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    <!-- http://purl.obolibrary.org/obo/BFO_0000054 -->

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        <rdfs:label xml:lang="en">realized in</rdfs:label>
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        <rdfs:label xml:lang="en">has disposition at some time</rdfs:label>
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        <rdfs:label xml:lang="en">agent_in_compromised_process</rdfs:label>
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    <!-- http://purl.obolibrary.org/obo/IDO_0100754 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/IDO_0100754">
        <rdfs:label>artificially mutated Brucella</rdfs:label>
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        <rdfs:label xml:lang="en">Brucella intracellular growth</rdfs:label>
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    <Class rdf:about="http://purl.obolibrary.org/obo/IDO_0101021">
        <rdfs:label xml:lang="en">Brucella lon mutant</rdfs:label>
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        <rdfs:comment xml:lang="en">MUTATION: In contrast to the parent strain, the Brucella abortus lon mutant, was impaired in its capacity to form isolated colonies on solid medium at 41 degrees C and displayed an increased sensitivity to killing by puromycin and H2O2. Brucella abortus  Lon  homologue functions as a stress response protease that is required for wild-type virulence during the initial stages of infection in the mouse model, but is not essential for the establishment and maintenance of chronic infection in this host [Ref6494:Robertson et al., 2000].  Both single lon or clpA mutations had comparable effects on growth inhibition, suggesting that the concerned proteases Lon and ClpAP both degrade a number of specific proteins, but are also both involved in general degradation of abnormal proteins. Compared to the single mutants, the double  mutant lon clpA was highly sensitive to canavanine. One possible explanation for this observation is that both proteases can substitute for each other to a large extent during bacterial growth. Hence, simultaneous inactivation or decrease in activation of both proteases, either by direct mutation or by elimination of the regulatory component ClpA, strongly increased growth inhibition [Ref6494:Robertson et al., 2000].</rdfs:comment>
        <ns3:IAO_0000232 xml:lang="en">See PMID:10672180</ns3:IAO_0000232>
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