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	<guid isPermaLink="true">https://bioinformaticsonline.com/pages/view/35386/list-of-visualization-tools-for-network-biology</guid>
	<pubDate>Mon, 29 Jan 2018 05:12:24 -0600</pubDate>
	<link>https://bioinformaticsonline.com/pages/view/35386/list-of-visualization-tools-for-network-biology</link>
	<title><![CDATA[List of visualization tools for network biology]]></title>
	<description><![CDATA[<p>Network analysis&nbsp;is any structured technique used to mathematically analyze a circuit (a &ldquo;network&rdquo; of interconnected components). The&nbsp;<span>Network analysis provides the ability to quantify associations between individuals, which makes it possible to infer details about the network as a whole at the species and/or population level.&nbsp;</span>Few tools published in BMC are listed here https://bmcbioinformatics.biomedcentral.com/articles/sections/networks-analysis.</p><p><img src="https://www.dropbox.com/pri/get/Public/Link%20to%20network.gif?_subject_uid=85115969&amp;raw=1&amp;revision_id=BBqs9eYx7G_faj5J33ExdjmtF8nXK2xrN5dUBsKyTLZQ9RB_hGM-YFmWZMBzbQZfRvjYzfs65HbQYrHRyoikxsQscSFTn1Nud2QeJ8KGfVI5wv4Kzp6froKOmPZu8ZygfKo&amp;size=1280x960&amp;size_mode=3&amp;w=AABQaErsFIz5ZjVZSxXvKaSVUkY5ob1Yjk0x7dghy0X7zw" alt="image" style="border: 0px; border: 0px;"></p><p>Following are the list of standalone applications for network analysis:</p><p>Arena 3D</p><p>3D visualization of multi-layer networks</p><p>http://www.arena3d.org</p><p>Biana</p><p>Data integration and network management</p><p>http://sbi.imim.es/web/BIANA.php</p><p>BioLayout Express 3D&nbsp;</p><p>2D/3D network visualization</p><p>http://www.biolayout.org/</p><p>BiologicalNetworks&nbsp;</p><p>Efficient integrated multi-level analysis of microarray, sequence, regulatory and other data</p><p>http://www.biologicalnetworks.org</p><p>BioMiner</p><p>Modeling, analyzing and visualizing biochemical pathways and networks</p><p>http://www.zbi.uni-saarland.de/chair/projects/BioMiner</p><p>Cell Illustrator&nbsp;</p><p>Petri nets for modeling and simulating biological networks</p><p>http://www.cellillustrator.com</p><p>COPASI</p><p>Analysis of biochemical networks and their dynamics</p><p>http://www.copasi.org/</p><p>Cytoscape&nbsp;</p><p>Network visualization and analysis. Over 200 plugins [60]</p><p>http://www.cytoscape.org/</p><p>Dizzy</p><p>Chemical kinetics stochastic simulation software</p><p>http://magnet.systemsbiology.net/software/Dizzy/</p><p>DyCoNet</p><p>Gephi plugin that can be used to identify dynamic communities in networks</p><p>https://github.com/juliemkauffman/DyCoNet</p><p>GENeVis&nbsp;</p><p>Network and pathway visualization</p><p>http://tinyurl.com/genevis/</p><p>GEPHI&nbsp;</p><p>Interactive visualization and exploration for any network and complex system, dynamic and hierarchical graph.</p><p>https://gephi.org</p><p>Igraph</p><p>Collection of network analysis tools with the emphasis on efficiency, portability and ease of use</p><p>http://igraph.sourceforge.net</p><p>Medusa</p><p>Semantic and multi-edged simple networks</p><p>https://sites.google.com/site/medusa3visualization/</p><p>NAViGaTOR</p><p>Visualizing and analyzing protein-protein interaction networks</p><p>http://tinyurl.com/navigator1/</p><p>N-Browse</p><p>Interactive graphical browser for biological networks</p><p>http://www.gnetbrowse.org/</p><p>NeAT</p><p>Topological and clustering analysis of networks</p><p>http://rsat.ulb.ac.be/neat/</p><p>Ondex&nbsp;</p><p>Data integration and visualization of large networks</p><p>http://www.ondex.org/</p><p>Osprey</p><p>Visualization and annotation of biological networks</p><p>http://biodata.mshri.on.ca/osprey/servlet/Index</p><p>Pajek&nbsp;</p><p>Analysis and visualization of large networks and social network analysis</p><p>http://vlado.fmf.uni-lj.si/pub/networks/pajek/</p><p>PathwayAssist&nbsp;</p><p>Navigation and analysis of biological pathways, gene regulation networks and protein interaction maps.</p><p>http://www.ariadnegenomics.com/downloads/</p><p>PIVOT&nbsp;</p><p>Layout algorithms for visualizing protein interactions and families</p><p>http://acgt.cs.tau.ac.il/pivot/</p><p>ProCope&nbsp;</p><p>Prediction and evaluation of protein complexes from purification data experiments</p><p>http://www.bio.ifi.lmu.de/Complexes/ProCope/</p><p>ProViz&nbsp;</p><p>Visualization and exploration of interaction networks. Gene Ontology and PSI-MI formats supported</p><p>http://cbi.labri.fr/eng/proviz.htm</p><p>SpectralNET&nbsp;</p><p>Network analysis and visualizations. Scatter plots and dimensionality reduction algorithms</p><p>https://www.broadinstitute.org/software/spectralnet</p><p>Tulip&nbsp;</p><p>Enables the development of algorithms, visual encodings, interaction techniques, data models and domain-specific visualizations</p><p>http://tulip.labri.fr/TulipDrupal/</p><p>VANESA&nbsp;</p><p>Automatic reconstruction and analysis of biological networks and Petri nets based on life-science database information</p><p>http://agbi.techfak.uni-bielefeld.de/vanesa/</p><p>VANTED&nbsp;</p><p>Network reconstruction, data visualization, integration of various data types, network simulation</p><p>http://tinyurl.com/vanted/</p><p>yEd</p><p>Creation of diagrams manually and import external data</p><p>http://tinyurl.com/yEdGraph/</p><p>Web tools for network analysis</p><p>APID&nbsp;</p><p>Unified protein-protein interactions from BIND, BioGRID, DIP, HPRD, IntAct and MINT</p><p>http://bioinfow.dep.usal.es/apid/</p><p>Arcadia&nbsp;</p><p>Translates text-based descriptions of biological networks (SBML files) into standardized diagrams (Systems Biology Graphical Notation Process Description maps)</p><p>http://arcadiapathways.sourceforge.net/</p><p>AVIS&nbsp;</p><p>Viewer for signaling networks</p><p>http://actin.pharm.mssm.edu/AVIS2</p><p>bioPIXIE&nbsp;</p><p>Discovery of biological networks from diverse functional genomic data</p><p>http://pixie.princeton.edu/pixie</p><p>CellPublisher</p><p>Interactive representations of biochemical processes</p><p>http://cellpublisher.gobics.de/</p><p>Graphle</p><p>Distributed network exploration and visualization of interactive large, dense graphs</p><p>http://tinyurl.com/graphle/</p><p>GraphWeb&nbsp;</p><p>Web server for graph-based analysis of biological networks</p><p>http://biit.cs.ut.ee/graphweb/</p><p>Hubba</p><p>Web-based service to explore the essential nodes in a network</p><p>http://hub.iis.sinica.edu.tw/Hubba</p><p>NetworkBLAST&nbsp;</p><p>Analysis of protein interaction networks across species to infer protein complexes that are conserved in evolution</p><p>http://www.cs.tau.ac.il/~bnet/networkblast.htm</p><p>Pathview&nbsp;</p><p>Tool set for pathway-based data integration and visualization</p><p>http://Pathview.r-forge.r-project.org/</p><p>PINA&nbsp;</p><p>Integrated platform for protein interaction network construction, filtering, analysis, visualization and management</p><p>http://cbg.garvan.unsw.edu.au/pina/home.do</p><p>ReMatch&nbsp;</p><p>Web-based tool for integration of user-given stoichiometric metabolic models into a database collected from public data sources</p><p>http://www.cs.helsinki.fi/group/sysfys/software/rematch/</p><p>SNOW&nbsp;</p><p>Gene mapping on a reference or human protein-protein interaction network that SNOW hosts</p><p>http://snow.bioinfo.cipf.es</p><p>STITCH&nbsp;</p><p>Resource to explore known and predicted interactions of chemicals and proteins</p><p>http://stitch.embl.de/</p><p>STRING</p><p>Protein interaction networks and integration of data such as genomic context, high-throughput experiments, conserved coexpression and previous knowledge derived from the literature</p><p>http://string-db.org</p><p>TVNViewer&nbsp;</p><p>An interactive visualization tool for exploring networks that change over time or space</p><p>http://www.sailing.cs.cmu.edu/main/?page_id=545</p><p>tYNA&nbsp;</p><p>System for managing, comparing and mining multiple networks</p><p>http://tyna.gersteinlab.org/tyna/</p><p>VisANT&nbsp;</p><p>Visualization, mining, analysis and modeling of biological networks, metabolic networks and ecosystems</p><p>http://visant.bu.edu/</p><p>&nbsp;</p>]]></description>
	<dc:creator>Jit</dc:creator>
</item>

