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

  <description>
    
      A receptor is a molecule found on the surface of the cell. This receptor’s main task is to receive chemical signals from the external environment of the cell. The signals received by the cells “instruct” the cell to perform a specific function—the cell could allow certain molecules to enter or exit the membrane, initiate the process of cell division, or to die. Receptors are basically made up of protein molecules, which are embedded in the plasma membrane (these receptors are called “cell surface receptors”) or in the cytoplasm or nucleus of the cell (these receptors are “nuclear receptors”), to which on or more kinds of signaling molecules can attach themselves to. A molecule that attaches itself to a receptor is then called a ligand, which can be either a peptide or a small molecule (can be a hormone, a neurotransmitter, a pharmaceutical drug, or even a toxin).

There are different receptor types found in the surface of a typical cell, and each f these types us is connected to a very specific biochemical pathway. Each type of receptor will only recognize and bind to specific ligand shapes—the selecting binding of a specific ligand to the corresponding receptor activates or inhibits a certain pathway. 

The binding of ligand and receptor stabilizes a specific receptor conformation, and is associated with the loss or gain or certain protein activities. But there are some antagonistic ligands that simply block the receptors without inducing any kind of response within the cell. Ligands typically induce change in the cellular environment.

When it comes to molecules of pharmaceutical drugs, there are four theories that are used by medical professionals. The first is the occupatin theory, which states: “drug effect is directly proportional to the number of receptors occupied.” There are also the Ariens and Stephenson, rate, and induced fit theories.

This category contains scientific information about cellular receptors, which receive chemical signals from the external environment of the cells.
    
  </description>

  

  
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        <rdf:li rdf:resource="http://triscience.com/Cells/Receptor/structure-of-human-cyclophilin-and-its-binding-site-for-cyclosporin-a-determined-by-x-ray-crystallography-and-nmr-spectroscopy"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Receptor/structure-of-capnoidine-a-phthalide-isoquinoline-alkaloid"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Receptor/structure-function-relationships-in-the-mast-cell-high-affinity-receptor-for-ige-role-of-the-cytoplasmic-domains-and-of-the-beta-subunit"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Receptor/structure-expression-and-t-cell-costimulatory-activity-of-the-murine-homologue-of-the-human-b-lymphocyte-activation-antigen-b7"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Receptor/structure-and-neutrophil-activating-properties-of-a-novel-inflammatory-peptide-ena-78-with-homology-to-interleukin-8"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Receptor/structure-and-functions-of-c3-receptors"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Receptor/structure-and-function-of-non-enzymatically-dissociated-lacrimal-gland-acini"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Receptor/structure-activity-relationships-in-calcitonin-gene-related-peptide-cyclic-amp-response-in-a-preosteoblast-cell-line-ks-4"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Receptor/structure-activity-relationships-for-platelet-activating-factor-paf-and-analogues-reveal-differences-between-paf-receptors-on-platelets-and-macrophages"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Receptor/structure-activity-relationship-of-philanthotoxins-presynaptic-and-postsynaptic-inhibition-of-the-locust-neuromuscular-transmission"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Receptor/structural-requirements-of-the-cytoplasmic-domains-of-the-human-macrophage-fc-gamma-receptor-iia-and-b-cell-fc-gamma-receptor-iib2-for-the-endocytosis-of-immune-complexes"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Receptor/structural-characterization-of-a-new-anticoagulant-fucan-sulfate-from-the-brown-seaweed-ecklonia-kurome"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Receptor/structural-and-functional-studies-on-the-human-hepatic-interleukin-6-receptor-molecular-cloning-and-overexpression-in-hepg2-cells"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Receptor/structural-and-functional-characterization-of-paramecium-dynein-initial-studies"/>
      
      
        <rdf:li rdf:resource="http://triscience.com/Cells/Receptor/striatal-neurons-express-increased-level-of-dopamine-d-2-receptor-mrna-in-response-to-haloperidol-treatment-a-quantitative-in-situ-hybridization-study"/>
      
