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  <title>Cell Binding</title>
  <link>http://triscience.com</link>

  <description>
    
      Cell adhesion is the term that refers to the binding of a cell to a specific surface, extracellular matrix, or another cell. The cell attaches itself to one of the aforementioned places by using cell adhesion molecules such as integrins, cadherins, and selectins. Proper cellular adhesion plays an important role in maintaining multicellular structure. Signal transduction is a possible result of cellular adhesion, because it can link the cytoplasm of binding cells.

The process of cell adhesion occurs differently in different types of cells. The process typically involves adhesion molecules that are first hydrolyzed by a couple of extracellular enzymes, and because of this, the cellular adhesion process is directly related to protein adsorption. In eukaryotic protozoan organisms, the cells express multiple adhesion molecules to start the process. In human cells, the adhesion molecules are immunoglobulin superfamily members, integrins, cadherins, and selectins, and each of these plays a different role and recognizes different types of ligand. If the cell adhesion process is defective, the problem can usually be traced and attributed to depects in the expression of adhesion molecules.

Cell junctions are the main ingredients that allow cells to adhere. There are four basic types of cell junctions: the anchoring junctions (these transmit stress through attaching to the cytoskeleton and usually of the cell-cell or cell-matrix variety). The occluding junctions (these seal the gaps between the cells to form an impermeable barrier around the binding cells), the channel forming junctions (these link the cytoplasm of the adjacent cells) and the signal relaying junction (these are the synapses in the nervous system).

Cell to cell adhesions in anchoring junctions are often mediated by the cadherins, but cell to matrix adhesions are governed by integrins. Selective cell to cell adhesion, on the other hand, uses homophilic attachment and allows vertebrate cells to assemble into organized tsissues that will then form organs. 

This category contains information about cell binding or adhesion, which is a process that initiates “communication” between different cells.
    
  </description>

  

  
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        <rdf:li rdf:resource="http://triscience.com/Cells/Binding/sequestrin-a-cd36-recognition-protein-on-plasmodium-falciparum-malaria-infected-erythrocytes-identified-by-anti-idiotype-antibodies"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Binding/sequential-proton-nmr-assignments-and-secondary-structure-of-an-igg-binding-domain-from-protein-g"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Binding/sequential-changes-in-muscarinic-acetylcholine-adenosine-a-1-and-calcium-antagonist-binding-sites-in-the-gerbil-hippocampus-following-repeated-brief-ischemia"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Binding/sequencing-of-hla-d-in-responders-and-nonresponders-to-short-ragweed-allergen-amb-a-v"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Binding/sequences-involved-in-the-control-of-adenovirus-l1-alternative-rna-splicing"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Binding/sequence-specific-protein-binding-to-and-activation-of-the-tgf-beta-3-promoter-through-a-repeated-tccc-motif"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Binding/sequence-specific-interaction-of-the-ets1-protein-with-the-long-terminal-repeat-of-the-human-t-lymphotropic-virus-type-i"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Binding/sequence-specific-binding-of-a-c-myc-nuclear-matrix-associated-region-shows-increased-nuclear-matrix-retention-after-leukemic-cell-hl-60-differentiation"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Binding/sequence-requirement-for-peptide-recognition-by-rat-brain-p21r-a-s-protein-farnesyltransferase"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Binding/sequence-of-the-lyc-gene-encoding-the-autolytic-lysozyme-of-clostridium-acetobutylicum-atcc824-comparison-with-other-lytic-enzymes"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Binding/sequence-of-the-clathrin-heavy-chain-from-saccharomyces-cerevisiae-and-requirement-of-the-carboxyl-terminus-for-clathrin-function"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Binding/sequence-dependence-of-protein-isoprenylation"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Binding/sequence-and-structural-analysis-of-surface-protein-antigen-i-ii-spaa-of-streptococcus-sobrinus"/>
      
      
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        <rdf:li rdf:resource="http://triscience.com/Cells/Binding/sequence-analysis-of-the-haemagglutinin-ha-of-influenza-a-h1n1-viruses-present-in-clinical-material-and-comparison-with-the-ha-of-laboratory-derived-virus"/>
      
