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    <!-- 
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    <!-- http://purl.obolibrary.org/obo/RO_0002233 -->

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    <!-- http://purl.obolibrary.org/obo/RO_0002234 -->

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    <!-- http://purl.obolibrary.org/obo/CHEBI_15422 -->

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    <!-- http://purl.obolibrary.org/obo/CHEBI_16761 -->

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    <!-- http://purl.obolibrary.org/obo/HINO_0007310 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/HINO_0007310">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Kinesins:microtubule</rdfs:label>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/HINO_0020180 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/HINO_0020180">
        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Kinesins move along microtubules consuming ATP</rdfs:label>
        <rdfs:subClassOf rdf:resource="http://purl.obolibrary.org/obo/INO_0000040"/>
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        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Authored: Akkerman, JW, 2010-10-29</rdfs:comment>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Edited: Jupe, S, 2010-11-15</rdfs:comment>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Kinesins consume ATP to power the motor which allows them to move along microtubules. The motor region contains highly conserved Switch 1 (SSRSH) and 2 (DLAGSE) motifs which change conformation during ATP hydrolysis (Rice et al. 1999). These form a salt-bridge that, in myosin, closes the nucleotide-binding cleft, enabling the motor to hydrolyze ATP (Geeves &amp; Holmes 1999). This closed conformation has now been seen by cryo-electron microscopy in human conventional kinesin (Sindelar &amp; Downing 2010) and in a crystal structure of the frog kinesin-5 Eg5  (Parke et al. 2010).</rdfs:comment>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed10617199</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed10872464</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed12368902</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed20018897</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed20160108</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed2142332</ns3:IAO_0000119>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed8602245</ns3:IAO_0000119>
        <rdfs:seeAlso rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reactome Database ID Release 43983259</rdfs:seeAlso>
        <ns3:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reactome, http://www.reactome.org</ns3:IAO_0000119>
        <rdfs:seeAlso rdf:datatype="http://www.w3.org/2001/XMLSchema#string">ReactomeREACT_24947</rdfs:seeAlso>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reviewed: Ouwehand, WH, 2010-11-12</rdfs:comment>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/INO_0000040 -->

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