Pages that link to "Q44127981"

The following pages link to Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge (Q44127981):

Displaying 50 items.

• Arrestins: ubiquitous regulators of cellular signaling pathways (Q21184142) (← links)
• The structural basis of arrestin-mediated regulation of G-protein-coupled receptors (Q24657537) (← links)
• The retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domain (Q24673655) (← links)
• The emerging roles of β-arrestins in fibrotic diseases (Q26783047) (← links)
• Crystal Structure of Arrestin-3 Reveals the Basis of the Difference in Receptor Binding Between Two Non-visual Subtypes (Q27666519) (← links)
• Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide (Q27677473) (← 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)
• Casein kinase 1 controls the activation threshold of an α-arrestin by multisite phosphorylation of the interdomain hinge. (Q30654811) (← links)
• Rhodopsin TM6 can interact with two separate and distinct sites on arrestin: evidence for structural plasticity and multiple docking modes in arrestin-rhodopsin binding (Q33689499) (← links)
• Identification of receptor binding-induced conformational changes in non-visual arrestins (Q33947214) (← links)
• The effect of arrestin conformation on the recruitment of c-Raf1, MEK1, and ERK1/2 activation (Q34103312) (← links)
• Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding (Q34489038) (← links)
• Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin (Q34596638) (← links)
• G-protein-coupled receptor phosphorylation: where, when and by whom (Q34735704) (← links)
• Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins (Q35085144) (← links)
• The new face of active receptor bound arrestin attracts new partners (Q35214608) (← links)
• The functional cycle of visual arrestins in photoreceptor cells (Q35387361) (← links)
• Role of receptor-attached phosphates in binding of visual and non-visual arrestins to G protein-coupled receptors. (Q35841895) (← links)
• Silent scaffolds: inhibition OF c-Jun N-terminal kinase 3 activity in cell by dominant-negative arrestin-3 mutant (Q36003914) (← links)
• Manipulation of very few receptor discriminator residues greatly enhances receptor specificity of non-visual arrestins (Q36215950) (← links)
• Conformation of receptor-bound visual arrestin (Q36389593) (← links)
• Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin (Q36545558) (← links)
• Engineering visual arrestin-1 with special functional characteristics (Q36579557) (← links)
• Cone arrestin binding to JNK3 and Mdm2: conformational preference and localization of interaction sites (Q36726873) (← links)
• Visual and both non-visual arrestins in their "inactive" conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm (Q36726881) (← links)
• Visual arrestin binding to microtubules involves a distinct conformational change (Q36726921) (← links)
• The differential engagement of arrestin surface charges by the various functional forms of the receptor (Q36737719) (← links)
• Arrestin binds to different phosphorylated regions of the thyrotropin-releasing hormone receptor with distinct functional consequences (Q36953762) (← links)
• Regulation of arrestin binding by rhodopsin phosphorylation level (Q37089132) (← links)
• JNK3 enzyme binding to arrestin-3 differentially affects the recruitment of upstream mitogen-activated protein (MAP) kinase kinases (Q37213763) (← links)
• Arrestin-3 binds c-Jun N-terminal kinase 1 (JNK1) and JNK2 and facilitates the activation of these ubiquitous JNK isoforms in cells via scaffolding (Q37415694) (← links)
• The role of arrestin alpha-helix I in receptor binding (Q37456291) (← links)
• Functional map of arrestin-1 at single amino acid resolution (Q37571225) (← links)
• Custom-designed proteins as novel therapeutic tools? The case of arrestins (Q37735949) (← links)
• Beta-arrestins as regulators of signal termination and transduction: How do they determine what to scaffold? (Q37800215) (← links)
• The Cytoplasmic Rhodopsin-Protein Interface: Potential for Drug Discovery (Q37903343) (← links)
• Synthetic biology with surgical precision: targeted reengineering of signaling proteins (Q38016028) (← links)
• Structural determinants of arrestin functions (Q38114211) (← links)
• Extensive shape shifting underlies functional versatility of arrestins (Q38200331) (← links)
• Overview of different mechanisms of arrestin-mediated signaling (Q38274970) (← links)
• Direct binding of visual arrestin to microtubules determines the differential subcellular localization of its splice variants in rod photoreceptors. (Q38338549) (← links)
• The Diverse Roles of Arrestin Scaffolds in G Protein-Coupled Receptor Signaling (Q39381430) (← links)
• Monitoring agonist-promoted conformational changes of beta-arrestin in living cells by intramolecular BRET. (Q40110003) (← links)
• Arrestin mobilizes signaling proteins to the cytoskeleton and redirects their activity. (Q40159254) (← links)
• Structural evidence for the role of polar core residue Arg175 in arrestin activation (Q40383376) (← links)
• Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins (Q40628650) (← links)
• Elucidation of inositol hexaphosphate and heparin interaction sites and conformational changes in arrestin-1 by solution nuclear magnetic resonance. (Q41894869) (← links)
• Arrestin-3 binds the MAP kinase JNK3α2 via multiple sites on both domains. (Q41981772) (← links)
• Differential regulation of endosomal GPCR/β-arrestin complexes and trafficking by MAPK (Q42126128) (← links)
• Ubiquitin Ligase Parkin Promotes Mdm2–Arrestin Interaction but Inhibits Arrestin Ubiquitination (Q42173591) (← links)