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  <item rdf:about="http://triscience.com/Cells/Binding/sequestrin-a-cd36-recognition-protein-on-plasmodium-falciparum-malaria-infected-erythrocytes-identified-by-anti-idiotype-antibodies">
    <title>Sequestrin a cd36 recognition protein on plasmodium falciparum malaria infected erythrocytes identified by anti idiotype antibodies</title>
    <link>http://triscience.com/Cells/Binding/sequestrin-a-cd36-recognition-protein-on-plasmodium-falciparum-malaria-infected-erythrocytes-identified-by-anti-idiotype-antibodies</link>
    <description>The Cd36 molecule expressed by human endothelial cells is a receptor for the adhesion of erythrocytes infected with the human malaria parasite Plasmodium falciparum. A Cd36-specific monoclonal antibod...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>anti</dc:subject>
    
    
      <dc:subject>antibodies</dc:subject>
    
    
      <dc:subject>antibody</dc:subject>
    
    
      <dc:subject>antigen</dc:subject>
    
    
      <dc:subject>apprxeq</dc:subject>
    
    
      <dc:subject>binding</dc:subject>
    
    
      <dc:subject>cell</dc:subject>
    
    
      <dc:subject>cells</dc:subject>
    
    
      <dc:subject>competitively</dc:subject>
    
    
      <dc:subject>cytoadherence</dc:subject>
    
    
      <dc:subject>endothelial</dc:subject>
    
    
      <dc:subject>endothelium</dc:subject>
    
    
      <dc:subject>erythrocytes</dc:subject>
    
    
      <dc:subject>falciparum</dc:subject>
    
    
      <dc:subject>human</dc:subject>
    
    
      <dc:subject>hypothesis</dc:subject>
    
    
      <dc:subject>immunofluorescence</dc:subject>
    
    
      <dc:subject>immunoprecipitated</dc:subject>
    
    
      <dc:subject>immunotherapy</dc:subject>
    
    
      <dc:subject>irbc</dc:subject>
    
    <dc:date>2013-05-19T04:14:44Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Binding/sequential-proton-nmr-assignments-and-secondary-structure-of-an-igg-binding-domain-from-protein-g">
    <title>Sequential proton nmr assignments and secondary structure of an igg binding domain from protein g</title>
    <link>http://triscience.com/Cells/Binding/sequential-proton-nmr-assignments-and-secondary-structure-of-an-igg-binding-domain-from-protein-g</link>
    <description>Protein G is a member of a class of cell surface bacterial proteins from Streptococcus that bind IgG with high affinity. A fragment of molecular mass 6988, which retains IgG-binding activity, has been...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>bacterial</dc:subject>
    
