Matches in Nanopublications for { ?s ?p "HSP22 interacts preferentially with the triple aspartate form of HSP27 as compared with wild-type HSP27. HSP22 is expressed predominantly in muscles. In vitro, HSP22 is phosphorylated by protein kinase C (at residues Ser(14) and Thr(63)) and by p44 mitogen-activated protein kinase It is a new binding partner of HSP27 occurring in muscles, and the HSP27-HSP22 interaction is regulated by phosphorylation of HSP27." ?g. }
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- _5 value "HSP22 interacts preferentially with the triple aspartate form of HSP27 as compared with wild-type HSP27. HSP22 is expressed predominantly in muscles. In vitro, HSP22 is phosphorylated by protein kinase C (at residues Ser(14) and Thr(63)) and by p44 mitogen-activated protein kinase It is a new binding partner of HSP27 occurring in muscles, and the HSP27-HSP22 interaction is regulated by phosphorylation of HSP27." provenance.
- _5 value "HSP22 interacts preferentially with the triple aspartate form of HSP27 as compared with wild-type HSP27. HSP22 is expressed predominantly in muscles. In vitro, HSP22 is phosphorylated by protein kinase C (at residues Ser(14) and Thr(63)) and by p44 mitogen-activated protein kinase It is a new binding partner of HSP27 occurring in muscles, and the HSP27-HSP22 interaction is regulated by phosphorylation of HSP27." provenance.