Matches in Nanopublications for { <http://www.tkuhn.ch/bel2nanopub/RAAbhkWFjMF8LzNWHpuIpQQyuWBvo1XQCreo_WI3NTelM#_5> ?p ?o ?g. }
Showing items 1 to 2 of
2
with 100 items per page.
- _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 wasQuotedFrom 11342557 provenance.