    
      <dc:subject>binding</dc:subject>
    
    
      <dc:subject>cell</dc:subject>
    
    
      <dc:subject>helix</dc:subject>
    
    
      <dc:subject>molecular</dc:subject>
    
    
      <dc:subject>noesy</dc:subject>
    
    
      <dc:subject>nuclear</dc:subject>
    
    
      <dc:subject>overhauser</dc:subject>
    
    
      <dc:subject>peptide</dc:subject>
    
    
      <dc:subject>protein</dc:subject>
    
    
      <dc:subject>proteins</dc:subject>
    
    
      <dc:subject>proteolytic</dc:subject>
    
    
      <dc:subject>proton</dc:subject>
    
    
      <dc:subject>solution</dc:subject>
    
    
      <dc:subject>spectra</dc:subject>
    
    
      <dc:subject>spectrum</dc:subject>
    
    
      <dc:subject>streptococcus</dc:subject>
    
    
      <dc:subject>tocsy</dc:subject>
    
    
      <dc:subject>torigoe</dc:subject>
    
    <dc:date>2013-05-19T04:14:42Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Binding/sequential-changes-in-muscarinic-acetylcholine-adenosine-a-1-and-calcium-antagonist-binding-sites-in-the-gerbil-hippocampus-following-repeated-brief-ischemia">
    <title>Sequential changes in muscarinic acetylcholine adenosine a 1 and calcium antagonist binding sites in the gerbil hippocampus following repeated brief ischemia</title>
    <link>http://triscience.com/Cells/Binding/sequential-changes-in-muscarinic-acetylcholine-adenosine-a-1-and-calcium-antagonist-binding-sites-in-the-gerbil-hippocampus-following-repeated-brief-ischemia</link>
    <description>We performed quantitative autoradiography to determine sequential alterations in the binding of muscarinic cholinergic and adenosine A1 receptors and of an L-type calcium channel blocker in the gerbil...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>adenosine</dc:subject>
    
    
      <dc:subject>autoradiography</dc:subject>
    
    
      <dc:subject>benzilate</dc:subject>
    
    
      <dc:subject>binding</dc:subject>
    
    
      <dc:subject>blocker</dc:subject>
    
    
      <dc:subject>calcium</dc:subject>
    
    
      <dc:subject>cells</dc:subject>
    
    
      <dc:subject>cholinergic</dc:subject>
    
    
      <dc:subject>dentate</dc:subject>
    
    
      <dc:subject>gyrus</dc:subject>
    
    
      <dc:subject>hippocampal</dc:subject>
    
    
      <dc:subject>hippocampus</dc:subject>
    
    
      <dc:subject>histopathological</dc:subject>
    
    
      <dc:subject>ischemia</dc:subject>
    
    
      <dc:subject>ischemic</dc:subject>
    
    
      <dc:subject>label</dc:subject>
    
    
      <dc:subject>muscarinic</dc:subject>
    
    
      <dc:subject>neuronal</dc:subject>
    
    
      <dc:subject>produced</dc:subject>
    
    
      <dc:subject>receptor</dc:subject>
    
    <dc:date>2013-05-19T04:14:38Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Binding/sequencing-of-hla-d-in-responders-and-nonresponders-to-short-ragweed-allergen-amb-a-v">
    <title>Sequencing of hla d in responders and nonresponders to short ragweed allergen amb a v</title>
    <link>http://triscience.com/Cells/Binding/sequencing-of-hla-d-in-responders-and-nonresponders-to-short-ragweed-allergen-amb-a-v</link>
    <description>"We investigated the molecular basis for the striking association between Hla-Dr2,Dw2 and human immune responsiveness to the Ambrosia artemisiifolia (short ragweed) pollen allergen Amb a V by sequenci...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>acid</dc:subject>
    
    
      <dc:subject>agretope</dc:subject>
    
    
      <dc:subject>agretopes</dc:subject>
    
    
      <dc:subject>allergen</dc:subject>
    
    
      <dc:subject>amino</dc:subject>
    
    
      <dc:subject>andor</dc:subject>
    
    
      <dc:subject>antibody</dc:subject>
    
    
      <dc:subject>antigen</dc:subject>
    
    
      <dc:subject>aprs</dc:subject>
    
    
      <dc:subject>artemisiifolia</dc:subject>
    
    
      <dc:subject>betai</dc:subject>
    
    
      <dc:subject>binding</dc:subject>
    
    
      <dc:subject>caucasoid</dc:subject>
    
    
      <dc:subject>cell</dc:subject>
    
    
      <dc:subject>dralphabetai</dc:subject>
    
    
      <dc:subject>dralphabetav</dc:subject>
    
    
      <dc:subject>exons</dc:subject>
    
    
      <dc:subject>genes</dc:subject>
    
    
      <dc:subject>haplotypes</dc:subject>
    
    
      <dc:subject>human</dc:subject>
    
    <dc:date>2013-05-19T04:14:36Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Binding/sequences-involved-in-the-control-of-adenovirus-l1-alternative-rna-splicing">
    <title>Sequences involved in the control of adenovirus l1 alternative rna splicing</title>
    <link>http://triscience.com/Cells/Binding/sequences-involved-in-the-control-of-adenovirus-l1-alternative-rna-splicing</link>
    <description>During an adenovirus infection the expression of mRNA from late region L1 is temporally regulated at the level of alternative 3' splice site selection to produce two major mRNAs encoding the 52,55k an...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>adenovirus</dc:subject>
    
