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	<title><![CDATA[BOL: Related items]]></title>
	<link>https://bioinformaticsonline.com/related/37669?offset=60</link>
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	<guid isPermaLink="true">https://bioinformaticsonline.com/news/view/4295/rcsb-pdb-sept13-release</guid>
	<pubDate>Thu, 05 Sep 2013 15:07:48 -0500</pubDate>
	<link>https://bioinformaticsonline.com/news/view/4295/rcsb-pdb-sept13-release</link>
	<title><![CDATA[RCSB PDB Sept'13 Release]]></title>
	<description><![CDATA[<p>RCSB PDB Sept'13 Release offers following new features:</p><p>- New tools to search for drugs and drug targets<br />- Improved interface for 3D visualisation using Jmol/JSmol<br />- An update to the representation of protein symmetry and stoichiometry.<br />- Improvements when performing sequence searches.</p><p>Reference</p><p><a href="http://www.rcsb.org/pdb/static.do?p=general_information/whats_new.jsp?b=1308">http://www.rcsb.org/pdb/static.do?p=general_information/whats_new.jsp?b=1308</a></p><p>&nbsp;</p>]]></description>
	<dc:creator>Jitendra Narayan</dc:creator>
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  <guid isPermaLink='true'>https://bioinformaticsonline.com/researchlabs/view/5210/sandelin-group</guid>
  <pubDate>Mon, 30 Sep 2013 19:12:58 -0500</pubDate>
  <link></link>
  <title><![CDATA[Sandelin group]]></title>
  <description><![CDATA[
<p>Sandelin group have a deep interest in most biology, but focus on gene regulation and the many areas that are connected with this, including transcriptomics, epigenetics and technological and informatics aspects.</p>

<p>The group is both computational and experimental.</p>

<p>We ask biological questions to large datasets made using novel genomics techniques, with the help of computers. One of the strengths in the group are the many connections to high-profile experimental laboratories which supply data to be analyzed.</p>

<p>Lab webpage @ http://people.binf.ku.dk/albin/Sandelin_group_at_the_Bioinformatic_Centre/The_Sandelin_group.html</p>
]]></description>
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  <guid isPermaLink='true'>https://bioinformaticsonline.com/researchlabs/view/7214/lapti-lab</guid>
  <pubDate>Thu, 12 Dec 2013 18:19:12 -0600</pubDate>
  <link></link>
  <title><![CDATA[LAPTI Lab]]></title>
  <description><![CDATA[
<p>The main theme of our research is the understanding of how genetic information is decoded from DNA into RNA and proteins. Someone may find this topic a little strange and argue that we already know how this is happening.</p>

<p>Translational recoding. </p>

<p>RNA editing. </p>

<p>Evolution of the genetic code and translation.</p>

<p>More at http://lapti.ucc.ie/research.html</p>

<p>Lab page http://lapti.ucc.ie/index.html</p>
]]></description>
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  <guid isPermaLink='true'>https://bioinformaticsonline.com/opportunity/view/13338/protein-function-annotation-and-machine-learning-upmc-paris-france</guid>
  <pubDate>Sat, 02 Aug 2014 01:22:52 -0500</pubDate>
  <link></link>
  <title><![CDATA[Protein function annotation and machine learning - UPMC - Paris, France]]></title>
  <description><![CDATA[
<p>Protein function annotation and machine learning - UPMC - Paris, France</p>

<p>Job Description: We are interested in finding an excellent postdoc with interests in protein functional annotation, machine learning and computer grids. The position is open for 3.5 years at the Université Pierre et Marie Curie, in the heart of paris.</p>

<p>Research topic: Protein function annotation, multiple probabilistic models, domain architecture, machine learning, combinatorial optimization, computer grid.</p>

<p>Title: A novel integrative platform for large scale protein annotation that exploits a multitude of diversified probabilistic models in several protein signature databases.</p>

<p>We propose a novel integrated approach for large scale protein annotation that will exploit an unprecedented amount of genomic data as well as sophisticated machine learning techniques and combinatorial optimization approaches taking advantages of High Performance Computing (HPC) environments. The idea is to uncover as much as possible the evolutionary processes of protein sequences that took place throughout the whole tree of life and that affected the evolution of a protein family. We have already demonstrated in a previous work that the problem of functional annotation is inherent to the ability of uncovering such paths. Now, we shall extend this approach to large scale genome annotation by considering 11 different protein databases, constituted by about 10^9 protein sequences, and by producing a large pool of diversified probabilistic models coding for about 10^7 evolutionary protein pathways. Such models will be used to search for specific domains in genomes to be annotated. Our previous methodology needs to be fundamentally improved to deal with this large amount of biological data. In this project, we shall work on the algorithms to reduce the space of models and the search complexity, and we shall implement some important algorithmic changes towards the realization of a powerful integrated annotation tool.</p>

<p>Where: This project is run on the Laboratoire de Biologie Computationnelle et Quantitative UMR7238 CNRS-UPMC – Analytical Genomics team, headed by A.Carbone. It is co-advised with Pierre-Henri Wuillemin, Laboratoire d’Informatique de Paris 6 – Equipe DECISION.</p>

