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	<title><![CDATA[BOL: Related items]]></title>
	<link>https://bioinformaticsonline.com/related/10260?offset=1110</link>
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	<description><![CDATA[]]></description>
	
	
<item>
  <guid isPermaLink='true'>https://bioinformaticsonline.com/opportunity/view/22938/research-assistant-in-computational-biology</guid>
  <pubDate>Wed, 24 Jun 2015 07:55:16 -0500</pubDate>
  <link></link>
  <title><![CDATA[Research assistant in computational biology]]></title>
  <description><![CDATA[
<p>http://www.au.dk/en/about/vacant-positions/scientific-positions/stillinger/Vacancy/show/743161/5283/</p>

<p>Qualifications:<br />MSc degree in computer science, engineering, genetics or similar field with a strong emphasis on computational methods.</p>

<p>Deadline<br />01.08.2015</p>
]]></description>
</item>
<item>
	<guid isPermaLink="true">https://bioinformaticsonline.com/videolist/watch/12943/a-history-of-bioinformatics-in-the-year-2039</guid>
	<pubDate>Wed, 23 Jul 2014 06:37:51 -0500</pubDate>
	<link>https://bioinformaticsonline.com/videolist/watch/12943/a-history-of-bioinformatics-in-the-year-2039</link>
	<title><![CDATA[A History of Bioinformatics (in the Year 2039)]]></title>
	<description><![CDATA[<iframe width="" height="" src="https://www.youtube-nocookie.com/embed/uwsjwMO-TEA" frameborder="0" allowfullscreen></iframe><p>C. Titus Brown http://video.open-bio.org/video/1/a-history-of-bioinformatics-in-the-year-2039</p>]]></description>
	
</item>
<item>
	<guid isPermaLink="true">https://bioinformaticsonline.com/bookmarks/view/4943/molecular-genetics-lecture</guid>
	<pubDate>Fri, 27 Sep 2013 04:24:45 -0500</pubDate>
	<link>https://bioinformaticsonline.com/bookmarks/view/4943/molecular-genetics-lecture</link>
	<title><![CDATA[Molecular Genetics Lecture]]></title>
	<description><![CDATA[<p><span>"Robert Sapolsky makes interdisciplinary connections between behavioral biology and molecular genetic influences. He relates protein synthesis and point mutations to microevolutionary change, and discusses conflicting theories of gradualism and punctuated equilibrium and the influence of epigenetics on development theories."&nbsp;</span></p>
<p><span>"<span><strong>Robert Sapolsky</strong> is an American neuroendocrinologist, professor of biology, neuroscience, and neurosurgery at Stanford University, researcher and author" ----Wikipedia</span></span></p><p>Address of the bookmark: <a href="http://www.youtube.com/watch?v=_dRXA1_e30o" rel="nofollow">http://www.youtube.com/watch?v=_dRXA1_e30o</a></p>]]></description>
	<dc:creator>Rahul Agarwal</dc:creator>
</item>
<item>
	<guid isPermaLink="true">https://bioinformaticsonline.com/bookmarks/view/36752/minmax-a-versatile-tool-for-calculating-and-comparing-synonymous-codon-usage-and-its-impact-on-protein-folding</guid>
	<pubDate>Thu, 24 May 2018 02:53:31 -0500</pubDate>
	<link>https://bioinformaticsonline.com/bookmarks/view/36752/minmax-a-versatile-tool-for-calculating-and-comparing-synonymous-codon-usage-and-its-impact-on-protein-folding</link>
	<title><![CDATA[%MinMax: A versatile tool for calculating and comparing synonymous codon usage and its impact on protein folding.]]></title>
	<description><![CDATA[%MM calculates whether a given gene sequence encodes amino acids using the most common codons possible, the least common codons possible, or (most typically) some combination of these extremes. See our PLoS ONE paper for more details on how the %MinMax algorithm works. 