    
      <dc:subject>binding</dc:subject>
    
    
      <dc:subject>branch</dc:subject>
    
    
      <dc:subject>cells</dc:subject>
    
    
      <dc:subject>competition</dc:subject>
    
    
      <dc:subject>encoding</dc:subject>
    
    
      <dc:subject>expression</dc:subject>
    
    
      <dc:subject>hela</dc:subject>
    
    
      <dc:subject>iiia</dc:subject>
    
    
      <dc:subject>infection</dc:subject>
    
    
      <dc:subject>mrna</dc:subject>
    
    
      <dc:subject>mrnas</dc:subject>
    
    
      <dc:subject>nuclear</dc:subject>
    
    
      <dc:subject>nucleotide</dc:subject>
    
    
      <dc:subject>polypeptides</dc:subject>
    
    
      <dc:subject>polypyrimidine</dc:subject>
    
    
      <dc:subject>produce</dc:subject>
    
    
      <dc:subject>proteins</dc:subject>
    
    
      <dc:subject>vitro</dc:subject>
    
    <dc:date>2013-05-19T04:14:35Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Binding/sequence-specific-protein-binding-to-and-activation-of-the-tgf-beta-3-promoter-through-a-repeated-tccc-motif">
    <title>Sequence specific protein binding to and activation of the tgf beta 3 promoter through a repeated tccc motif</title>
    <link>http://triscience.com/Cells/Binding/sequence-specific-protein-binding-to-and-activation-of-the-tgf-beta-3-promoter-through-a-repeated-tccc-motif</link>
    <description>We have previously characterized the Tgf-.beta.3 promoter and shown that the activity of this promoter is highly variable in different cell types. Although the promoter contains a proximal cAMP respon...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>binding</dc:subject>
    
    
      <dc:subject>ccctccctccc</dc:subject>
    
    
      <dc:subject>cell</dc:subject>
    
    
      <dc:subject>cells</dc:subject>
    
    
      <dc:subject>cytokine</dc:subject>
    
    
      <dc:subject>expression</dc:subject>
    
    
      <dc:subject>forskolin</dc:subject>
    
    
      <dc:subject>mrna</dc:subject>
    
    
      <dc:subject>mutation</dc:subject>
    
    
      <dc:subject>promoter</dc:subject>
    
    
      <dc:subject>protein</dc:subject>
    
    
      <dc:subject>regulation</dc:subject>
    
    
      <dc:subject>rotein</dc:subject>
    
    
      <dc:subject>sequence</dc:subject>
    
    
      <dc:subject>tccc</dc:subject>
    
    
      <dc:subject>tissue</dc:subject>
    
    
      <dc:subject>transactivate</dc:subject>
    
    
      <dc:subject>trnasactivation</dc:subject>
    
    <dc:date>2013-05-19T04:14:33Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Binding/sequence-specific-interaction-of-the-ets1-protein-with-the-long-terminal-repeat-of-the-human-t-lymphotropic-virus-type-i">
    <title>Sequence specific interaction of the ets1 protein with the long terminal repeat of the human t lymphotropic virus type i</title>
    <link>http://triscience.com/Cells/Binding/sequence-specific-interaction-of-the-ets1-protein-with-the-long-terminal-repeat-of-the-human-t-lymphotropic-virus-type-i</link>
    <description>We recently demonstrated that members of the c-ets proto-oncogene family, Ets1 and Ets2, are sequence-specific transcriptional activators of the human T-lymphotropic virus type I (Htlv-I) long termina...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>binding</dc:subject>
    
