CORD-19:4ca5d854d3f99440b507fd7dfae73c8ad6fc45d5 / 592540-592839 JSONTXT

Annnotations TAB JSON ListView MergeView

    CORD-19-Sentences

    {"project":"CORD-19-Sentences","denotations":[{"id":"T96921","span":{"begin":0,"end":178},"obj":"Sentence"},{"id":"T83399","span":{"begin":179,"end":299},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"We recently discovered a bacterial PI phosphatase, which is translocated into the host via the Icm/Dot T4SS and preferentially hydrolyses poly-phosphorylated PIs yielding PI(4)P. This PI phosphatase, termed LppA, might shape the LCV PI pattern to promote binding of L. pneumophila effector proteins."}

    Epistemic_Statements

    {"project":"Epistemic_Statements","denotations":[{"id":"T1017","span":{"begin":0,"end":299},"obj":"Epistemic_statement"}],"text":"We recently discovered a bacterial PI phosphatase, which is translocated into the host via the Icm/Dot T4SS and preferentially hydrolyses poly-phosphorylated PIs yielding PI(4)P. This PI phosphatase, termed LppA, might shape the LCV PI pattern to promote binding of L. pneumophila effector proteins."}

    CORD-19_Custom_license_subset

    {"project":"CORD-19_Custom_license_subset","denotations":[{"id":"T138","span":{"begin":0,"end":178},"obj":"Sentence"},{"id":"T139","span":{"begin":179,"end":299},"obj":"Sentence"}],"text":"We recently discovered a bacterial PI phosphatase, which is translocated into the host via the Icm/Dot T4SS and preferentially hydrolyses poly-phosphorylated PIs yielding PI(4)P. This PI phosphatase, termed LppA, might shape the LCV PI pattern to promote binding of L. pneumophila effector proteins."}