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When unphosphorylated, dematin's two F-actin binding domains move independent of one another permitting them to bind different F-actin filaments.
the headpiece domain of dematin (zeige EPB49 Antikörper) regulates calcium mobilization and signaling in platelets
a novel functional role for dematin (zeige EPB49 Antikörper) in regulating erythrocyte membrane function.
Fast backbone dynamics probed at amide nitrogen versus carbonyl carbon sites for dematin (zeige EPB49 Antikörper) headpiece C-terminal. The reduction of mobility in the loop region upon the S74E mutation can be seen from the (15)N order parameters.
results suggest that phosphorylation of the dematin (zeige EPB49 Antikörper) headpiece acts as a conformational switch within this headpiece domain
a crucial role for this proline residue in structural stability and folding potential of HP (sub)domains consistent with Pro-Trp (zeige TBPL1 Antikörper) stacking as a more general determinant of protein stability
study investigated motions in the backbone of dematin (zeige EPB49 Antikörper) headpiece domain and its mutant DHPS74E using several complementary NMR relaxation techniques
results suggest that the core domain of dematin (zeige EPB49 Antikörper) exhibits properties typical of a natively unfolded protein, while the headpiece domain is folded in a conformation essentially identical to its native structure
Dematin, or EPB49, is an actin-bundling protein originally identified in the erythroid membrane skeleton. Its actin-bundling activity is abolished upon phosphorylation by cAMP-dependent protein kinase and is restored after dephosphorylation (Rana et al., 1993
, dematin actin-binding protein
, erythrocyte membrane protein band 4.9 (dematin)