    
      <dc:subject>cells</dc:subject>
    
    
      <dc:subject>dnase</dc:subject>
    
    
      <dc:subject>expression</dc:subject>
    
    
      <dc:subject>htlv</dc:subject>
    
    
      <dc:subject>human</dc:subject>
    
    
      <dc:subject>lymphoid</dc:subject>
    
    
      <dc:subject>lymphotropic</dc:subject>
    
    
      <dc:subject>methylation</dc:subject>
    
    
      <dc:subject>mobility</dc:subject>
    
    
      <dc:subject>nucleotide</dc:subject>
    
    
      <dc:subject>oncogene</dc:subject>
    
    
      <dc:subject>oncogenes</dc:subject>
    
    
      <dc:subject>plasmids</dc:subject>
    
    
      <dc:subject>promoter</dc:subject>
    
    
      <dc:subject>protein</dc:subject>
    
    
      <dc:subject>proto</dc:subject>
    
    
      <dc:subject>recombinant</dc:subject>
    
    
      <dc:subject>sequence</dc:subject>
    
    
      <dc:subject>stable</dc:subject>
    
    <dc:date>2013-05-19T04:14:33Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Binding/sequence-specific-binding-of-a-c-myc-nuclear-matrix-associated-region-shows-increased-nuclear-matrix-retention-after-leukemic-cell-hl-60-differentiation">
    <title>Sequence specific binding of a c myc nuclear matrix associated region shows increased nuclear matrix retention after leukemic cell hl 60 differentiation</title>
    <link>http://triscience.com/Cells/Binding/sequence-specific-binding-of-a-c-myc-nuclear-matrix-associated-region-shows-increased-nuclear-matrix-retention-after-leukemic-cell-hl-60-differentiation</link>
    <description>Hl-60 cells, a human promyelocytic leukemia cell line, contain amplified c-myc Dna sequences and mRNA transcripts. These cells can be induced to undergo macrophage differentiation by phorbol esters, w...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>binding</dc:subject>
    
    
      <dc:subject>cell</dc:subject>
    
    
      <dc:subject>cells</dc:subject>
    
    
      <dc:subject>competitor</dc:subject>
    
    
      <dc:subject>copolymers</dc:subject>
    
    
      <dc:subject>dnase</dc:subject>
    
    
      <dc:subject>esters</dc:subject>
    
    
      <dc:subject>expression</dc:subject>
    
    
      <dc:subject>extraction</dc:subject>
    
    
      <dc:subject>gene</dc:subject>
    
    
      <dc:subject>human</dc:subject>
    
    
      <dc:subject>idra</dc:subject>
    
    
      <dc:subject>leukemia</dc:subject>
    
    
      <dc:subject>macrophage</dc:subject>
    
    
      <dc:subject>macrophages</dc:subject>
    
    
      <dc:subject>mitosis</dc:subject>
    
    
      <dc:subject>monocytic</dc:subject>
    
    
      <dc:subject>mrna</dc:subject>
    
    
      <dc:subject>nuclear</dc:subject>
    
    
      <dc:subject>phorbol</dc:subject>
    
    <dc:date>2013-05-19T04:14:32Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Binding/sequence-requirement-for-peptide-recognition-by-rat-brain-p21r-a-s-protein-farnesyltransferase">
    <title>Sequence requirement for peptide recognition by rat brain p21r a s protein farnesyltransferase</title>
    <link>http://triscience.com/Cells/Binding/sequence-requirement-for-peptide-recognition-by-rat-brain-p21r-a-s-protein-farnesyltransferase</link>
    <description>We tested 42 tetrapeptides for their ability to bind to the rat brain p21ras protein farnesyltransferase as estimated by their ability to compete with p21Ha-ras in a farnesyltransfer assay. Peptides w...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>acids</dc:subject>
    
