through genetic mechanisms, but selection acts on biological assemblies. I define a protodomain as a minimal independently evolving unit with conserved structure. Protodomain rearrangements have minimal impact on biological assemblies, so they represent a valid evolutionary path through fold space. This report is the written portion of my Candidacy Exam at University of California, San Diego. It discusses my current research in Philip Bourne's lab, as well as proposes research for my thesis over the next two years. �ݺ�ߣs for the oral presentation are available at http://www.slideshare.net/sbliven/following-the-evolution-of-new-protein-folds-via-protodomains <img style="border:1px solid #C3E6D8;float:right;" alt="" src="https://cdn.slidesharecdn.com/ss_thumbnails/blivencandidacyexam-130129194914-phpapp02-thumbnail.jpg?width=120&height=120&fit=bounds" /> Protein evolution proceeds through genetic mechanisms, but selection acts on biological assemblies. I define a protodomain as a minimal independently evolving unit with conserved structure. Protodomain rearrangements have minimal impact on biological assemblies, so they represent a valid evolutionary path through fold space. This report is the written portion of my Candidacy Exam at University of California, San Diego. It discusses my current research in Philip Bourne's lab, as well as proposes research for my thesis over the next two years. �ݺ�ߣs for the oral presentation are available at http://www.slideshare.net/sbliven/following-the-evolution-of-new-protein-folds-via-protodomains

Following the Evolution of New Protein Folds via Protodomains [Report] from Spencer Bliven

]]> 708 5 https://cdn.slidesharecdn.com/ss_thumbnails/blivencandidacyexam-130129194914-phpapp02-thumbnail.jpg?width=120&height=120&fit=bounds document White http://activitystrea.ms/schema/1.0/post

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0 Following the Evolution of New Protein Folds via Protodomains /slideshow/following-the-evolution-of-new-protein-folds-via-protodomains/16246306 blivencandidacyexam-130129185959-phpapp02
Protein evolution proceeds through genetic mechanisms, but selection acts on biological assemblies. I define a protodomain as a minimal independently evolving unit with conserved structure. Protodomain rearrangements have minimal impact on biological assemblies, so they represent a valid evolutionary path through fold space. These slides are from my Candidacy Exam on Jan 28, 2013 at University of California, San Diego. It discusses my current research in Philip Bourne's lab, as well as proposes research for my thesis over the next two years. An audio version is available at http://www.scivee.tv/node/57082]]>
Protein evolution proceeds through genetic mechanisms, but selection acts on biological assemblies. I define a protodomain as a minimal independently evolving unit with conserved structure. Protodomain rearrangements have minimal impact on biological assemblies, so they represent a valid evolutionary path through fold space. These slides are from my Candidacy Exam on Jan 28, 2013 at University of California, San Diego. It discusses my current research in Philip Bourne's lab, as well as proposes research for my thesis over the next two years. An audio version is available at http://www.scivee.tv/node/57082]]> Tue, 29 Jan 2013 18:59:59 GMT /slideshow/following-the-evolution-of-new-protein-folds-via-protodomains/16246306 sbliven@slideshare.net(sbliven) Following the Evolution of New Protein Folds via Protodomains sbliven Protein evolution proceeds through genetic mechanisms, but selection acts on biological assemblies. I define a protodomain as a minimal independently evolving unit with conserved structure. Protodomain rearrangements have minimal impact on biological assemblies, so they represent a valid evolutionary path through fold space. These slides are from my Candidacy Exam on Jan 28, 2013 at University of California, San Diego. It discusses my current research in Philip Bourne's lab, as well as proposes research for my thesis over the next two years. An audio version is available at http://www.scivee.tv/node/57082 <img style="border:1px solid #C3E6D8;float:right;" alt="" src="https://cdn.slidesharecdn.com/ss_thumbnails/blivencandidacyexam-130129185959-phpapp02-thumbnail.jpg?width=120&height=120&fit=bounds" /> Protein evolution proceeds through genetic mechanisms, but selection acts on biological assemblies. I define a protodomain as a minimal independently evolving unit with conserved structure. Protodomain rearrangements have minimal impact on biological assemblies, so they represent a valid evolutionary path through fold space. These slides are from my Candidacy Exam on Jan 28, 2013 at University of California, San Diego. It discusses my current research in Philip Bourne's lab, as well as proposes research for my thesis over the next two years. An audio version is available at http://www.scivee.tv/node/57082

Following the Evolution of New Protein Folds via Protodomains from Spencer Bliven