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  <item rdf:about="http://triscience.com/Cells/Receptor/structure-of-human-cyclophilin-and-its-binding-site-for-cyclosporin-a-determined-by-x-ray-crystallography-and-nmr-spectroscopy">
    <title>Structure of human cyclophilin and its binding site for cyclosporin a determined by x ray crystallography and nmr spectroscopy</title>
    <link>http://triscience.com/Cells/Receptor/structure-of-human-cyclophilin-and-its-binding-site-for-cyclosporin-a-determined-by-x-ray-crystallography-and-nmr-spectroscopy</link>
    <description>The protein cyclophilin is the major intracellular receptor for the immunosuppressive drug cyclosporin A (ref.1). Cyclosporin A acts as an inhibitor of T-cell activation and can prevent graft rejectio...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>activation</dc:subject>
    
    
      <dc:subject>cell</dc:subject>
    
    
      <dc:subject>cyclophilin</dc:subject>
    
    
      <dc:subject>cyclosporin</dc:subject>
    
    
      <dc:subject>drug</dc:subject>
    
    
      <dc:subject>immunosuppressive</dc:subject>
    
    
      <dc:subject>inhibitor</dc:subject>
    
    
      <dc:subject>organ</dc:subject>
    
    
      <dc:subject>protein</dc:subject>
    
    
      <dc:subject>receptor</dc:subject>
    
    <dc:date>2013-05-20T02:15:02Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Receptor/structure-of-capnoidine-a-phthalide-isoquinoline-alkaloid">
    <title>Structure of capnoidine a phthalide isoquinoline alkaloid</title>
    <link>http://triscience.com/Cells/Receptor/structure-of-capnoidine-a-phthalide-isoquinoline-alkaloid</link>
    <description>C20h17no6, Mr = 367.36, orthorhombic, P212121, a = 7.446 (3), b = 13.239 (5), c = 16.634 (5).Ang., V = 1640 (1).Ang.3, Z = 4, Dx = 1.488 Mg m-3,.lambda.(Mo K.alpha.) = 0.7107.Ang.,.mu. = 0.104 mm-1, F...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>17</dc:subject>
    
    <dc:date>2013-05-20T02:15:00Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Receptor/structure-function-relationships-in-the-mast-cell-high-affinity-receptor-for-ige-role-of-the-cytoplasmic-domains-and-of-the-beta-subunit">
    <title>Structure function relationships in the mast cell high affinity receptor for ige role of the cytoplasmic domains and of the beta subunit</title>
    <link>http://triscience.com/Cells/Receptor/structure-function-relationships-in-the-mast-cell-high-affinity-receptor-for-ige-role-of-the-cytoplasmic-domains-and-of-the-beta-subunit</link>
    <description>To define functionally critical regions of the high affinity receptor for IgE (Fc,Ri) we stably transfected P815 cells with mutated cDNAs coding for subunits with truncated cytoplasmic domains (Cd). I...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>biochemical</dc:subject>
    
    
      <dc:subject>cdnas</dc:subject>
    
    
      <dc:subject>cells</dc:subject>
    
    
      <dc:subject>chimeric</dc:subject>
    
    
      <dc:subject>cooh</dc:subject>
    
    
      <dc:subject>coordinately</dc:subject>
    
    
      <dc:subject>cytoplasmic</dc:subject>
    
    
      <dc:subject>endogenously</dc:subject>
    
    
      <dc:subject>fcepsilonri</dc:subject>
    
    
      <dc:subject>fcepsilonrialpha</dc:subject>
    
    
      <dc:subject>fcepsilonris</dc:subject>
    
    
      <dc:subject>fcri</dc:subject>
    
    
      <dc:subject>gamma</dc:subject>
    
    
      <dc:subject>human</dc:subject>
    
    
      <dc:subject>hydrolysis</dc:subject>
    
    
      <dc:subject>mutated</dc:subject>
    
    
      <dc:subject>phosphoinositides</dc:subject>
    
    
      <dc:subject>phosphorylation</dc:subject>
    
    
      <dc:subject>protein</dc:subject>
    
    
      <dc:subject>receptor</dc:subject>
    
    <dc:date>2013-05-20T02:14:53Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Receptor/structure-expression-and-t-cell-costimulatory-activity-of-the-murine-homologue-of-the-human-b-lymphocyte-activation-antigen-b7">
    <title>Structure expression and t cell costimulatory activity of the murine homologue of the human b lymphocyte activation antigen b7</title>
    <link>http://triscience.com/Cells/Receptor/structure-expression-and-t-cell-costimulatory-activity-of-the-murine-homologue-of-the-human-b-lymphocyte-activation-antigen-b7</link>
    <description>Following occupancy of the T cell receptor by antigen, T cell proliferation and lymphokine production are determined by a second costimulatory signal delivered by a ligand expressed on antigen present...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>acid</dc:subject>
    