%MinMax results are averaged over an 18-codon sliding window; hence the result for "codon window = 1" is the average codon usage for codons 1-18, codon window 2 = codons 2-19, etc.<p>Address of the bookmark: <a href="http://www.codons.org/" rel="nofollow">http://www.codons.org/</a></p>]]></description>
	<dc:creator>Surabhi Chaudhary</dc:creator>
</item>
<item>
	<guid isPermaLink="true">https://bioinformaticsonline.com/bookmarks/view/37965/kobas-a-web-server-for-geneprotein-functional-annotation-and-functional-gene-set-enrichment</guid>
	<pubDate>Fri, 19 Oct 2018 09:36:11 -0500</pubDate>
	<link>https://bioinformaticsonline.com/bookmarks/view/37965/kobas-a-web-server-for-geneprotein-functional-annotation-and-functional-gene-set-enrichment</link>
	<title><![CDATA[KOBAS: a web server for gene/protein functional annotation and functional gene set enrichment]]></title>
	<description><![CDATA[<p><span>KOBAS 3.0 is a web server for gene/protein functional annotation (</span><a href="http://kobas.cbi.pku.edu.cn/annotate.php">Annotate</a><span>&nbsp;module) and functional gene set enrichment(Enrichment module). For Annotate module, it accepts gene list as input, including IDs or sequences, and generates annotations for each gene based on multiple databases about pathways, diseases, and Gene Ontology. For Enrichment module, it can accept either gene list or gene expression data as input, and generates enriched gene sets, corresponding name, p-value or a probability of enrichment and enrichment score based on results of multiple methods.</span></p><p>Address of the bookmark: <a href="http://kobas.cbi.pku.edu.cn/" rel="nofollow">http://kobas.cbi.pku.edu.cn/</a></p>]]></description>
	<dc:creator>Jit</dc:creator>
</item>
<item>
	<guid isPermaLink="true">https://bioinformaticsonline.com/bookmarks/view/42405/caretta-%E2%80%93-a-multiple-protein-structure-alignment-and-feature-extraction-suite</guid>
	<pubDate>Fri, 18 Dec 2020 02:09:44 -0600</pubDate>
	<link>https://bioinformaticsonline.com/bookmarks/view/42405/caretta-%E2%80%93-a-multiple-protein-structure-alignment-and-feature-extraction-suite</link>
	<title><![CDATA[Caretta – A multiple protein structure alignment and feature extraction suite]]></title>
	<description><![CDATA[<h3>Caretta &ndash;&nbsp;a multiple protein structure alignment and feature extraction suite</h3>
<p><span>Caretta, a multiple structure alignment suite meant for homologous but sequentially divergent protein families which consistently returns accurate alignments with a higher coverage than current state-of-the-art tools. Caretta is available as a GUI and command-line application and additionally outputs an aligned structure feature matrix for a given set of input structures, which can readily be used in downstream steps for supervised or unsupervised machine learning.&nbsp;</span></p><p>Address of the bookmark: <a href="http://www.bioinformatics.nl/caretta/" rel="nofollow">http://www.bioinformatics.nl/caretta/</a></p>]]></description>
	<dc:creator>Rahul Nayak</dc:creator>
</item>

<item>
  <guid isPermaLink='true'>https://bioinformaticsonline.com/researchlabs/view/4546/sowdhamini-lab</guid>
  <pubDate>Sun, 15 Sep 2013 09:19:12 -0500</pubDate>
  <link></link>
  <title><![CDATA[SOWDHAMINI Lab]]></title>
  <description><![CDATA[
<p>Genome sequencing projects have enormous potential for benefiting human endeavors. However, just as acquiring a language's vocabulary does not enable one to speak it, databases that list the amino acid composition of proteins do not directly tell us much about these proteins' higher-level structure and function. The most productive way to indirectly exploit these databases has been to start with the small number of proteins that are fully-characterised and to assume that other "similar" proteins will have a related structure and function. Proteins with very similar amino acid sequence are "no-brainers", but the real test, which our group largely focuses on, is to detect the "essential" similarity in proteins whose non-critical sections have experienced random rearrangements during evolution. In such cases functionally similar proteins may have less than 25% sequence overlap.</p>