    
      <dc:subject>amino</dc:subject>
    
    
      <dc:subject>animal</dc:subject>
    
    
      <dc:subject>binding</dc:subject>
    
    
      <dc:subject>biotinylated</dc:subject>
    
    
      <dc:subject>brain</dc:subject>
    
    
      <dc:subject>cail</dc:subject>
    
    
      <dc:subject>cell</dc:subject>
    
    
      <dc:subject>cooh</dc:subject>
    
    
      <dc:subject>cysteine</dc:subject>
    
    
      <dc:subject>enzymes</dc:subject>
    
    
      <dc:subject>farnesyl</dc:subject>
    
    
      <dc:subject>farnesylated</dc:subject>
    
    
      <dc:subject>farnesyltransfer</dc:subject>
    
    
      <dc:subject>farnesyltransferase</dc:subject>
    
    
      <dc:subject>gamma</dc:subject>
    
    
      <dc:subject>geranylgeranyl</dc:subject>
    
    
      <dc:subject>geranylgeranylated</dc:subject>
    
    
      <dc:subject>guanine</dc:subject>
    
    
      <dc:subject>heptapeptide</dc:subject>
    
    <dc:date>2013-05-19T04:14:31Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Binding/sequence-of-the-lyc-gene-encoding-the-autolytic-lysozyme-of-clostridium-acetobutylicum-atcc824-comparison-with-other-lytic-enzymes">
    <title>Sequence of the lyc gene encoding the autolytic lysozyme of clostridium acetobutylicum atcc824 comparison with other lytic enzymes</title>
    <link>http://triscience.com/Cells/Binding/sequence-of-the-lyc-gene-encoding-the-autolytic-lysozyme-of-clostridium-acetobutylicum-atcc824-comparison-with-other-lytic-enzymes</link>
    <description>The lyc gene, encoding an autolytic lysozyme from Clostridium acetobutylicum Atcc824, has been cloned. The nucleotide sequence of the lyc gene has been determined and found to encode a protein of 324 ...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>acetobutylicum</dc:subject>
    
    
      <dc:subject>acids</dc:subject>
    
    
      <dc:subject>albus</dc:subject>
    
    
      <dc:subject>amino</dc:subject>
    
    
      <dc:subject>autolytic</dc:subject>
    
    
      <dc:subject>bacteriophage</dc:subject>
    
    
      <dc:subject>bacteriophages</dc:subject>
    
    
      <dc:subject>binding</dc:subject>
    
    
      <dc:subject>bulgaricus</dc:subject>
    
    
      <dc:subject>carboyxpeptidase</dc:subject>
    
    
      <dc:subject>cell</dc:subject>
    
    
      <dc:subject>chalaropsis</dc:subject>
    
    
      <dc:subject>cleavable</dc:subject>
    
    
      <dc:subject>cloned</dc:subject>
    
    
      <dc:subject>clostridial</dc:subject>
    
    
      <dc:subject>clostridium</dc:subject>
    
    
      <dc:subject>encoding</dc:subject>
    
    
      <dc:subject>enzyme</dc:subject>
    
    
      <dc:subject>enzymes</dc:subject>
    
    
      <dc:subject>fungus</dc:subject>
    
    <dc:date>2013-05-19T04:14:30Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Binding/sequence-of-the-clathrin-heavy-chain-from-saccharomyces-cerevisiae-and-requirement-of-the-carboxyl-terminus-for-clathrin-function">
    <title>Sequence of the clathrin heavy chain from saccharomyces cerevisiae and requirement of the carboxyl terminus for clathrin function</title>
    <link>http://triscience.com/Cells/Binding/sequence-of-the-clathrin-heavy-chain-from-saccharomyces-cerevisiae-and-requirement-of-the-carboxyl-terminus-for-clathrin-function</link>
    <description>The sequence of the clathrin heavy chain gene, CHCl, from Saccharomyces cerevisiae is reported. The gene encodes a protein of 1,653 amino acids that is 50% identical to the rat clathrin heavy chain (H...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>acad</dc:subject>
    