    
      <dc:subject>activation</dc:subject>
    
    
      <dc:subject>amino</dc:subject>
    
    
      <dc:subject>antigen</dc:subject>
    
    
      <dc:subject>attachmet</dc:subject>
    
    
      <dc:subject>cell</dc:subject>
    
    
      <dc:subject>cells</dc:subject>
    
    
      <dc:subject>cloned</dc:subject>
    
    
      <dc:subject>conserved</dc:subject>
    
    
      <dc:subject>costimulatory</dc:subject>
    
    
      <dc:subject>gamma</dc:subject>
    
    
      <dc:subject>gene</dc:subject>
    
    
      <dc:subject>hematopoietic</dc:subject>
    
    
      <dc:subject>homologue</dc:subject>
    
    
      <dc:subject>human</dc:subject>
    
    
      <dc:subject>ligand</dc:subject>
    
    
      <dc:subject>lymphocytes</dc:subject>
    
    
      <dc:subject>lymphokine</dc:subject>
    
    
      <dc:subject>monocytes</dc:subject>
    
    
      <dc:subject>mrna</dc:subject>
    
    <dc:date>2013-05-20T02:14:52Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Receptor/structure-and-neutrophil-activating-properties-of-a-novel-inflammatory-peptide-ena-78-with-homology-to-interleukin-8">
    <title>Structure and neutrophil activating properties of a novel inflammatory peptide ena 78 with homology to interleukin 8</title>
    <link>http://triscience.com/Cells/Receptor/structure-and-neutrophil-activating-properties-of-a-novel-inflammatory-peptide-ena-78-with-homology-to-interleukin-8</link>
    <description>A new neutrophil-activating peptide, termed Ena-78, was identified in the conditioned media of stimulated human type Ii epthelial cell line A54 In response to stimulation with either interleukin 1.bet...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>acids</dc:subject>
    
    
      <dc:subject>agpaaavlrelrcvclqttqgv</dc:subject>
    
    
      <dc:subject>amino</dc:subject>
    
    
      <dc:subject>calcium</dc:subject>
    
    
      <dc:subject>cell</dc:subject>
    
    
      <dc:subject>chemotaxis</dc:subject>
    
    
      <dc:subject>cysteines</dc:subject>
    
    
      <dc:subject>desensitization</dc:subject>
    
    
      <dc:subject>epthelial</dc:subject>
    
    
      <dc:subject>exocytosis</dc:subject>
    
    
      <dc:subject>groalpha</dc:subject>
    
    
      <dc:subject>grogamma</dc:subject>
    
    
      <dc:subject>human</dc:subject>
    
    
      <dc:subject>interleukin</dc:subject>
    
    
      <dc:subject>molecular</dc:subject>
    
    
      <dc:subject>necrosis</dc:subject>
    
    
      <dc:subject>neutrophil</dc:subject>
    
    
      <dc:subject>neutrophils</dc:subject>
    
    
      <dc:subject>peptide</dc:subject>
    
    
      <dc:subject>peptides</dc:subject>
    
    <dc:date>2013-05-20T02:14:46Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Receptor/structure-and-functions-of-c3-receptors">
    <title>Structure and functions of c3 receptors</title>
    <link>http://triscience.com/Cells/Receptor/structure-and-functions-of-c3-receptors</link>
    <description>Most of the biological effects derived from complement activation depends on interactions between cleavage fragments of complement components and cells bearing specific receptors. This review overview...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>activation</dc:subject>
    