<item>
  <guid isPermaLink='true'>https://bioinformaticsonline.com/opportunity/view/22040/karpagam-university-coimbatore-of-sr-prof-prof-associate-and-assistant-professors-karpagam-university-coimbatore-coimbatore-tamil-nadu</guid>
  <pubDate>Thu, 16 Apr 2015 00:30:45 -0500</pubDate>
  <link></link>
  <title><![CDATA[Karpagam University, Coimbatore, of Sr. Prof, Prof, Associate and Assistant Professors Karpagam University, Coimbatore - Coimbatore, Tamil Nadu]]></title>
  <description><![CDATA[
<p>Karpagam University, Coimbatore, Recruitment of Sr. Prof, Prof, Associate and Assistant Professors</p>

<p>Name of the College: Karpagam University, Coimbatore</p>

<p>Date of official publication: 15th April 2015</p>

<p>The newspaper wherein this job advertised: The Hindu Newspaper</p>

<p>Name of the posts: Senior Professors, Professors, Associate Professors and Assistant Professors</p>

<p>Departments:<br />Bioinformatics<br />Biotechnology<br />Qualifications/Eligibility: The candidates should have qualifications as M.E/M.Tech/M.A/M.Com/MBA/M.Sc/M.Phil/NET/SLET/Ph.D</p>

<p>Job Location: Coimbatore, TN</p>

<p>Salary: As per college norms</p>

<p>How to apply: Interested and eligible candidates are requested to apply online at http://www.karpagamuniversity.edu.in/career</p>