]]> 764 5 https://cdn.slidesharecdn.com/ss_thumbnails/blivencandidacyexam-130129185959-phpapp02-thumbnail.jpg?width=120&height=120&fit=bounds presentation White http://activitystrea.ms/schema/1.0/post

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0 Topic Pages: The Peer-reviewed Wikipedia Article (BOSC 2012 Poster) /slideshow/bosc-2012-poster-topic-pages-the-peerreviewed-wikipedia-article/13688327 topicpageposter-120718192424-phpapp02
PLoS Computational Biology recently launched a new initiative called Topic Pages with the goal of motivating scientists to write Wikipedia articles for computational biology topics. This poster gives some resources for interested authors to get started. This poster was presented at BOSC 2012. My thanks to Eagle Genomics for their generous Student Travel Award. �ݺ�ߣs from the talk which accompanied this poster are also available on slideshare, from http://www.slideshare.net/jandot/s-bliven-why-scientists-should-contribute-to-wikipedia]]>
PLoS Computational Biology recently launched a new initiative called Topic Pages with the goal of motivating scientists to write Wikipedia articles for computational biology topics. This poster gives some resources for interested authors to get started. This poster was presented at BOSC 2012. My thanks to Eagle Genomics for their generous Student Travel Award. �ݺ�ߣs from the talk which accompanied this poster are also available on slideshare, from http://www.slideshare.net/jandot/s-bliven-why-scientists-should-contribute-to-wikipedia]]> Wed, 18 Jul 2012 19:24:21 GMT /slideshow/bosc-2012-poster-topic-pages-the-peerreviewed-wikipedia-article/13688327 sbliven@slideshare.net(sbliven) Topic Pages: The Peer-reviewed Wikipedia Article (BOSC 2012 Poster) sbliven PLoS Computational Biology recently launched a new initiative called Topic Pages with the goal of motivating scientists to write Wikipedia articles for computational biology topics. This poster gives some resources for interested authors to get started. This poster was presented at BOSC 2012. My thanks to Eagle Genomics for their generous Student Travel Award. �ݺ�ߣs from the talk which accompanied this poster are also available on slideshare, from http://www.slideshare.net/jandot/s-bliven-why-scientists-should-contribute-to-wikipedia <img style="border:1px solid #C3E6D8;float:right;" alt="" src="https://cdn.slidesharecdn.com/ss_thumbnails/topicpageposter-120718192424-phpapp02-thumbnail.jpg?width=120&height=120&fit=bounds" /> PLoS Computational Biology recently launched a new initiative called Topic Pages with the goal of motivating scientists to write Wikipedia articles for computational biology topics. This poster gives some resources for interested authors to get started. This poster was presented at BOSC 2012. My thanks to Eagle Genomics for their generous Student Travel Award. �ݺ�ߣs from the talk which accompanied this poster are also available on slideshare, from http://www.slideshare.net/jandot/s-bliven-why-scientists-should-contribute-to-wikipedia

Topic Pages: The Peer-reviewed Wikipedia Article (BOSC 2012 Poster) from Spencer Bliven

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0 https://cdn.slidesharecdn.com/profile-photo-sbliven-48x48.jpg?cb=1718132670 I am currently a PhD student in Bioinformatics at UCSD. I am a member of Philip Bourne's lab, where I work on protein structural. In particular, I am interested in algorithms for comparing protein structure, and the application of such algorithms for gaining insights about protein fold space. As a computational biologist, I enjoy both the technical challenges associated with writing good code and the beauty of biological systems. Specialties: Experience with: Java, including Swing and Java 1.5 features; Objective-C and Cocoa; PHP, Javascript, AJAX, CSS, and MySQL; Mac OS X, Linux, and Windows; https://cdn.slidesharecdn.com/ss_thumbnails/2018-05-24acgt-180601141634-thumbnail.jpg?width=320&height=320&fit=bounds slideshow/20180524-research-update-on-armadillo-repeat-proteins-evolution-and-design-potential/99934823 2018-05-24 Research up... https://cdn.slidesharecdn.com/ss_thumbnails/3dsig16bliven-160711163347-thumbnail.jpg?width=320&height=320&fit=bounds slideshow/3dsig-2016-presentaion-exploring-internal-symmetry-and-structural-repeats-with-cesymm/63917370 3DSIG 2016 Presentatio... https://cdn.slidesharecdn.com/ss_thumbnails/bliven3dsig13-141020112106-conversion-gate01-thumbnail.jpg?width=320&height=320&fit=bounds slideshow/bliven3-dsig13/40497928 Aligning Subunits of I...