    
      <dc:subject>biological</dc:subject>
    
    
      <dc:subject>cells</dc:subject>
    
    
      <dc:subject>cellular</dc:subject>
    
    
      <dc:subject>cloned</dc:subject>
    
    
      <dc:subject>encoding</dc:subject>
    
    
      <dc:subject>expression</dc:subject>
    
    
      <dc:subject>genes</dc:subject>
    
    
      <dc:subject>glycoproteins</dc:subject>
    
    
      <dc:subject>human</dc:subject>
    
    
      <dc:subject>immune</dc:subject>
    
    
      <dc:subject>molecules</dc:subject>
    
    
      <dc:subject>pathology</dc:subject>
    
    
      <dc:subject>phagocytosis</dc:subject>
    
    
      <dc:subject>receptors</dc:subject>
    
    
      <dc:subject>regulation</dc:subject>
    
    
      <dc:subject>transmembrane</dc:subject>
    
    <dc:date>2013-05-20T02:14:44Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Receptor/structure-and-function-of-non-enzymatically-dissociated-lacrimal-gland-acini">
    <title>Structure and function of non enzymatically dissociated lacrimal gland acini</title>
    <link>http://triscience.com/Cells/Receptor/structure-and-function-of-non-enzymatically-dissociated-lacrimal-gland-acini</link>
    <description>Lacrimal gland acini were isolated utilizing a non-enzymatic dissociation procedure. This method resulted in the rapid isolation of an enriched population of acini from rat lacrimal gland with a compl...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>acinar</dc:subject>
    
    
      <dc:subject>acini</dc:subject>
    
    
      <dc:subject>adrenergic</dc:subject>
    
    
      <dc:subject>alkaline</dc:subject>
    
    
      <dc:subject>biochemistry</dc:subject>
    
    
      <dc:subject>cell</dc:subject>
    
    
      <dc:subject>cells</dc:subject>
    
    
      <dc:subject>cellular</dc:subject>
    
    
      <dc:subject>cholinergic</dc:subject>
    
    
      <dc:subject>enzymatic</dc:subject>
    
    
      <dc:subject>epithelium</dc:subject>
    
    
      <dc:subject>histological</dc:subject>
    
    
      <dc:subject>interlobular</dc:subject>
    
    
      <dc:subject>intralobular</dc:subject>
    
    
      <dc:subject>lacrimal</dc:subject>
    
    
      <dc:subject>myoepithelial</dc:subject>
    
    
      <dc:subject>peroxidase</dc:subject>
    
    
      <dc:subject>phosphatase</dc:subject>
    
    
      <dc:subject>physiologically</dc:subject>
    
    
      <dc:subject>physiology</dc:subject>
    
    <dc:date>2013-05-20T02:14:44Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Receptor/structure-activity-relationships-in-calcitonin-gene-related-peptide-cyclic-amp-response-in-a-preosteoblast-cell-line-ks-4">
    <title>Structure activity relationships in calcitonin gene related peptide cyclic amp response in a preosteoblast cell line ks 4</title>
    <link>http://triscience.com/Cells/Receptor/structure-activity-relationships-in-calcitonin-gene-related-peptide-cyclic-amp-response-in-a-preosteoblast-cell-line-ks-4</link>
    <description>Synthetic analogs of chicken and human Cgrp were used to define structure-function relationships in a murine osteoblast precursor cell line, Ks-4, that exhibits a substantial cyclic Amp response to Cg...</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>analogs</dc:subject>
    