<p>Last date: As soon as possible from 15th April 2015</p>

<p>Reference: The Hindu Newspaper dated 15-04-2015, Coimbatore edition on 14th page</p>
]]></description>
</item>
<item>
	<guid isPermaLink="true">https://bioinformaticsonline.com/blog/view/38238/list-of-motif-discovery-tools</guid>
	<pubDate>Tue, 20 Nov 2018 03:54:26 -0600</pubDate>
	<link>https://bioinformaticsonline.com/blog/view/38238/list-of-motif-discovery-tools</link>
	<title><![CDATA[List of motif discovery tools !]]></title>
	<description><![CDATA[<div><div>In genetics, a sequence motif is a nucleotide or amino-acid sequence pattern that is widespread and has, or is conjectured to have, a biological significance. For proteins, a sequence motif is distinguished from a structural motif, a motif formed by the three-dimensional arrangement of amino acids which may not be adjacent.</div><div>&nbsp;</div><div>Following are the list of tools for motif discovery:</div><div>&nbsp;</div><div><a href="http://genius.embnet.dkfz-heidelberg.de/menu/biounit/open-husar/">2Dsweep -- protein annotation by secondary structure elements</a></div><p>Perform secondary structure predictions on protein sequences.</p></div><div><div><a href="http://floresta.eead.csic.es/3dfootprint/">3D-footprint -- database of DNA-binding protein structures</a></div><p>Find binding specificity information about DNA-protein complexes.</p></div><div><div><a href="http://floresta.eead.csic.es/3dfootprint/">3D-footprint: DNA-binding protein database</a></div><p>Find information about the binding specificity of DNA-binding proteins.</p></div><div><div><a href="http://3d-partner.life.nctu.edu.tw/">3D-partner -- a web server to infer interacting partners and binding models</a></div><p>Predict interacting partners and binding models.</p></div><div><div><a href="http://motif.stanford.edu/distributions/3motif/">3MOTIF -- a protein structure visualization system for conserved sequence motifs</a></div><p>Use this web-based sequence motif visualization system to display sequence motif information in its appropriate three-dimensional (3D) context.</p></div><div><div><a href="http://bioinfo.mpiz-koeln.mpg.de/afawe/">AFAWE -- Automatic functional annotation in a distributed Web Services Environment</a></div><p>Protein function prediction and annotation in an integrated environment powered by web service.</p></div><div><div><a href="http://anchor.enzim.hu/">ANCHOR -- Prediction of Protein Binding Regions in Disordered Proteins</a></div><p>Find information about protein binding.</p></div><div><div><a href="http://annie.bii.a-star.edu.sg/annie/home.do">ANNIE -- ANNotation and Interpretation Environment for Protein Sequences</a></div><p>Use to predict function from de novo protein sequences.</p></div><div><div><a href="http://bioinformatica.isa.cnr.it/ASC/">Active Sequences Collection (ASC) database -- A new tool to assign functions to protein sequences</a></div><p>Search for short active protein sequences with demonstrated biological activities.</p></div><div><div><a href="http://blocks.fhcrc.org/">Blocks -- Ungapped segments in conserved protein sequences</a></div><p>Search for ungapped segments corresponding to the most highly conserved regions of proteins.</p></div><div><div><a href="http://cast.engr.uic.edu/">CASTp -- computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues</a></div><p>Identify and measure surface accessible pockets as well as interior inaccessible cavities, for proteins and other molecules.</p></div><div><div><a href="http://www.ebi.ac.uk/thornton-srv/databases/CSA">CSA -- The Catalytic Site Atlas</a></div><p>To search for catalytic residue annotation for enzymes in the Protein Data Bank.</p></div><div><div><a href="http://www.sbg.bio.ic.ac.uk/~confunc/">ConFunc -- Conserved residue Protein Function Prediction Server</a></div><p>Predict protein function using Gene Ontology.</p></div><div><div><a href="http://consurf.tau.ac.il/">ConSurf-DB -- evolutionary conservation profiles of protein structures database</a></div><p>Automatically calculate evolutionary conservation scores of key amino acid residues and map them on protein structures.</p></div><div><div><a href="http://salilab.org/DBAli/">DBAli -- A Database of Structure Alignments</a></div><p>Mine the protein structure space.</p></div><div><div><a href="http://dilimot.embl.de/">DILIMOT -- discovery of linear motifs in proteins</a></div><p>Predict short linear motifs (3-8 residues) in a set of protein sequences.</p></div><div><div><a href="http://www.ebi.ac.uk/dasty/">Dasty2 -- an Ajax protein DAS client</a></div><p>A web client for visualizing protein sequence feature information using DAS.</p></div><div><div><a href="http://genius.embnet.dkfz-heidelberg.de/menu/biounit/open-husar/">DomainSweep -- protein annotation by domain analysis</a></div><p>Identify the domain architecture within a protein sequence.</p></div><div><div><a href="http://e1ds.csbb.ntu.edu.tw/">E1DS -- catalytic site prediction based on 1D signatures of concurrent conservation</a></div><p>Predict enzyme catalytic site.</p></div><div><div><a href="http://elm.eu.org/">ELM -- Eukarotic Linear Motif Resource</a></div><p>Predict functional sites in eukaryotic proteins.</p></div><div><div><a href="http://us.expasy.org/tools/#proteome">EXPASY Proteome Tools Collection</a></div><p>Use a collection of tools for protein analyses.</p></div><div><div><a href="http://us.expasy.org/tools/findmod/">EXPASY-Findmod</a></div><p>Predict potential protein post-translational modifications and find potential single amino acid substitutions in peptides.</p></div><div><div><a href="http://mbs.cbrc.jp/EzCatDB/">EzCatDB -- the Enzyme Catalytic-mechanism Database</a></div><p>Search for information related to the catalytic mechanisms of enzymes.</p></div><div><div><a href="http://bioinf.cs.ucl.ac.uk/ffpred/">FFPred -- feature-based function prediction</a></div><p>An integrated feature-based function prediction server for vertebrate proteomes.</p></div><div><div><a href="http://www.ebi.ac.uk/printsscan/">FingerPRINT Scan</a></div><p>Identify the closest matching PRINTS sequence motif fingerprints in a protein sequence.</p></div><div><div><a href="http://firedb.bioinfo.cnio.es/">FireDB -- a database of functionally important residues from proteins of known structure</a></div><p>Search for functional annotation of important sites in proteins with known structures.</p></div><div><div><a href="http://bioserv.rpbs.univ-paris-diderot.fr/cgi-bin/Frog2">Frog2 -- a FRee Online druG 3D conformation generator</a></div><p>Produce 3D conformations of small drug compounds.</p></div><div><div><a href="http://www.hgpd.jp/">HGPD -- Human Gene and Protein Database</a></div><p>A database presenting experiment-based results in human proteomics.</p></div><div><div><a href="http://hhsenser.tuebingen.mpg.de/">HHsenser -- exhaustive transitive profile search using HMMx96HMM comparison</a></div><p>Conduct exhaustive intermediate profile searches of a set of homologous protein sequences.</p></div><div><div><a href="http://loschmidt.chemi.muni.cz/hotspotwizard/">HotSpot Wizard -- Substrate Specificity Hot Spot Identification web server</a></div><p>Design protein mutations in site-directed mutagenesis.</p></div><div><div><a href="http://phylogenomics.berkeley.edu/intrepid/">INTREPID -- INformation-theoretic TREe traversal for Protein functional site IDentification</a></div><p>Use for protein functional site identification.</p></div><div><div><a href="http://www.cbs.dtu.dk/">Integrating protein annotation resources through the Distributed Annotation System</a></div><p>Annotate protein using this integrated annotation resource.</p></div><div><div><a href="http://www.ebi.ac.uk/InterProScan/">InterProScan -- protein domains identifier</a></div><p>Identify protein family (and DNA) domains, patterns, motifs, protein families, and functional sites.</p></div><div><div><a href="http://kfc.mitchell-lab.org/">KFC -- Knowledge-based FADE and Contacts</a></div><p>Interactive forecasting of protein interaction hot spots.</p></div><div><div><a href="http://biominer.bime.ntu.edu.tw/magiicpro/">MAGIIC-PRO -- detecting functional signatures by efficient discovery of long patterns in protein sequences</a></div><p>Discover long patterns in protein sequences.</p></div><div><div><a href="http://prodata.swmed.edu/malisam">MALISAM -- Manual ALIgnments for Structurally Analogous Motifs</a></div><p>Database containing pairs of structural analogs and their alignments.</p></div><div><div><a href="http://meme.nbcr.net/">MEME -- discovering and analyzing DNA and protein sequence motifs</a></div><p>Find sequence patterns in DNA and protein sequences.</p></div><div><div><a href="http://www.nii.res.in/modpropep.html">MODPROPEP -- a program for knowledge-based modeling of protein-peptide complexes</a></div><p>A web server for knowledge-based modeling of protein-peptide complexes, specifically peptides in complex with major histocompatibility complex (MHC) proteins and kinases.</p></div><div><div><a href="http://www.bioinfo.tsinghua.edu.cn/~tigerchen/memo.html">MeMo -- a web tool for prediction of protein methylation modifications</a></div><p>Predict protein methylation sites.</p></div><div><div><a href="http://caps.ncbs.res.in/MegaMotifbase/index.html">MegaMotifBase -- a database of structural motifs in protein families and superfamilies</a></div><p>Find structural segments or motifs for protein structures.</p></div><div><div><a href="http://mnm.engr.uconn.edu/MNM/SMSSearchServlet">Minimotif Miner -- a tool for investigating protein function</a></div><p>Find motifs in a protein sequence.</p></div><div><div><a href="http://umber.sbs.man.ac.uk/dbbrowser/motif3d/motif3d.html">Motif3D -- Relating protein sequence motifs to 3D structure</a></div><p>Visualize protein sequence motifs on the 3D protein structures.</p></div><div><div><a href="http://myhits.isb-sib.ch/cgi-bin/motif_scan">MotifScan</a></div><p>Find presence of any known protein motif (Prosite and Pfam) in a protein sequence.