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1 , most closely resembling residues 16-181 of protein phosphatase 5.
2 e-dimensional structure of the TPR domain of protein phosphatase 5.
5 ordinated manner to suppress the activity of protein phosphatase 5 and mediate its activation by lipi
6 variety of "target" proteins including MEK1, protein phosphatase 5, and the CDC42-regulated kinase, t
7 larity to the tetratricopeptide repeats from protein phosphatase 5 but has a different overall twist.
8 catalytic domain and the NL of Lck, whereas protein phosphatase 5 demonstrated unique modes of kinas
14 e was identified as the bovine equivalent of protein phosphatase 5 or a closely related homolog by se
15 y, when paired with the deactivation of a GR-protein phosphatase 5 pathway, resulted in sustained GR
16 annel regulation have implicated the Ser/Thr protein phosphatase 5 (PP5) as an effector of Rac1 GTPas
19 ion of the tetratricopeptide repeat (TPR) of protein phosphatase 5 (PP5) increased PPARalpha or PPARb
29 al differentially expressed proteins, namely protein phosphatase 5 (PP5), formyl peptide receptor 2,
30 , ASK1 was found to physically interact with protein phosphatase 5 (PP5), previously identified as a
31 function is exemplified by the TPR domain of protein phosphatase 5 (PP5), which binds to the C termin
32 e show that estrogen increases expression of protein phosphatase 5 (PP5), which mediates the dephosph
34 y dephosphorylated by the chaperone-targeted protein phosphatase 5 (PP5/Ppt1), which does not affect
40 hile the Hsp90 cochaperones p23, FKBP52, and protein phosphatase 5 remained associated with immature
41 overall identity and 60-65% similarity with protein phosphatase 5's (PP5) from different species.
42 The structural basis for lipid activation of protein phosphatase 5 was examined by limited proteolysi
44 hatase 2A (PP2A), protein phosphatase 4, and protein phosphatase 5 were knocked out in Drosophila Sch
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