<p>More @ http://www.ncbs.res.in/sowdhamini/groups_sowdhamini.htm</p>
]]></description>
</item>
<item>
	<guid isPermaLink="true">https://bioinformaticsonline.com/bookmarks/view/33789/i-pv-interactive-protein-sequence-visualization</guid>
	<pubDate>Mon, 03 Jul 2017 07:52:51 -0500</pubDate>
	<link>https://bioinformaticsonline.com/bookmarks/view/33789/i-pv-interactive-protein-sequence-visualization</link>
	<title><![CDATA[I-PV: Interactive Protein Sequence Visualization]]></title>
	<description><![CDATA[<p><span>I-PV is a interactive data visualization software designed for inspection of protein sequences and mutation information. It is mainly used for Genetics and Bioinformatics. So what exactly makes it standout?</span></p>
<p><span>http://i-pv.org/ipv_rec</span></p><p>Address of the bookmark: <a href="http://i-pv.org/" rel="nofollow">http://i-pv.org/</a></p>]]></description>
	<dc:creator>Jit</dc:creator>
</item>
<item>
	<guid isPermaLink="true">https://bioinformaticsonline.com/pages/view/36392/protein-protein-interaction-sites-predictions</guid>
	<pubDate>Wed, 25 Apr 2018 04:53:20 -0500</pubDate>
	<link>https://bioinformaticsonline.com/pages/view/36392/protein-protein-interaction-sites-predictions</link>
	<title><![CDATA[Protein-Protein Interaction Sites Predictions !]]></title>
	<description><![CDATA[<p><span>The study of Protein&ndash;Protein Interactions (PPIs) has a crucial role in biology, medicine and the pharmaceutical industry. PPIs can be investigated from two aspects: The interaction partners of a specific protein and the amino acid residues participating in a given PPI. Information about a protein&rsquo;s interaction partners allows scientists to construct protein interaction networks, such as signaling pathways, which in turn facilitate the understanding of many biological and clinical observations.&nbsp;</span></p><p><span>Following are the list of tools commonly used to PPIs predictions:</span></p><p>Protein-Protein Interaction Sites</p><p><a href="http://pipe.scs.fsu.edu/ppisp.html" target="_blank">PPISP</a></p><p>A consensus neural network method for predicting protein-protein interaction sites</p><p><a href="http://biunit.naist.jp/homcos/" target="_blank">HOMCOS</a></p><p>A server to predict interacting protein pairs and interacting sites by homology modeling of complex structures</p><p><a href="http://prism.ccbb.ku.edu.tr/hotpoint/" target="_blank">HotPOINT</a></p><p>Prediction of protein interfaces using an empirical model</p><p><a href="http://cubic.bioc.columbia.edu/services/isis/" target="_blank">ISIS</a></p><p>Prediction of interaction hotspots from sequence</p><p><a href="http://kfc.mitchell-lab.org/" target="_blank">KFC server</a></p><p>Automated decision-tree approach to predicting protein-protein interaction hot spots</p><p><a href="http://pipe.scs.fsu.edu/meta-ppisp.html" target="_blank">meta-PPISP</a></p><p>A meta server for predicting protein-protein interaction sites. meta-PPISP is built on three individual web servers:&nbsp;<a href="https://bip.weizmann.ac.il/toolbox/structure/binding.htm#cons">cons-PPISP</a>,&nbsp;<a href="https://bip.weizmann.ac.il/toolbox/structure/binding.htm#pin">PINUP</a>, and&nbsp;<a href="https://bip.weizmann.ac.il/toolbox/structure/binding.htm#pro">Promate</a></p><p><a href="http://www.molsoft.com/oda.html" target="_blank">ODA</a></p><p>Identification of optimal surface patches with the lowest docking desolvation energy values</p><p><a href="http://sparks.informatics.iupui.edu/PINUP/" target="_blank">PINUP</a></p><p>Protein binding site prediction with an empirical scoring function</p><p>Other Sites (DNA, RNA, Metals)</p><p><a href="http://ligin.weizmann.ac.il/~lpgerzon/mbs4/mbs.cgi" target="_blank">CHED</a>&nbsp;</p><p>Web server for predicting soft metal binding sites in proteins</p><p><a href="http://cssb.biology.gatech.edu/skolnick/webservice/DBD-Hunter/" target="_blank">DBD-Hunter</a></p><p>A knowledge-based method for the prediction of DNA-protein interactions</p><p><a href="http://pipe.scs.fsu.edu/displar.html" target="_blank">DISPLAR</a></p><p>Given the structure of a protein known to bind DNA, the method predicts residues that contact DNA using neural network method</p><p><a href="http://idbps.tau.ac.il/" target="_blank">iDBPs</a></p><p>Predicts DNA binding proteins for proteins with known 3D structure.</p><p><a href="http://pfp.technion.ac.il/" target="_blank">PFplus</a></p><div style="text-align: left;">A tool for extracting and displaying positive electrostatic patches on protein surfaces which can be indicative of nucleic acid binding interfaces.</div>]]></description>
	<dc:creator>Poonam Mahapatra</dc:creator>
</item>
<item>
	<guid isPermaLink="true">https://bioinformaticsonline.com/bookmarks/view/44882/fantasia</guid>
	<pubDate>Wed, 20 Aug 2025 02:48:15 -0500</pubDate>
	<link>https://bioinformaticsonline.com/bookmarks/view/44882/fantasia</link>
	<title><![CDATA[FANTASIA]]></title>
	<description><![CDATA[<p dir="auto">FANTASIA is an advanced pipeline for the automatic functional annotation of protein sequences using state-of-the-art protein language models. It integrates deep learning embeddings and in-memory similarity searches, retrieving reference vectors from a PostgreSQL database with pgvector, to associate Gene Ontology (GO) terms with proteins.</p>
<p>https://www.nature.com/articles/s42003-025-08651-2</p><p>Address of the bookmark: <a href="https://github.com/CBBIO/FANTASIA" rel="nofollow">https://github.com/CBBIO/FANTASIA</a></p>]]></description>
	<dc:creator>BioStar</dc:creator>
</item>

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