Pages that link to "Q42524440"
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The following pages link to The solution structure and activation of visual arrestin studied by small-angle X-ray scattering (Q42524440):
Displaying 16 items.
- Structure of an Arrestin2-Clathrin Complex Reveals a Novel Clathrin Binding Domain That Modulates Receptor Trafficking (Q27657193) (← links)
- The active conformation of beta-arrestin1: direct evidence for the phosphate sensor in the N-domain and conformational differences in the active states of beta-arrestins1 and -2 (Q28570207) (← links)
- Analysis of self-associating proteins by singular value decomposition of solution scattering data (Q33315748) (← links)
- Structural NMR of protein oligomers using hybrid methods (Q34579372) (← links)
- Visual arrestin binding to microtubules involves a distinct conformational change (Q36726921) (← links)
- Monomeric rhodopsin is the minimal functional unit required for arrestin binding (Q37360145) (← links)
- Diversity in arrestin function (Q37550019) (← links)
- Role of β-arrestins and arrestin domain-containing proteins in G protein-coupled receptor trafficking (Q37676928) (← links)
- Structure and function of the visual arrestin oligomer (Q38304145) (← links)
- Concentration-dependent tetramerization of bovine visual arrestin (Q40248090) (← links)
- A model for the solution structure of the rod arrestin tetramer (Q40262832) (← links)
- Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins (Q40628650) (← links)
- Self-association of arrestin family members (Q41965656) (← links)
- Dynamics of arrestin-rhodopsin interactions: arrestin and retinal release are directly linked events (Q45182666) (← links)
- Homo- and hetero-oligomerization of beta-arrestins in living cells (Q46731935) (← links)
- Phosphorylated peptide of G protein-coupled receptor induces dimerization in activated arrestin (Q96950729) (← links)