    
      <dc:subject>biologic</dc:subject>
    
    
      <dc:subject>calcitonin</dc:subject>
    
    
      <dc:subject>calcium</dc:subject>
    
    
      <dc:subject>cell</dc:subject>
    
    
      <dc:subject>cells</dc:subject>
    
    
      <dc:subject>cgrp</dc:subject>
    
    
      <dc:subject>cgrps</dc:subject>
    
    
      <dc:subject>chicken</dc:subject>
    
    
      <dc:subject>compounds</dc:subject>
    
    
      <dc:subject>deamino</dc:subject>
    
    
      <dc:subject>disulfide</dc:subject>
    
    
      <dc:subject>equipotent</dc:subject>
    
    
      <dc:subject>human</dc:subject>
    
    
      <dc:subject>hypocalcemic</dc:subject>
    
    
      <dc:subject>liver</dc:subject>
    
    
      <dc:subject>murine</dc:subject>
    
    
      <dc:subject>osteoblast</dc:subject>
    
    <dc:date>2013-05-20T02:14:34Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Receptor/structure-activity-relationships-for-platelet-activating-factor-paf-and-analogues-reveal-differences-between-paf-receptors-on-platelets-and-macrophages">
    <title>Structure activity relationships for platelet activating factor paf and analogues reveal differences between paf receptors on platelets and macrophages</title>
    <link>http://triscience.com/Cells/Receptor/structure-activity-relationships-for-platelet-activating-factor-paf-and-analogues-reveal-differences-between-paf-receptors-on-platelets-and-macrophages</link>
    <description>Analogues of Paf were examined for their potency in stimulating either platelet aggregation or macrophage superoxide anion generation. Modification of either the alkyl side-chain or the acetyl side-ch...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>acetyl</dc:subject>
    
    
      <dc:subject>agonist</dc:subject>
    
    
      <dc:subject>cell</dc:subject>
    
    
      <dc:subject>compound</dc:subject>
    
    
      <dc:subject>compounds</dc:subject>
    
    
      <dc:subject>hexanolamine</dc:subject>
    
    
      <dc:subject>ionic</dc:subject>
    
    
      <dc:subject>macrophage</dc:subject>
    
    
      <dc:subject>macrophages</dc:subject>
    
    
      <dc:subject>rabbit</dc:subject>
    
    
      <dc:subject>receptors</dc:subject>
    
    
      <dc:subject>stimulating</dc:subject>
    
    
      <dc:subject>superoxide</dc:subject>
    
    <dc:date>2013-05-20T02:14:34Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Receptor/structure-activity-relationship-of-philanthotoxins-presynaptic-and-postsynaptic-inhibition-of-the-locust-neuromuscular-transmission">
    <title>Structure activity relationship of philanthotoxins presynaptic and postsynaptic inhibition of the locust neuromuscular transmission</title>
    <link>http://triscience.com/Cells/Receptor/structure-activity-relationship-of-philanthotoxins-presynaptic-and-postsynaptic-inhibition-of-the-locust-neuromuscular-transmission</link>
    <description>Like the natural toxin, synthetic delta-philanthotoxin, now called Ptx-4.3.3 acts as a reversible postsynaptic open ion-channel blocker of the glutamatergic neuromuscular system of the locust. It also...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>blocker</dc:subject>
    
    
      <dc:subject>blockers</dc:subject>
    
    
      <dc:subject>cells</dc:subject>
    
    
      <dc:subject>decay</dc:subject>
    
    
      <dc:subject>dehydroxy</dc:subject>
    
    
      <dc:subject>dephenol</dc:subject>
    
    
      <dc:subject>dideaza</dc:subject>
    
    
      <dc:subject>equipotent</dc:subject>
    
    
      <dc:subject>glial</dc:subject>
    
    
      <dc:subject>glutamate</dc:subject>
    
    
      <dc:subject>glutamatergic</dc:subject>
    
    
      <dc:subject>iontophoretically</dc:subject>
    
    
      <dc:subject>molecule</dc:subject>
    
    
      <dc:subject>natural</dc:subject>
    
    
      <dc:subject>neuromuscular</dc:subject>
    
    
      <dc:subject>philanthotoxin</dc:subject>
    
    
      <dc:subject>polyamine</dc:subject>
    
    
      <dc:subject>postsynaptic</dc:subject>
    
    
      <dc:subject>presynaptic</dc:subject>
    
    
      <dc:subject>receptor</dc:subject>
    
    <dc:date>2013-05-20T02:14:34Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Receptor/structural-requirements-of-the-cytoplasmic-domains-of-the-human-macrophage-fc-gamma-receptor-iia-and-b-cell-fc-gamma-receptor-iib2-for-the-endocytosis-of-immune-complexes">
    <title>Structural requirements of the cytoplasmic domains of the human macrophage fc gamma receptor iia and b cell fc gamma receptor iib2 for the endocytosis of immune complexes</title>
    <link>http://triscience.com/Cells/Receptor/structural-requirements-of-the-cytoplasmic-domains-of-the-human-macrophage-fc-gamma-receptor-iia-and-b-cell-fc-gamma-receptor-iib2-for-the-endocytosis-of-immune-complexes</link>
    <description>Two isotypes of the monocyte/macrophage as well as B cell Fc.gamma. receptor type Ii (FcRIIa and FcRIIb2, respectively) mainly differ in the length (76 vs. 44 amino acids) and amino acid sequence of t...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>acid</dc:subject>
    