</p></div><div><div><a href="http://bioinfo3d.cs.tau.ac.il/MultiBind">MultiBind -- Multiple Alignment of Protein Binding Sites</a></div><p>Recognize spatial chemical binding patterns common to a set of protein structures.</p></div><div><div><a href="http://mendel.imp.univie.ac.at/myristate/SUPLpredictor.htm">NMT -- The MYR Predictor</a></div><p>Analyze proteins for the presence of N-terminal N-myristoylation site.</p></div><div><div><a href="http://www.cbs.dtu.dk/services/NetNGlyc/">NetNGlyc -- N-Glycosylation sites prediction tool</a></div><p>Find the presence of N-Glycosylation sites in human proteins.</p></div><div><div><a href="http://www.cbs.dtu.dk/services/NetOGlyc/">NetOGly 3.1 -- O-glycosylation sites prediction tool</a></div><p>Find the presence of O-GalNAc (mucin type) glycosylation sites in mammalian proteins.</p></div><div><div><a href="http://www.cbs.dtu.dk/services/NetPhos/">NetPhos 2.0 -- Phosphorylation sites predictions</a></div><p>Analyze eukaryotic proteins for the presence of serine, threonine and tyrosine phosphorylation sites.</p></div><div><div><a href="http://www.cbs.dtu.dk/services/NetPhosK/">NetPhosK 1.0 Server -- kinase specific eukaryotic protein phosphorylation sites prediction tool</a></div><p>Find possible kinase specific phosphorylation sites in eukaryotic proteins.</p></div><div><div><a href="http://networkin.info/search.php">NetworKIN -- a resource for exploring cellular phosphorylation networks</a></div><div>&nbsp;</div></div><div><div><a href="http://neuroproteomics.scs.uiuc.edu/neuropred.html">NeuroPred -- a tool to predict cleavage sites in neuropeptide precursors and provide the masses of the resulting peptides</a></div><p>Predict cleavage sites at basic amino acid locations in neuropeptide precursor sequences.</p></div><div><div><a href="http://www.ebi.ac.uk/patentdata/nr/">Non-Redundant Patent Sequences - Patented Sequence Database</a></div><p>Find information about patented nucleotide and protein sequences.</p></div><div><div><a href="http://www.cbs.dtu.dk/databases/OGLYCBASE/">O-GLYCBASE</a></div><p>Search for information about glycoproteins with O-linked and C-linked glycosylation sites.</p></div><div><div><a href="http://www.pandora.cs.huji.ac.il/">PANDORA -- Protein ANnotation Diagram ORiented Analysis</a></div><p>Find information about protein sequence annotations.</p></div><div><div><a href="http://sunserver.cdfd.org.in:8080/protease/PAR_3D/index.html">PAR-3D -- Protein Active site Residue - 3D structural motif</a></div><p>A server to predict protein active site residues.</p></div><div><div><a href="http://wwwmgs.bionet.nsc.ru/mgs/gnw/pdbsite/">PDBSite -- a database of the 3D structure of protein functional sites</a></div><p>Search for structural and functional information on the protein functional sites.</p></div><div><div><a href="http://wwwmgs.bionet.nsc.ru/mgs/systems/fastprot/pdbsitescan.html">PDBSiteScan -- A program for searching for active, binding and posttranslational modification sites in the 3D structures of proteins</a></div><p>Search 3D protein fragments similar in structure to known active, binding and posttranslational modification sites.</p></div><div><div><a href="http://pedant.gsf.de/">PEDANT -- Protein Extraction, Description and ANalysis Tool</a></div><p>Conduct genome wide functional and structural analysis.</p></div><div><div><a href="http://phosida.org/">PHOSIDA -- Phosphorylation site database</a></div><p>Search for phosphorylation data of any protein of interest.</p></div><div><div><a href="http://www.phosphorylation.biochem.vt.edu/">PHOSPHORYLATION SITE DATABASE</a></div><p>Search for information on prokaryotic proteins that undergo serine, threonine, or tyrosine phosphorylation.</p></div><div><div><a href="http://www.jcvi.org/pn-utility/web/smarty_wrapper/about.php">PNU -- Protein Naming Utility</a></div><p>Determine correct names for proteins.</p></div><div><div><a href="http://mbs.cbrc.jp/poodle/poodle-s.html">POODLE-S -- Predicition Of Order and Disorder by machine LEarning</a></div><p>Web application for predicting protein disorder by using physicochemical features and reduced amino acid set of a position-specific scoring matrix.</p></div><div><div><a href="http://gemdock.life.nctu.edu.tw/ppisearch/">PPISearch -- Protein-Protein Interaction Search</a></div><p>Find homologous protein-protein interactions across multiple species.</p></div><div><div><a href="http://www.ebi.ac.uk/ppsearch/">PPSearch</a></div><p>Search your query sequence against PROSITE pattern database for protein motifs.</p></div><div><div><a href="http://pridb.gdcb.iastate.edu/">PRIDB -- Protein-RNA Interface DataBase</a></div><p>Find information about protein-RNA complexes from the Protein Data Bank (PDB).</p></div><div><div><a href="http://umber.sbs.man.ac.uk/dbbrowser/PRINTS/">PRINTS and its automatic supplement, prePRINTS -- A compendium of protein fingerprints</a></div><p>Search for protein fingerprints.</p></div><div><div><a href="http://www.expasy.org/prosite/">PROSITE</a></div><p>Identify protein families and domains for a given protein sequence.</p></div><div><div><a href="http://www.imtech.res.in/raghava/prrdb/">PRRDB -- Pattern Recognition Receptor Database</a></div><p>A comprehensive database of pattern-recognition receptors and their ligands.</p></div><div><div><a href="http://www.arabidopsis.org/cgi-bin/patmatch/nph-patmatch.pl">PatMatch -- a program for finding patterns in peptide and nucleotide sequences</a></div><p>Search for short nucleotide or peptide sequences such as cis-elements in nucleotide sequences or small domains and motifs in protein sequences.</p></div><div><div><a href="http://pepcyber.umn.edu/PPEP/">PepCyber:P~PEP -- a database of human protein protein interactions mediated by phosphoprotein-binding domains</a></div><p>Database specialized in documenting human PPBD-containing proteins and PPBD-mediated interactions.</p></div><div><div><a href="http://us.expasy.org/tools/peptidecutter/">PeptideCutter -- protein cleavage sites prediction tool</a></div><p>Predicts potential protease cleavage sites and sites cleaved by chemicals in a given protein sequence.</p></div><div><div><a href="http://phobius.binf.ku.dk/">Phobius -- A combined transmembrane topology and signal peptide predictor</a></div><p>Predict combined transmembrane topology and signal peptides.</p></div><div><div><a href="http://phospho.elm.eu.org/">Phospho.ELM -- a database of phosphorylation sites</a></div><p>Search for eukaryotic phosphorylation sites.</p></div><div><div><a href="http://www.phospho3d.org/">Phospho3D -- a database of three-dimensional structures of protein phosphorylation sites</a></div><p>Search for 3D structure and functional annotation of phosphorylation sites in proteins.</p></div><div><div><a href="http://www.phosphosite.org/">PhosphoSite -- A bioinformatics resource dedicated to physiological protein phosphorylation.</a></div><p>Search the database of in vivo phosphorylation sites of human and mouse proteins</p></div><div><div><a href="http://pxgrid.med.monash.edu.au/polyq/">PolyQ -- Polyglutamine Database</a></div><p>Find information about polyglutamine (polyQ) repeats.</p></div><div><div><a href="http://www.ebi.ac.uk/pratt/">Pratt Protein motif and pattern discovery</a></div><p>Find the presence of protein motifs and patterns in an amino acid sequence.</p></div><div><div><a href="http://www.predisi.de/">PrediSi -- Prediction of Signal Peptides and their Cleavage Positions</a></div><p>Predict signal peptide sequences and their cleavage positions in bacterial and eukaryotic amino acid sequences.</p></div><div><div><a href="http://www.ebi.ac.uk/thornton-srv/databases/ProFunc/">ProFunc -- a server for predicting protein function from 3D structure</a></div><p>Predict protein functions based on known structures.</p></div><div><div><a href="http://bioinfo41.weizmann.ac.il/promate/promateus.html">ProMateus--an open research approach to protein-binding sites analysis</a></div><p>Predict the location of potential protein-protein binding sites for unbound proteins.</p></div><div><div><a href="http://www.proteus.cs.huji.ac.il/">ProTeus -- identifying signatures in protein termini</a></div><p>Identify short linear signatures in protein termini.</p></div><div><div><a href="http://genius.embnet.dkfz-heidelberg.de/menu/cgi-bin/w2h-open/w2h.open/w2h.startthis?SIMGO=w2h%2ewelcome">ProtSweep -- protein annotation by homology</a></div><p>Analyze and identify newly obtained protein sequences.</p></div><div><div><a href="http://protemot.csbb.ntu.edu.tw/">Protemot -- prediction of protein binding sites with automatically extracted geometrical templates</a></div><p>Predict protein binding sites in a protein sequence based on geometrical analysis of protein tertiary substructures.</p></div><div><div><a href="http://quasimotifinder.tau.ac.il/">QuasiMotiFinder -- protein annotation by searching for evolutionarily conserved motif-like patterns</a></div><p>Search for evolutionarily conserved motif-like patterns in protein sequences.</p></div><div><div><a href="http://bindr.gdcb.iastate.edu/RNABindR">RNABindR -- software for prediction of RNA binding residues in proteins</a></div><p>Web-based server for analyzing and predicting RNA binding sites in proteins.</p></div><div><div><a href="http://caps.ncbs.res.in/scanmot/scanmot.html">SCANMOT -- searching for similar sequences using a simultaneous scan of multiple sequence motifs</a></div><p>Search for similarities between proteins by simultaneous matching of multiple motifs.</p></div><div><div><a href="http://bioinf.fbb.msu.ru/SDPpred/">SDPpred -- A Tool for Prediction of Amino Acid Residues that Determine Differences in Functional Specificity of Homologous Proteins</a></div><p>Predict residues in protein sequences that determine the proteins' functional specificity.</p></div><div><div><a href="http://tamm.mit.edu/SDR/">SDR -- Specificity Determining Residues Database</a></div><p>Predict specificity-determining residues in protein families.