    
      <dc:subject>acids</dc:subject>
    
    
      <dc:subject>amino</dc:subject>
    
    
      <dc:subject>binding</dc:subject>
    
    
      <dc:subject>brosius</dc:subject>
    
    
      <dc:subject>cells</dc:subject>
    
    
      <dc:subject>cerevisiae</dc:subject>
    
    
      <dc:subject>chcl</dc:subject>
    
    
      <dc:subject>chow</dc:subject>
    
    
      <dc:subject>clathrin</dc:subject>
    
    
      <dc:subject>coated</dc:subject>
    
    
      <dc:subject>cooh</dc:subject>
    
    
      <dc:subject>gene</dc:subject>
    
    
      <dc:subject>genetic</dc:subject>
    
    
      <dc:subject>globular</dc:subject>
    
    
      <dc:subject>growth</dc:subject>
    
    
      <dc:subject>kirchhausen</dc:subject>
    
    
      <dc:subject>light</dc:subject>
    
    
      <dc:subject>mattaliano</dc:subject>
    
    
      <dc:subject>mutation</dc:subject>
    
    <dc:date>2013-05-19T04:14:29Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Binding/sequence-dependence-of-protein-isoprenylation">
    <title>Sequence dependence of protein isoprenylation</title>
    <link>http://triscience.com/Cells/Binding/sequence-dependence-of-protein-isoprenylation</link>
    <description>Several proteins have been shown to be post-translationally modified on a specific C-terminal cysteine residue by either of two isoprenoid biosynthetic pathway metabolites, farnesyl diphosphate or ger...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>acid</dc:subject>
    
    
      <dc:subject>amino</dc:subject>
    
    
      <dc:subject>binding</dc:subject>
    
    
      <dc:subject>biosynthetic</dc:subject>
    
    
      <dc:subject>brain</dc:subject>
    
    
      <dc:subject>caax</dc:subject>
    
    
      <dc:subject>cell</dc:subject>
    
    
      <dc:subject>cerevisiae</dc:subject>
    
    
      <dc:subject>chimeric</dc:subject>
    
    
      <dc:subject>chromatographically</dc:subject>
    
    
      <dc:subject>cysteine</dc:subject>
    
    
      <dc:subject>cytosolic</dc:subject>
    
    
      <dc:subject>diphosphate</dc:subject>
    
    
      <dc:subject>enzymes</dc:subject>
    
    
      <dc:subject>farnesyl</dc:subject>
    
    
      <dc:subject>farnesylated</dc:subject>
    
    
      <dc:subject>fraction</dc:subject>
    
    
      <dc:subject>ftase</dc:subject>
    
    
      <dc:subject>gamma</dc:subject>
    
    
      <dc:subject>genetic</dc:subject>
    
    <dc:date>2013-05-19T04:14:25Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Binding/sequence-and-structural-analysis-of-surface-protein-antigen-i-ii-spaa-of-streptococcus-sobrinus">
    <title>Sequence and structural analysis of surface protein antigen i ii spaa of streptococcus sobrinus</title>
    <link>http://triscience.com/Cells/Binding/sequence-and-structural-analysis-of-surface-protein-antigen-i-ii-spaa-of-streptococcus-sobrinus</link>
    <description>Streptococcal antigen I/Ii or the surface protein antigen A (SpaA) of Streptococcus sobrinus is an adhesin which mediates binding of the organism to tooth surfaces. The complete sequence of the gene w...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>acid</dc:subject>
    