    
      <dc:subject>acids</dc:subject>
    
    
      <dc:subject>amino</dc:subject>
    
    
      <dc:subject>carboxyl</dc:subject>
    
    
      <dc:subject>cell</dc:subject>
    
    
      <dc:subject>cells</dc:subject>
    
    
      <dc:subject>chimeric</dc:subject>
    
    
      <dc:subject>cytoplasmic</dc:subject>
    
    
      <dc:subject>endocytosis</dc:subject>
    
    
      <dc:subject>fcgamma</dc:subject>
    
    
      <dc:subject>fcrii</dc:subject>
    
    
      <dc:subject>fcriia</dc:subject>
    
    
      <dc:subject>fcriii</dc:subject>
    
    
      <dc:subject>glycan</dc:subject>
    
    
      <dc:subject>hydrophobic</dc:subject>
    
    
      <dc:subject>immune</dc:subject>
    
    
      <dc:subject>inframe</dc:subject>
    
    
      <dc:subject>inositol</dc:subject>
    
    
      <dc:subject>isotypes</dc:subject>
    
    
      <dc:subject>ligand</dc:subject>
    
    <dc:date>2013-05-20T02:14:28Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Receptor/structural-characterization-of-a-new-anticoagulant-fucan-sulfate-from-the-brown-seaweed-ecklonia-kurome">
    <title>Structural characterization of a new anticoagulant fucan sulfate from the brown seaweed ecklonia kurome</title>
    <link>http://triscience.com/Cells/Receptor/structural-characterization-of-a-new-anticoagulant-fucan-sulfate-from-the-brown-seaweed-ecklonia-kurome</link>
    <description>Methylation analysis of a fucose-containing, sulfated polysaccharide (C-Ii), which was isolated from the brown seaweed Ecklonia kurome and has a potent anticoagulant activity, showed the presence of 3...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>17</dc:subject>
    
    
      <dc:subject>anticoagulant</dc:subject>
    
    
      <dc:subject>branched</dc:subject>
    
    
      <dc:subject>desulfated</dc:subject>
    
    
      <dc:subject>disubstituted</dc:subject>
    
    
      <dc:subject>ecklonia</dc:subject>
    
    
      <dc:subject>fraction</dc:subject>
    
    
      <dc:subject>fractions</dc:subject>
    
    
      <dc:subject>fucan</dc:subject>
    
    
      <dc:subject>fucfuc</dc:subject>
    
    
      <dc:subject>fucofuranosyl</dc:subject>
    
    
      <dc:subject>fucopyranosyl</dc:subject>
    
    
      <dc:subject>fucose</dc:subject>
    
    
      <dc:subject>fucosyl</dc:subject>
    
    
      <dc:subject>fwdarw</dc:subject>
    
    
      <dc:subject>galactopyranosyl</dc:subject>
    
    
      <dc:subject>glycosidic</dc:subject>
    
    
      <dc:subject>iodide</dc:subject>
    
    
      <dc:subject>kurome</dc:subject>
    
    
      <dc:subject>methanolysis</dc:subject>
    
    
      <dc:subject>methylated</dc:subject>
    
    <dc:date>2013-05-20T02:14:16Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Receptor/structural-and-functional-studies-on-the-human-hepatic-interleukin-6-receptor-molecular-cloning-and-overexpression-in-hepg2-cells">
    <title>Structural and functional studies on the human hepatic interleukin 6 receptor molecular cloning and overexpression in hepg2 cells</title>
    <link>http://triscience.com/Cells/Receptor/structural-and-functional-studies-on-the-human-hepatic-interleukin-6-receptor-molecular-cloning-and-overexpression-in-hepg2-cells</link>
    <description>CDNAs coding for the human hepatic interleukin-6 receptor (Il-6-R) have been isolated from a library made from poly(A) Rna of dexmethasone-treated human hepatoma cells (HepG2). We found the hepatic Il...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>antibodies</dc:subject>
    