</p></div><div><div><a href="http://bioware.ucd.ie/~slimdisc/">SLiMDisc -- Short, Linear Motif Discovery</a></div><p>Find shared motifs in proteins with a common attribute.</p></div><div><div><a href="http://sumosp.biocuckoo.org/">SUMOsp -- a web server for sumoylation site prediction</a></div><p>Conduct in silico sumoylation sites prediction.</p></div><div><div><a href="http://oxytricha.princeton.edu/SWAKK/">SWAKK -- a web server for detecting positive selection in proteins using a sliding window substitution rate analysis</a></div><p>Detect protein sequence section under positive evolution selection.</p></div><div><div><a href="http://www.expasy.org/tools/scanprosite/">ScanProsite</a></div><p>Search for motifs and patterns within protein sequences.</p></div><div><div><a href="http://www.expasy.org/tools/scanprosite/">ScanProsite -- detection of PROSITE signature matches and ProRule-associated functional and structural residues in proteins</a></div><p>Detect patterns, profiles and motifs in a protein sequence.</p></div><div><div><a href="http://scansite.mit.edu/">ScanSite 2.0 -- Proteome-wide prediction of cell signaling interactions using short sequence motifs</a></div><p>Search for motifs within proteins that are likely to be phosphorylated by specific protein kinases or bind to domains such as SH2 domains, 14-3-3 domains or PDZ domains.</p></div><div><div><a href="http://sepresa.bio-x.cn/">SePreSA -- SErver for the PREdiction of populations susceptible to Serious Adverse drug reaction</a></div><p>Find information about populations carrying polymorphisms within protein binding pockets that make them susceptible to serious adverse drug reaction (SADR).</p></div><div><div><a href="http://motif.genome.jp/">Sequence Motif Search</a></div><p>Search the presence of a motif in either amino acid sequence or nucleotide sequence.</p></div><div><div><a href="http://www.csbio.sjtu.edu.cn/bioinf/Signal-3L/">Signal-3L -- A 3-layer approach for predicting signal peptides</a></div><p>Predict signal peptides.</p></div><div><div><a href="http://www.cbs.dtu.dk/services/SignalP/">SignalP -- Machine learning approaches to the prediction of signal peptides, their cleavage sites, and other protein sorting signals</a></div><p>Predict signal peptides and their cleavage sites.</p></div><div><div><a href="http://us.expasy.org/tools/sulfinator/">Sulfinator -- tyrosine sulfation sites prediction tool</a></div><p>Predict the presence of tyrosine sulfation sites in protein sequences</p></div><div><div><a href="http://bioinf-services.charite.de/supersite/">SuperSite -- Ligand Binding Site Database</a></div><p>Look at protein structure from a ligand and binding site perspective.</p></div><div><div><a href="http://www.ch.embnet.org/">Swiss EMBnet node web server</a></div><p>Use a collection of bioinformatics tools at this portal site.</p></div><div><div><a href="http://bioinfo.montp.cnrs.fr/?r=t-reks">T-REKS -- identification of Tandem REpeats in sequences with a K-meanS based algorithm</a></div><p>Find information about tandem repeats in proteins that carry fundamental biological functions and are related to a number of human diseases.</p></div><div><div><a href="http://tmbeta-genome.cbrc.jp/TMFunction/">TMFunction -- The Functional Database of Membrane Proteins</a></div><p>Find information about functional residues in alpha-helical and beta-barrel membrane proteins.</p></div><div><div><a href="http://topdom.enzim.hu/">TOPDOM -- Conservatively Located Domains and Motifs in Transmembrane Proteins</a></div><p>Database of domains and motifs with conservative location in transmembrane proteins.</p></div><div><div><a href="http://motif.stanford.edu/distributions/emotif/">The EMOTIF database</a></div><p>Search for highly conserved and specific protein sequence motifs.</p></div><div><div><a href="http://treedetv2.bioinfo.cnio.es/treedet/index.html">TreeDet -- Predicting Functional Residues in Protein Sequence Alignments</a></div><p>Predict functional sites in protein sequence alignments use different methodologies.</p></div><div><div><a href="http://motif.bmi.ohio-state.edu/ChIPMotifs/">W-ChIPMotifs -- ChIP-based protein Motif discovery web server</a></div><p>Find de novo protein motifs from chromatin immunoprecipitation data.</p></div><div><div><a href="http://feature.stanford.edu/webfeature/">WebFEATURE -- an interactive web tool for identifying and visualizing functional sites on macromolecular structures</a></div><p>Scan query structures for functional sites in both proteins and nucleic acids.</p></div><div><div><a href="http://wwwmgs.bionet.nsc.ru/mgs/programs/panalyst/">WebProAnalyst -- an interactive tool for analysis of quantitative structurex96activity relationships in protein families</a></div><p>Analyze quantitative structure-activity relationship of related protein families.</p></div><div><div><a href="http://motif.stanford.edu/distributions/eblocks/">eBLOCKs -- enumerating conserved protein blocks to achieve maximal sensitivity and specificity</a></div><p>Search for ungapped alignments of highly conserved regions among a protein family or superfamily.</p></div><div><div><a href="http://ef-site.hgc.jp/eF-seek/">eF-seek -- prediction of the functional sites of proteins by searching for similar electrostatic potential and molecular surface shape</a></div><p>Predict the functional sites of proteins.</p></div><div><div><a href="http://firedb.bioinfo.cnio.es/Php/FireStar.php">firestar -- prediction of functionally important residues using structural templates and alignment reliability</a></div><p>An expert system for predicting ligand-binding residues in protein structures.</p></div><div><div><a href="http://caps.ncbs.res.in/imotdb/">iMOTdb -- a comprehensive collection of spatially interacting motifs in proteins</a></div><p>Automatically identify spatially interacting motifs among distantly related proteins sharing similar folds and possessing common ancestral lineage.</p></div>]]></description>
	<dc:creator>Neel</dc:creator>
</item>
<item>
	<guid isPermaLink="true">https://bioinformaticsonline.com/file/view/22053/binc-sample-question-paper</guid>
	<pubDate>Thu, 16 Apr 2015 09:16:18 -0500</pubDate>
	<link>https://bioinformaticsonline.com/file/view/22053/binc-sample-question-paper</link>
	<title><![CDATA[BINC Sample Question Paper !!!]]></title>
	<description><![CDATA[<p>BINC sample question paper. Wish you all the best for BINC examination.</p>]]></description>
	<dc:creator>Jitendra Narayan</dc:creator>
	<enclosure url="https://bioinformaticsonline.com/file/download/22053" length="4041" type="text/plain" />
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	<guid isPermaLink="true">https://bioinformaticsonline.com/blog/view/43260/bioinformatics-tools-for-telomere-to-telomere-assembly</guid>
	<pubDate>Tue, 17 Aug 2021 13:17:09 -0500</pubDate>
	<link>https://bioinformaticsonline.com/blog/view/43260/bioinformatics-tools-for-telomere-to-telomere-assembly</link>
	<title><![CDATA[Bioinformatics tools for telomere to telomere assembly !]]></title>
	<description><![CDATA[<p>●&nbsp;<a href="https://github.com/arangrhie/merfin" target="_blank">Merfin</a>&nbsp;&ndash; k-mer-based assembly and variant calling evaluation for improved consensus accuracy (Arang Rhie)<br />●&nbsp;<a href="https://www.biorxiv.org/content/10.1101/2020.11.11.378133v1" target="_blank">PanGenie</a>&nbsp;&ndash; algorithm that leverages a pangenome reference built from haplotype-resolved genome assemblies in conjunction with k-mer count information from raw, short-read sequencing data to genotype a wide spectrum of genetic variation (Tobias Marschall)<br />●&nbsp;<a href="https://github.com/ConesaLab/SQANTI3" target="_blank">SQANTI3</a>&nbsp;&ndash; an automated pipeline for the classification of long-read transcripts that can assess the quality of data and the preprocessing pipeline (Roc&iacute;o Amor&iacute;n de Heged&uuml;s&nbsp;<a href="https://twitter.com/rocioadh" target="_blank">@rocioadh</a>)<br />●&nbsp;<a href="https://github.com/GenomeRIK/tama" target="_blank">tama</a>&nbsp;(Transcriptome Annotation by Modular Algorithms) &ndash; software designed for processing Iso-Seq data and other long-read transcriptome data (Richard Kuo&nbsp;<a href="https://twitter.com/GenomeRIK" target="_blank">@GenomeRIK</a>)<br />●&nbsp;<a href="https://github.com/PacificBiosciences/pbAA" target="_blank">pbaa</a>&nbsp;(PacBio Amplicon Analysis) &ndash; separates complex mixtures of amplicon targets from genomic samples to cluster and generate high-quality consensus sequences from HiFi reads (Zev Kronenberg&nbsp;<a href="https://twitter.com/zevkronenberg" target="_blank">@zevkronenberg</a>)<br />●&nbsp;<a href="https://github.com/yuanyuan929/bellerophon" target="_blank">bellerophon</a>&nbsp;&ndash; analyzes MHC typing and other low-complexity gene amplicon data; performs allele calling while detecting polymorphic sites within the sequences and removing potential chimeric sequence variants (Yuanyuan Cheng&nbsp;<a href="https://twitter.com/Yuanyuan929" target="_blank">@Yuanyuan929</a>)<br />●&nbsp;<a href="https://github.com/amwenger/svpack" target="_blank">svpack</a>&nbsp;&ndash; tools for filtering, comparing, and annotating structural variant (SV) calls in VCF format (Aaron Wenger)<br />●&nbsp;<a href="https://github.com/AntonBankevich/jumboDB" target="_blank">JumboDB</a>&nbsp;&ndash; tool for de Bruijn graph construction (Anton Bankevich&nbsp;<a href="https://twitter.com/AntonBankevich" target="_blank">@AntonBankevich</a>)<br />●&nbsp;<a href="https://github.com/ksahlin/ultra" target="_blank">uLTRA</a>&nbsp;&ndash; tool for splice alignment of long transcriptomic reads to a genome, guided by a database of exon annotations. (Kristoffer Sahlin&nbsp;<a href="https://twitter.com/krsahlin" target="_blank">@krsahlin</a>)<br />●&nbsp;<a href="https://www.biorxiv.org/content/10.1101/2021.01.25.428044v1.full.pdf" target="_blank">LeafGo</a>&nbsp;&ndash; workflow to rapidly produce high-quality de novo plant genomes (Luca Ermini&nbsp;<a href="https://twitter.com/ermini_luca" target="_blank">@ermini_luca</a>)</p><p>Reference:</p><p>https://www.pacb.com/blog/young-investigators-share-stellar-science-career-advice-and-bioinformatics-tools-at-smrt-leiden-2021/</p><p>&nbsp;</p>]]></description>