    
      <dc:subject>adhesin</dc:subject>
    
    
      <dc:subject>adhesins</dc:subject>
    
    
      <dc:subject>amino</dc:subject>
    
    
      <dc:subject>antigen</dc:subject>
    
    
      <dc:subject>binding</dc:subject>
    
    
      <dc:subject>cell</dc:subject>
    
    
      <dc:subject>conserved</dc:subject>
    
    
      <dc:subject>gene</dc:subject>
    
    
      <dc:subject>homology</dc:subject>
    
    
      <dc:subject>hydrophobic</dc:subject>
    
    
      <dc:subject>hydrophobicity</dc:subject>
    
    
      <dc:subject>membrane</dc:subject>
    
    
      <dc:subject>mutans</dc:subject>
    
    
      <dc:subject>posttranslational</dc:subject>
    
    
      <dc:subject>proline</dc:subject>
    
    
      <dc:subject>protein</dc:subject>
    
    
      <dc:subject>residue</dc:subject>
    
    
      <dc:subject>residues</dc:subject>
    
    
      <dc:subject>sanguis</dc:subject>
    
    <dc:date>2013-05-19T04:14:24Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Binding/sequence-analysis-of-the-ryanodine-receptor-possible-association-with-a-12k-fk-506-binding-immunophilin-protein-kinase-c-inhibitor">
    <title>Sequence analysis of the ryanodine receptor possible association with a 12k fk 506 binding immunophilin protein kinase c inhibitor</title>
    <link>http://triscience.com/Cells/Binding/sequence-analysis-of-the-ryanodine-receptor-possible-association-with-a-12k-fk-506-binding-immunophilin-protein-kinase-c-inhibitor</link>
    <description>"A computer-assisted sequence analysis of the ryanodine receptor pointed to a 15-residue peptide, ""kc7"", reported to have been purified from a proteolytic digest of the 565 kDa rabbit skeletal muscl...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>binding</dc:subject>
    
    
      <dc:subject>calcium</dc:subject>
    
    
      <dc:subject>cell</dc:subject>
    
    
      <dc:subject>copurified</dc:subject>
    
    
      <dc:subject>fkbp</dc:subject>
    
    
      <dc:subject>human</dc:subject>
    
    
      <dc:subject>immunophilin</dc:subject>
    
    
      <dc:subject>immunosuppressant</dc:subject>
    
    
      <dc:subject>inhibitor</dc:subject>
    
    
      <dc:subject>kinase</dc:subject>
    
    
      <dc:subject>muscle</dc:subject>
    
    
      <dc:subject>peptide</dc:subject>
    
    
      <dc:subject>protein</dc:subject>
    
    
      <dc:subject>proteolytic</dc:subject>
    
    
      <dc:subject>purified</dc:subject>
    
    
      <dc:subject>rabbit</dc:subject>
    
    
      <dc:subject>receptor</dc:subject>
    
    
      <dc:subject>residue</dc:subject>
    
    
      <dc:subject>ryanodine</dc:subject>
    
    
      <dc:subject>sequence</dc:subject>
    
    <dc:date>2013-05-19T04:14:22Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Binding/sequence-analysis-of-the-haemagglutinin-ha-of-influenza-a-h1n1-viruses-present-in-clinical-material-and-comparison-with-the-ha-of-laboratory-derived-virus">
    <title>Sequence analysis of the haemagglutinin ha of influenza a h1n1 viruses present in clinical material and comparison with the ha of laboratory derived virus</title>
    <link>http://triscience.com/Cells/Binding/sequence-analysis-of-the-haemagglutinin-ha-of-influenza-a-h1n1-viruses-present-in-clinical-material-and-comparison-with-the-ha-of-laboratory-derived-virus</link>
    <description>We used the polymerase chain reaction in amplify the Ha1 coding region of influenza A (H1n1) viruses present in clinical material from recent cases of influenza in the U.K. Previously, we have demonst...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>acid</dc:subject>
    
    
      <dc:subject>amino</dc:subject>
    
    
      <dc:subject>antigenically</dc:subject>
    
    
      <dc:subject>binding</dc:subject>
    
    
      <dc:subject>byvirus</dc:subject>
    
    
      <dc:subject>cells</dc:subject>
    
    
      <dc:subject>clinical</dc:subject>
    
    
      <dc:subject>cloned</dc:subject>
    
    
      <dc:subject>clones</dc:subject>
    
    
      <dc:subject>disease</dc:subject>
    
    
      <dc:subject>eggs</dc:subject>
    
    
      <dc:subject>embryonated</dc:subject>
    
    
      <dc:subject>haemagglutinin</dc:subject>
    
    
      <dc:subject>homogeneous</dc:subject>
    
    
      <dc:subject>human</dc:subject>
    
    
      <dc:subject>influenza</dc:subject>
    
    
      <dc:subject>mammalian</dc:subject>
    
    
      <dc:subject>mdck</dc:subject>
    
    
      <dc:subject>natural</dc:subject>
    
    
      <dc:subject>naturally</dc:subject>
    
    <dc:date>2013-05-19T04:14:21Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>





</rdf:RDF>