    
      <dc:subject>antiserum</dc:subject>
    
    
      <dc:subject>cdna</dc:subject>
    
    
      <dc:subject>cdnas</dc:subject>
    
    
      <dc:subject>cells</dc:subject>
    
    
      <dc:subject>cloned</dc:subject>
    
    
      <dc:subject>coes</dc:subject>
    
    
      <dc:subject>coli</dc:subject>
    
    
      <dc:subject>concentrations</dc:subject>
    
    
      <dc:subject>cytoplasmic</dc:subject>
    
    
      <dc:subject>dexmethasone</dc:subject>
    
    
      <dc:subject>escherichia</dc:subject>
    
    
      <dc:subject>fibrinogen</dc:subject>
    
    
      <dc:subject>gamma</dc:subject>
    
    
      <dc:subject>hepatoma</dc:subject>
    
    
      <dc:subject>hepotic</dc:subject>
    
    
      <dc:subject>human</dc:subject>
    
    
      <dc:subject>immunization</dc:subject>
    
    
      <dc:subject>immunoprecipitation</dc:subject>
    
    
      <dc:subject>interleukin</dc:subject>
    
    <dc:date>2013-05-20T02:14:09Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Receptor/structural-and-functional-characterization-of-paramecium-dynein-initial-studies">
    <title>Structural and functional characterization of paramecium dynein initial studies</title>
    <link>http://triscience.com/Cells/Receptor/structural-and-functional-characterization-of-paramecium-dynein-initial-studies</link>
    <description>Dynein arms and isolated dynein from Paramecium tetraurelia ciliary axonemes are comparable in structure, direction of force generation, and microtubule translocation ability to other dyneins. In situ...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>17</dc:subject>
    
    
      <dc:subject>dynein</dc:subject>
    
    <dc:date>2013-05-20T02:14:05Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>


  <item rdf:about="http://triscience.com/Cells/Receptor/striatal-neurons-express-increased-level-of-dopamine-d-2-receptor-mrna-in-response-to-haloperidol-treatment-a-quantitative-in-situ-hybridization-study">
    <title>Striatal neurons express increased level of dopamine d 2 receptor mrna in response to haloperidol treatment a quantitative in situ hybridization study</title>
    <link>http://triscience.com/Cells/Receptor/striatal-neurons-express-increased-level-of-dopamine-d-2-receptor-mrna-in-response-to-haloperidol-treatment-a-quantitative-in-situ-hybridization-study</link>
    <description>In the present study, quantitative in situ hybridization was used to analyse the effect of haloperidol treatment on D2 dopamine receptor gene expression in the rat caudate-putamen nucleus. Variations ...</description>
    
    <dc:publisher>No publisher</dc:publisher>
    <dc:creator>admin</dc:creator>
    <dc:rights></dc:rights>
    
      <dc:subject>autoradiographic</dc:subject>
    
    
      <dc:subject>biological</dc:subject>
    
    
      <dc:subject>caudate</dc:subject>
    
    
      <dc:subject>cells</dc:subject>
    
    
      <dc:subject>cholinergic</dc:subject>
    
    
      <dc:subject>densitometric</dc:subject>
    
    
      <dc:subject>disease</dc:subject>
    
    
      <dc:subject>dopaminoceptive</dc:subject>
    
    
      <dc:subject>drugs</dc:subject>
    
    
      <dc:subject>enkephalinergic</dc:subject>
    
    
      <dc:subject>expression</dc:subject>
    
    
      <dc:subject>gene</dc:subject>
    
    
      <dc:subject>haloperidol</dc:subject>
    
    
      <dc:subject>lead</dc:subject>
    
    
      <dc:subject>macroscopic</dc:subject>
    
    
      <dc:subject>mgkg</dc:subject>
    
    
      <dc:subject>microscopic</dc:subject>
    
    
      <dc:subject>mrna</dc:subject>
    
    
      <dc:subject>neuroleptic</dc:subject>
    
    
      <dc:subject>neuroleptics</dc:subject>
    
    <dc:date>2013-05-20T02:13:53Z</dc:date>
    <dc:type>Doculite</dc:type>
  </item>





</rdf:RDF>