	<dc:creator>BioStar</dc:creator>
</item>
<item>
	<guid isPermaLink="true">https://bioinformaticsonline.com/news/view/22133/r-320-is-released</guid>
	<pubDate>Sat, 18 Apr 2015 05:06:44 -0500</pubDate>
	<link>https://bioinformaticsonline.com/news/view/22133/r-320-is-released</link>
	<title><![CDATA[R 3.2.0 is released]]></title>
	<description><![CDATA[<p>R 3.2.0 (codename &ldquo;Full of Ingredients&rdquo;)&nbsp;was <a href="http://r.789695.n4.nabble.com/R-3-2-0-is-released-td4705933.html" target="_blank">released yesterday</a>.&nbsp;You can get the latest binaries version <strong><a href="http://cran.rstudio.com/" target="_blank">from here</a>.</strong>&nbsp;(or the .tar.gz&nbsp;<strong>source</strong> code from <a href="http://cran.r-project.org/src/base/R-3/R-3.2.0.tar.gz" target="_blank">here</a>).&nbsp;The full list of new features and bug fixes is provided below.</p><h3>Upgrading to R 3.2.0 on Windows</h3><p>If you are using <strong>Windows&nbsp;</strong>you can easily upgrade to the latest version of R using <a href="http://cran.r-project.org/web/packages/installr/" target="_blank">the installr package</a>. Simply run the following code:</p><div><table>
<tbody>
<tr id="p612572">
<td id="p61257code2">
<pre><span style="color: #228b22;"># installing/loading the latest installr package:</span>
<span style="color: #0000ff; font-weight: bold;">install.<span>packages</span></span><span style="color: #080;">(</span><span style="color: #ff0000;">"installr"</span><span style="color: #080;">)</span><span style="color: #080;">;</span> <span style="color: #0000ff; font-weight: bold;">library</span><span style="color: #080;">(</span>installr<span style="color: #080;">)</span> <span style="color: #228b22;">#load / install+load installr</span>
&nbsp;
updateR<span style="color: #080;">(</span><span style="color: #080;">)</span> <span style="color: #228b22;"># updating R.</span></pre>
</td>
</tr>
</tbody>
</table></div><p><span>Running &ldquo;updateR()&rdquo; will detect if there is a new R version available, and if so it will download+install it (etc.).</span></p><p><span><strong>If you are an R blogger yourself</strong> you are invited to <a href="http://www.r-bloggers.com/add-your-blog/">add your own R content feed to this site</a> (<strong>Non-English</strong> R bloggers should add themselves- <a href="http://www.r-bloggers.com/lang/add-your-blog">here</a>)</span></p><h4>NEW FEATURES</h4><ul>
<li><code>anyNA()</code> gains a <code>recursive</code> argument.</li>
<li>When <code>x</code> is missing and <code>names</code> is not false (including the default value), <code>Sys.getenv(x, names)</code> returns an object of class <code>"Dlist"</code> and hence prints tidily.</li>
<li>(Windows.) <code>shell()</code> no longer consults the environment variable <span>SHELL</span>: too many systems have been encountered where it was set incorrectly (usually to a path where software was compiled, not where it was installed). <span>R_SHELL</span>, the preferred way to select a non-default shell, can be used instead.</li>
<li>Some unusual arguments to <code>embedFonts()</code> can now be specified as character vectors, and the defaults have been changed accordingly.</li>
<li>Functions in the <code>Summary</code> group duplicate less. (<a href="https://bugs.r-project.org/bugzilla3/show_bug.cgi?id=15798" target="_blank">PR#15798</a>)</li>
<li>(Unix-alikes.) <code>system(cmd, input = )</code> now uses &lsquo;shell-execution-environment&rsquo; redirection, which will be more natural if <code>cmd</code> is not a single command (but requires a POSIX-compliant shell). (Wish of <a href="https://bugs.r-project.org/bugzilla3/show_bug.cgi?id=15508" target="_blank">PR#15508</a>)</li>
<li><code>read.fwf()</code> and <code>read.DIF()</code> gain a <code>fileEncoding</code> argument, for convenience.</li>
<li>Graphics devices can add attributes to their description in <code>.Device</code> and <code>.Devices</code>. Several of those included with <strong>R</strong> use a <code>"filepath"</code> attribute.</li>
<li><code>pmatch()</code> uses hashing in more cases and so is faster at the expense of using more memory. (<a href="https://bugs.r-project.org/bugzilla3/show_bug.cgi?id=15697" target="_blank">PR#15697</a>)</li>
<li><code>pairs()</code> gains new arguments to select sets of variables to be plotted against each other.</li>
<li><code>file.info(, extra_cols = FALSE)</code> allows a minimal set of columns to be computed on Unix-alikes: on some systems without properly-configured caching this can be significantly faster with large file lists.</li>
<li>New function <code>dir.exists()</code> in package <span>base</span> to test efficiently whether one or more paths exist and are directories.</li>
<li><code>dput()</code> and friends gain new controls <span>hexNumeric</span> and <span>digits17</span> which output double and complex quantities as, respectively, binary fractions (exactly, see <code>sprintf("%a")</code>) and as decimals with up to 17 significant digits.</li>
<li><code>save()</code>, <code>saveRDS()</code> and <code>serialize()</code> now support <code>ascii = NA</code> which writes ASCII files using <code>sprintf("%a")</code> for double/complex quantities. This is read-compatible with <code>ascii = TRUE</code> but avoids binary-&gt;decimal-&gt;binary conversions with potential loss of precision. Unfortunately the Windows C runtime&rsquo;s lack of C99 compliance means that the format cannot be read correctly there in <strong>R</strong> before 3.1.2.</li>
<li>The default for <code>formatC(decimal.mark =)</code> has been changed to be <code>getOption("OutDec")</code>; this makes it more consistent with <code>format()</code> and suitable for use in print methods, e.g. those for classes <code>"density"</code>, <code>"ecdf"</code>, <code>"stepfun"</code> and <code>"summary.lm"</code>.
<p><code>getOption("OutDec")</code> is now consulted by the print method for class <code>"kmeans"</code>, by <code>cut()</code>, <code>dendrogram()</code>, <code>plot.ts()</code> and <code>quantile()</code> when constructing labels and for the report from<code>legend(trace = TRUE)</code>.</p>
<p>(In part, wish of <a href="https://bugs.r-project.org/bugzilla3/show_bug.cgi?id=15819" target="_blank">PR#15819</a>.)</p>
</li>
<li><code>printNum()</code> and hence <code>format()</code> and <code>formatC()</code> give a warning if <code>big.mark</code> and <code>decimal.mark</code> are set to the same value (period and comma are not uncommonly used for each, and this is a check that conventions have not got mixed).</li>
<li><code>merge()</code> can create a result which uses long vectors on 64-bit platforms.</li>
<li><code>dget()</code> gains a new argument <code>keep.source</code> which defaults to <code>FALSE</code> for speed (<code>dput()</code> and <code>dget()</code> are most often used for data objects where this can make <code>dget()</code> many times faster).</li>
<li>Packages may now use a file of common macro definitions in their help files, and may import definitions from other packages.</li>
<li>A number of macros have been added in the new &lsquo;<span>share/Rd</span>&rsquo; directory for use in package overview help pages, and <code>promptPackage()</code> now makes use of them.</li>
<li><code>tools::parse_Rd()</code> gains a new <code>permissive</code> argument which converts unrecognized macros into text. This is used by <code>utils:::format.bibentry</code> to allow LaTeX markup to be ignored.</li>
<li><code>options(OutDec =)</code> can now specify a multi-byte character, e.g., <code>options(OutDec = "u00b7")</code> in a UTF-8 locale.</li>
<li><code>is.recursive(x)</code> is no longer true when <code>x</code> is an external pointer, a weak reference or byte code; the first enables <code>all.equal(x, x)</code> when <code>x .</code></li>
<li><code>ls()</code> (aka <code>objects()</code>) and <code>as.list.environment()</code> gain a new argument <code>sorted</code>.</li>
<li>The <code>"source"</code> attribute (which has not been added to functions by <strong>R</strong> since before <strong>R</strong> version 2.14.0) is no longer treated as special.</li>
<li>Function <code>returnValue()</code> has been added to give <code>on.exit()</code> code access to a function&rsquo;s return value for debugging purposes.</li>
<li><code>crossprod(x, y)</code> allows more matrix coercions when <code>x</code> or <code>y</code> are vectors, now equalling <code>t(x) %*% y</code> in these cases (also reported by Radford Neal). Similarly, <code>tcrossprod(x,y)</code> and <code>%*%</code> work in more cases with vector arguments.</li>
<li>Utility function <code>dynGet()</code> useful for detecting cycles, aka infinite recursions.</li>
<li>The byte-code compiler and interpreter include new instructions that allow many scalar subsetting and assignment and scalar arithmetic operations to be handled more efficiently. This can result in significant performance improvements in scalar numerical code.</li>
<li><code>apply(m, 2, identity)</code> is now the same as the matrix <code>m</code> when it has <em>named</em> row names.</li>
<li>A new function <code>debuggingState()</code> has been added, allowing to temporarily turn off debugging.</li>
<li><code>example()</code> gets a new optional argument <code>run.donttest</code> and <code>tools::Rd2ex()</code> a corresponding <code>commentDonttest</code>, with a default such that <code>example(..)</code> in help examples will run <code>donttest</code> code only if used interactively (a change in behaviour).</li>
<li><code>rbind.data.frame()</code> gains an optional argument <code>make.row.names</code>, for potential speedup.</li>
