CORD-19:4ca5d854d3f99440b507fd7dfae73c8ad6fc45d5 / 592540-592839 JSONTXT 3 Projects

Annnotations TAB TSV DIC JSON TextAE

Id Subject Object Predicate Lexical cue
T1017 0-299 Epistemic_statement denotes 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.