<p>Start date: September 1st, 2014<br />Contact Person: Alessandra Carbone<br />Contact: alessandra.carbone@lip6.fr</p>
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  <guid isPermaLink='true'>https://bioinformaticsonline.com/opportunity/view/18820/jrfsrf-at-university-of-calcutta</guid>
  <pubDate>Fri, 31 Oct 2014 08:53:10 -0500</pubDate>
  <link></link>
  <title><![CDATA[JRF/SRF at University of Calcutta]]></title>
  <description><![CDATA[
<p>Applications are invited to appear at a walk-in-interview for one post of Junior Research Fellow in the DBT(DBT Twinning NER) sponsored project entitled “Protein folding kinetics is a selection force on shaping codon usage bias in the high expression genes” in the room of the HOD, Department of Biotechnology and the Coordinator, DR. B. C. Guha Centre for Genetic Engineering and Biotechnology, University College of Science, 35 Ballygunge Circular Road, Kolkata 700019 on the 12th November, 2014 at 3:00 p.m.</p>

<p>Essential qualifications: First class M. Sc. in any branch of life sciences and qualified CSIR-UGC NET/GATE Examination.</p>

<p>Desirable qualifications: Practical experience in biochemical and biophysical studies of proteins</p>

<p>Emoluments: as per DBT norms</p>

<p>The project is tenable for two years, initially for one year.</p>

<p>Age: Below 28 years (relaxable in the case of SC/ST/OBC/women candidates)</p>

<p>Candidates are requested to bring two sets of complete applications on plain paper furnishing bio-data and copies of attested certificates along with originals (for verification) on the date of interview.</p>

<p>No TA/DA is admissible for candidates appearing at the interview.</p>

<p>Dr. Rajat Banerjee<br />Assistant Professor<br />Department of Biotechnology and<br />Dr. B. C. Guha Centre for Genetic Engineering and Biotechnology<br />University College of Science<br />35, Ballygunge Circular Road<br />Kolkata 700019</p>

<p>Advertisement: www.caluniv.ac.in/news/jrf_biotech_2.pdf</p>
]]></description>
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	<guid isPermaLink="true">https://bioinformaticsonline.com/bookmarks/view/31278/metapred2cs</guid>
	<pubDate>Fri, 03 Mar 2017 05:15:07 -0600</pubDate>
	<link>https://bioinformaticsonline.com/bookmarks/view/31278/metapred2cs</link>
	<title><![CDATA[MetaPred2CS]]></title>
	<description><![CDATA[<p style="text-align: justify;"><strong>MetaPred2CS Web server&nbsp;</strong>is a meta-predictor based on&nbsp;<a href="http://www.ncbi.nlm.nih.gov/pubmed/17160063">Support Vector Machine (SVM)</a>&nbsp;that combines 6 individual sequence based protein-protein interaction prediction methods to predict&nbsp;<strong>prokaryotic two-component system&nbsp;</strong>protein-protein interactions (PPIs). The methods implemented in MetaPred2CS are 2 co-evolutionary methods:&nbsp;<a href="http://www.ncbi.nlm.nih.gov/pubmed/11933068">in-silico two hybrid (i2h)</a>&nbsp;and&nbsp;<a href="http://www.ncbi.nlm.nih.gov/pubmed/11707606">mirror tree (MT)</a>&nbsp;methods and 4 genomics context based methods:&nbsp;<a href="http://www.ncbi.nlm.nih.gov/pubmed/15947018">phylogenetic profiling (PP)</a>,&nbsp;<a href="http://www.ncbi.nlm.nih.gov/pubmed/10573422">gene fusion (GF)</a>,&nbsp;<a href="http://www.ploscompbiol.org/article/info%3Adoi%2F10.1371%2Fjournal.pcbi.0030043">gene neighbourhood (GN)</a>&nbsp;and and&nbsp;<a href="http://www.ploscompbiol.org/article/info%3Adoi%2F10.1371%2Fjournal.pcbi.0030043">gene operon methods (GO)</a>.</p>
<p>&nbsp;http://metapred2cs.ibers.aber.ac.uk/</p><p>Address of the bookmark: <a href="https://github.com/martinjvickers/MetaPred2CS" rel="nofollow">https://github.com/martinjvickers/MetaPred2CS</a></p>]]></description>
	<dc:creator>Manisha Mishra</dc:creator>
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	<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>
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  <guid isPermaLink='true'>https://bioinformaticsonline.com/researchlabs/view/17501/nieduszynski-group</guid>
  <pubDate>Fri, 26 Sep 2014 19:35:06 -0500</pubDate>
  <link></link>
  <title><![CDATA[Nieduszynski Group]]></title>
  <description><![CDATA[
<p>Complete, accurate replication of the genome is essential for life. All chromosomes in eukaryotic cells must be duplicated and then segregated to daughter cells to ensure genetic integrity and produce the large number of cells that make up a multicellular organism. We are using genetic, genomic and computational methods to understand how chromosome replication is regulated to ensure genome stability. By focusing on the basic biology that underpins cell growth and division we aim to provide new insights that may help our understanding of diseases such as cancer and congenital disorders. </p>

<p>More http://www.nieduszynski.org/index.php<br />http://www.path.ox.ac.uk/research/cell-biology-and-pathology/conrad-nieduszynski-group</p>
]]></description>
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