<li>New function <code>extSoftVersion()</code> to report on the versions of third-party software in use in this session. Currently reports versions of <code>zlib</code>, <code>bzlib</code>, the <code>liblzma</code> from <code>xz</code>, PCRE, ICU, TRE and the <code>iconv</code> implementation.
<p>A similar function <code>grSoftVersion()</code> in package <span>grDevices</span> reports on third-party graphics software.</p>
<p>Function <code>tcltk::tclVersion()</code> reports the Tcl/Tk version.</p>
</li>
<li>Calling <code>callGeneric()</code> without arguments now works with primitive generics to some extent.</li>
<li><code>vapply(x, FUN, FUN.VALUE)</code> is more efficient notably for large <code>length(FUN.VALUE)</code>; as extension of <a href="https://bugs.r-project.org/bugzilla3/show_bug.cgi?id=16061" target="_blank">PR#16061</a>.</li>
<li><code>as.table()</code> now allows tables with one or more dimensions of length 0 (such as <code>as.table(integer())</code>).</li>
<li><code>names(x) now clears the names of call and <code>...</code> objects.</code></li>
<li><code>library()</code> will report a warning when an insufficient dependency version is masking a sufficient one later on the library search path.</li>
<li>A new <code>plot()</code> method for class <code>"raster"</code> has been added.</li>
<li>New <code>check_packages_in_dir_changes()</code> function in package <span>tools</span> for conveniently analyzing how changing sources impacts the check results of their reverse dependencies.</li>
<li>Speed-up from Peter Haverty for <code>ls()</code> and <code>methods:::.requirePackage()</code> speeding up package loading. (<a href="https://bugs.r-project.org/bugzilla3/show_bug.cgi?id=16133" target="_blank">PR#16133</a>)</li>
<li>New <code>get0()</code> function, combining <code>exists()</code> and <code>get()</code> in one call, for efficiency.</li>
<li><code>match.call()</code> gains an <code>envir</code> argument for specifying the environment from which to retrieve the <code>...</code> in the call, if any; this environment was wrong (or at least undesirable) when the<code>definition</code> argument was a function.</li>
<li><code>topenv()</code> has been made <code>.Internal()</code> for speedup, based on Peter Haverty&rsquo;s proposal in <a href="https://bugs.r-project.org/bugzilla3/show_bug.cgi?id=16140" target="_blank">PR#16140</a>.</li>
<li><code>getOption()</code> no longer calls <code>options()</code> in the main case.</li>
<li>Optional use of <code>libcurl</code> (version 7.28.0 from Oct 2012 or later) for Internet access:
<ul>
<li><code>capabilities("libcurl")</code> reports if this is available.</li>
<li><code>libcurlVersion()</code> reports the version in use, and other details of the <code>"libcurl"</code> build including which URL schemes it supports.</li>
<li><code>curlGetHeaders()</code> retrieves the headers for <code>http://</code>, <code>https://</code>, <code>ftp://</code> and <code>ftps://</code> URLs: analysis of these headers can provide insights into the &lsquo;existence&rsquo; of a URL (it might for example be permanently redirected) and is so used in <code>R CMD check --as-cran</code>.</li>
<li><code>download.file()</code> has a new optional method <code>"libcurl"</code> which will handle more URL schemes, follow redirections, and allows simultaneous downloads of multiple URLs.</li>
<li><code>url()</code> has a new method <code>"libcurl"</code> which handles more URL schemes and follows redirections. The default method is controlled by a new option <code>url.method</code>, which applies also to the opening of URLs <em>via</em> <code>file()</code> (which happens implicitly in functions such as <code>read.table</code>.)</li>
<li>When <code>file()</code> or <code>url()</code> is invoked with a <code>https://</code> or <code>ftps://</code> URL which the current method cannot handle, it switches to a suitable method if one is available.</li>
</ul>
</li>
<li>(Windows.) The DLLs &lsquo;<span>internet.dll</span>&rsquo; and &lsquo;<span>internet2.dll</span>&rsquo; have been merged. In this version it is safe to switch (repeatedly) between the internal and Windows internet functions within an <strong>R</strong>session.
<p>The Windows internet functions are still selected by flag <span>&ndash;internet2</span> or <code>setInternet2()</code>. This can be overridden for an <code>url()</code> connection <em>via</em> its new <code>method</code> argument.</p>
<p><code>download.file()</code> has new method <code>"wininet"</code>, selected as the default by <span>&ndash;internet2</span> or <code>setInternet2()</code>.</p>
</li>
<li><code>parent.env&lt;-</code> can no longer modify the parent of a locked namespace or namespace imports environment. Contributed by Karl Millar.</li>
<li>New function <code>isLoadedNamespace()</code> for readability and speed.</li>
<li><code>names(env)</code> now returns all the object names of an <code>environment</code> <code>env</code>, equivalently to <code>ls(env, all.names = TRUE, sorted = FALSE)</code> and also to the names of the corresponding list,<code>names(as.list(env, all.names = TRUE))</code>. Note that although <code>names()</code> returns a character vector, the names have no particular ordering.</li>
<li>The memory manager now grows the heap more aggressively. This reduces the number of garbage collections, in particular while data or code are loaded, at the expense of slightly increasing the memory footprint.</li>
<li>New function <code>trimws()</code> for removing leading/trailing whitespace.</li>
<li><code>cbind()</code> and <code>rbind()</code> now consider S4 inheritance during S3 dispatch and also obey <code>deparse.level</code>.</li>
<li><code>cbind()</code> and <code>rbind()</code> will delegate recursively to <code>methods::cbind2</code> (<code>methods::rbind2</code>) when at least one argument is an S4 object and S3 dispatch fails (due to ambiguity).</li>
<li>(Windows.) <code>download.file(quiet = FALSE)</code> now uses text rather than Windows progress bars in non-interactive use.</li>
<li>New function <code>hsearch_db()</code> in package <span>utils</span> for building and retrieving the help search database used by <code>help.search()</code>, along with functions for inspecting the concepts and keywords in the help search database.</li>
<li>New function <code>.getNamespaceInfo()</code>, a no-check version of <code>getNamespaceInfo()</code> mostly for internal speedups.</li>
<li>The help search system now takes <span>keyword</span> entries in Rd files which are not standard keywords (as given in &lsquo;<span>KEYWORDS</span>&rsquo; in the <strong>R</strong> documentation directory) as concepts. For standard keyword entries the corresponding descriptions are additionally taken as concepts.</li>
<li>New <code>lengths()</code> function for getting the lengths of all elements in a list.</li>
<li>New function <code>toTitleCase()</code> in package <span>tools</span>, tailored to package titles.</li>
<li>The matrix methods of <code>cbind()</code> and <code>rbind()</code> allow matrices as inputs which have <em>2^31</em> or more elements. (For <code>cbind()</code>, wish of <a href="https://bugs.r-project.org/bugzilla3/show_bug.cgi?id=16198" target="_blank">PR#16198</a>.)</li>
<li>The default method of <code>image()</code> has an explicit check for a numeric or logical matrix (which was always required).</li>
<li><code>URLencode()</code> will not by default encode further URLs which appear to be already encoded.</li>
<li><code>BIC(mod)</code> and <code>BIC(mod, mod2)</code> now give non-NA numbers for <code>arima()</code> fitted models, as <code>nobs(mod)</code> now gives the number of &ldquo;used&rdquo; observations for such models. This fixes <a href="https://bugs.r-project.org/bugzilla3/show_bug.cgi?id=16198" target="_blank">PR#16198</a>, quite differently than proposed there.</li>
<li>The <code>print()</code> methods for <code>"htest"</code>, <code>"pairwise.htest"</code> and <code>"power.htest"</code> objects now have a <code>digits</code> argument defaulting to (a function of) <code>getOption("digits")</code>, and influencing all printed numbers coherently. Unavoidably, this changes the display of such test results in some cases.</li>
<li>Code completion for namespaces now recognizes all loaded namespaces, rather than only the ones that are also attached.</li>
<li>The code completion mechanism can now be replaced by a user-specified completer function, for (temporary) situations where the usual code completion is inappropriate.</li>
<li><code>unzip()</code> will now warn if it is able to detect truncation when unpacking a file of 4GB or more (related to <a href="https://bugs.r-project.org/bugzilla3/show_bug.cgi?id=16243" target="_blank">PR#16243</a>).</li>
<li><code>methods()</code> reports S4 in addition to S3 methods; output is simplified when the <code>class</code> argument is used. <code>.S3methods()</code> and <code>methods::.S4methods()</code> report S3 and S4 methods separately.</li>
<li>Higher order functions such as the <code>apply</code> functions and <code>Reduce()</code> now force arguments to the functions they apply in order to eliminate undesirable interactions between lazy evaluation and variable capture in closures. This resolves <a href="https://bugs.r-project.org/bugzilla3/show_bug.cgi?id=16093" target="_blank">PR#16093</a>.</li>
</ul><p>More at http://cran.rstudio.com/</p><p>Reference: http://www.r-bloggers.com/r-3-2-0-is-released-using-the-installr-package-to-upgrade-in-windows-os/</p>]]></description>
	<dc:creator>Neel</dc:creator>
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  <guid isPermaLink='true'>https://bioinformaticsonline.com/opportunity/view/22239/jrf-bioinformatics-at-national-institute-of-high-security-animal-diseases-icar</guid>
  <pubDate>Tue, 28 Apr 2015 02:21:15 -0500</pubDate>
  <link></link>
  <title><![CDATA[JRF Bioinformatics at National Institute of High Security Animal Diseases (ICAR)]]></title>
  <description><![CDATA[
<p>F.No. 4-59/2013-NIHSAD Dated: 21st April, 2015</p>

