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February 2020

Analysis revealed that in the unbound state, all three variants were characterized by high flexibility, whereas binding to the catalytic (C) subunit of cAPK caused local folding of the N-terminal region of PKI alpha, whereas the segment around Ser59 remained highly flexible when bound to the C-subunit (Hauer et al., 1999), suggesting the fuzzy nature of the resulting PKI alpha-cAPK complex

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Published research has investigated Thymosin 4 in relation to cell migration, actin regulation, angiogenesis and tissue remodelling