<p>SRF/ JRF job vacancies in National Institute of High Security Animal Diseases (ICAR)</p>

<p>Name of Post : JRF</p>

<p>No. of Post : 01</p>

<p>Qualification : M.V.Sc or M.Tech./M.Sc. (preferably with NET qualification) in one of following disciplines. (Biotechnology/Molecular Biology/Genetics/Microbiology/Bioinformatics or equivalent Life Sciences discipline). Desirable: Working Knowledge in the areas of Recombinant DNA Techniques, Cell Culture, Handling Laboratory Animals, Genomics.</p>

<p>Emolument : Rs.16,000/-</p>

<p>Age Limit : Up to 30 years</p>

<p>Name of Post : Project Assistant</p>

<p>No of Post : 01</p>

<p>Qualifications : First class M.Sc. /B.E/B.Tech. in one of the following disciplines Biotechnology/ Bioinformatics/ Microbiology or equivalent Life Sciences discipline). Desirable : Exposure of working in research environment, Good command over written/spoken English and computer applications.</p>

<p>Emolument : Rs.8000/-</p>

<p>Age Limit : Upto 28 years</p>

<p>Name of Post : Project Assistant</p>

<p>No of Post : 01</p>

<p>Qualification : First class M.Sc. /B.V.Sc. and A.H., B.Tech. /B.E. in Life Sciences and related areas. Desirable: Exposure of working in research environment, Good command over written/type written/spoken English and computer applications. </p>

<p>Emoluments : Rs. 8000/-</p>

<p>Age Limit : Up to 28 years<br />How to apply</p>

<p>Desirous candidates may send their applications by e-mail (techcell@hsadl.nic.in ) followed by post in the prescribed proforma latest by 11/05/2015. Walk-in-Interview will be held at NIHSAD, Kokta Road, Anand Nagar, Bhopal-462022.</p>

<p>http://www.nihsad.nic.in/pdf/Advt.pdf</p>
]]></description>
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  <guid isPermaLink='true'>https://bioinformaticsonline.com/opportunity/view/22285/project-associate-bioinformatics-iit-mandi</guid>
  <pubDate>Wed, 06 May 2015 06:18:47 -0500</pubDate>
  <link></link>
  <title><![CDATA[Project Associate Bioinformatics @ IIT Mandi]]></title>
  <description><![CDATA[
<p>Eligibility : MSc(Bio-Informatics, Bio-Tech), BSc, BE/B.Tech(Bio-Medical /Bio-Technology Engg, CSE)</p>

<p>Location : Kulu</p>

<p>Job Category : Govt Jobs, Research</p>

<p>Last Date : 20 May 2015</p>

<p>Job Type : Full Time</p>

<p>Hiring Process : Walk - In<br />IIT Mandi - Job Details<br />IIT Mandi</p>

<p>Project Associate Bioinformatics Job vacancies in IIT Mandi on purely temporary</p>

<p>Project: “Exploring the Human Microbiome: A hunt for the candidates for Pre- and Pro-biotics.”</p>

<p>Minimum Qualification and Experience: M.Sc. in Bioinformatics OR B.Tech / BE in Bioinformatics OR M. Sc. in Biotechnology / Life sciences or related areas with Diploma or relevant experience in Bioinformatics OR B.Tech in Biotechnology / Computer Science or MCA or B. Sc. in Life Sciences or related areas with PG diploma in Bioinformatics. Candidates with experience in NGS data handling and analysis will be preferred. Tenure: Initially for one year, extendable based upon performance.</p>

<p>No of Posts: 01</p>

<p>Salary: Rs. 12000- 18000/- per month.</p>

<p>How to apply</p>

<p>Interested candidates can come for a Walk-in-Interview on 20th May 2015 starting at 8:30 AM at the Academic Block, Indian Institute of Technology (IIT), Mandi, Vallabh College Campus, Near Bus Stand, Mandi, HP. The candidates should bring along their curriculum vitae (CV) and copies of educational and experience certificates. In case of any queries please contact: Dr. Tulika Prakash Srivastava (Principal Investigator), Indian Institute of Technology Mandi, Near Bus Stand Mandi - 175 001, Himachal Pradesh.</p>

<p>More at</p>

<p>http://www.iitmandi.ac.in/administration/advrt/Walk-in-interview_Ad.pdf</p>
]]></description>
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  <guid isPermaLink='true'>https://bioinformaticsonline.com/opportunity/view/22317/project-associate-bioinformatics-central-food-technological-research-institute-cftri</guid>
  <pubDate>Tue, 19 May 2015 07:01:12 -0500</pubDate>
  <link></link>
  <title><![CDATA[Project Associate Bioinformatics @ Central Food Technological Research Institute (CFTRI)]]></title>
  <description><![CDATA[
<p>Central Food Technological Research Institute (CFTRI)</p>

<p>Project Assistant (Level-II) job position in Central Food Technological Research Institute (CFTRI) on a temporary contractual basis in the research project (GAP 0469) funded by Science &amp; Engineering Research Board (SERB), Government of India, New Delhi tenable at the Lipidomics Centre, CSIR-CFTRI, Mysore, Karnataka</p>

<p>Name of the Position : </p>

<p>Qualification : First class M. Sc. in Biochemistry/Microbiology/Genetics/ Bioinformatics with good academic record and preferably with experience in molecular biology techniques and basic knowledge of molecular biology and biological chemistry</p>

<p>Emoluments : Rs. 12,000/- per month (Consolidated)</p>

<p>Age Limit : The upper age limit for applying shall be 28 years (as on 22-5-2015), which is relaxed for candidates belonging to Scheduled Castes/Schedule Tribes, Women, Persons with Disabilities (PWD) and OBCs as per GoI norms. <br /> <br />How to apply</p>

<p>Eligible candidates may send their complete Bio-data with e-mail address/contact phone number along with attested copies of the necessary certificates through post to Prof. Ram Rajasekharan, Lipidomics Centre, Department of Lipid Science, CSIR-CFTRI, Mysore-570 020, Karnataka (email: ram@cftri.res.in) on or before 22.05.2015</p>

<p>More at http://www.cftri.com/pa_gap0469.html</p>
]]></description>
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  <guid isPermaLink='true'>https://bioinformaticsonline.com/opportunity/view/22430/nrco-vacancies-for-junior-research-fellow-%E2%80%93-pakyong-sikkim</guid>
  <pubDate>Thu, 28 May 2015 19:10:07 -0500</pubDate>
  <link></link>
  <title><![CDATA[NRCO Vacancies For Junior Research Fellow – Pakyong, Sikkim]]></title>
  <description><![CDATA[
<p>Junior Research Fellow<br />Pay Scale:Rs 25,000/-<br />Educational Requirements:MSc (with NET qualification) / M.Tech degree (with or without NET) with minimum 55% marks in Biotechnology/ Bioinformatics/ Molecular Biology or any other related field.<br />Other Qualification:Computer Skills (Linux, Perl, Java, MySQL) with experience in advanced molecular Biology techniques.<br />No of Post: 01<br />How To Apply: Walk-in-Interviews will be held at ICAR-National Research Centre for Orchids,Pakyong 737106, Sikkim for the post of 01 (One) Junior Research Fellow and 01 (One) Project Attendant under Project ‘DBT’s Twinning programme for the NE’ titled “Assessment of chemical and genetic divergence of some fragrant orchids of north-east India for sustainable improvement of community livelihood” as indicated below. The appointment will be on contractual basis and the incumbents shall not have any claim for regular appointment in ICAR.</p>

<p>Details will be available at: http://nrcorchids.nic.in/Employments/Vacancy%20-%20JRF.pdf</p>
]]></description>
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