Two basic residues of the h-VPAC1 receptor second transmembrane helix are essential for ligand binding and signal transduction.
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Solution structure and mutational analysis of pituitary adenylate cyclase-activating polypeptide binding to the extracellular domain of PAC1-RSStructure of the human glucagon class B G-protein-coupled receptorA Hydrogen-Bonded Polar Network in the Core of the Glucagon-Like Peptide-1 Receptor Is a Fulcrum for Biased Agonism: Lessons from Class B Crystal StructuresTransmembrane signal transduction by peptide hormones via family B G protein-coupled receptorsVPAC receptors for VIP and PACAPStructural Determinants of Binding the Seven-transmembrane Domain of the Glucagon-like Peptide-1 Receptor (GLP-1R)Mutational analysis of the human vasoactive intestinal peptide receptor subtype VPAC(2): role of basic residues in the second transmembrane helixDeamidation affects structural and functional properties of human alphaA-crystallin and its oligomerization with alphaB-crystallin.The serendipitous origin of chordate secretin peptide family members.The vasoactive intestinal peptide (VIP) alpha-Helix up to C terminus interacts with the N-terminal ectodomain of the human VIP/Pituitary adenylate cyclase-activating peptide 1 receptor: photoaffinity, molecular modeling, and dynamicsStructural study of an active analog of EX-4 in solution and micelle associated states.Insights into the structure of class B GPCRs.Ligand binding and activation of the secretin receptor, a prototypic family B G protein-coupled receptor.Calcitonin and calcitonin receptor-like receptors: common themes with family B GPCRs?The VPAC1 receptor: structure and function of a class B GPCR prototype.Mapping spatial approximations between the amino terminus of secretin and each of the extracellular loops of its receptor using cysteine trapping.Use of Cysteine Trapping to Map Spatial Approximations between Residues Contributing to the Helix N-capping Motif of Secretin and Distinct Residues within Each of the Extracellular Loops of Its Receptor.Structural and functional insights into the juxtamembranous amino-terminal tail and extracellular loop regions of class B GPCRs.Conformational switches in the VPAC(1) receptor.Expression and localization of VPAC1, the major receptor of vasoactive intestinal peptide along the length of the intestine.The peptide agonist-binding site of the glucagon-like peptide-1 (GLP-1) receptor based on site-directed mutagenesis and knowledge-based modelling.Different domains of the glucagon and glucagon-like peptide-1 receptors provide the critical determinants of ligand selectivityEvidence for a direct interaction between the Thr11 residue of vasoactive intestinal polypeptide and Tyr184 located in the first extracellular loop of the VPAC2 receptor.High affinity binding of the peptide agonist TIP-39 to the parathyroid hormone 2 (PTH2) receptor requires the hydroxyl group of Tyr-318 on transmembrane helix 5.Two tyrosine residues in the first transmembrane helix of the human vasoactive intestinal peptide receptors play a role in supporting the active conformation.Residues within the transmembrane domain of the glucagon-like peptide-1 receptor involved in ligand binding and receptor activation: modelling the ligand-bound receptor.Mutational analysis of the glucagon receptor: similarities with the vasoactive intestinal peptide (VIP)/pituitary adenylate cyclase-activating peptide (PACAP)/secretin receptors for recognition of the ligand's third residue.Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin toward beta LOW- and individual gamma-crystallins.Functional analysis of a small heat shock/alpha-crystallin protein from Artemia franciscana. Oligomerization and thermotolerance.
P2860
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P2860
Two basic residues of the h-VPAC1 receptor second transmembrane helix are essential for ligand binding and signal transduction.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
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2001年学术文章
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2001年学术文章
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2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
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2001年學術文章
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name
Two basic residues of the h-VP ...... nding and signal transduction.
@en
Two basic residues of the h-VP ...... nding and signal transduction.
@nl
type
label
Two basic residues of the h-VP ...... nding and signal transduction.
@en
Two basic residues of the h-VP ...... nding and signal transduction.
@nl
prefLabel
Two basic residues of the h-VP ...... nding and signal transduction.
@en
Two basic residues of the h-VP ...... nding and signal transduction.
@nl
P2093
P2860
P356
P1476
Two basic residues of the h-VP ...... nding and signal transduction.
@en
P2093
Juarranz MG
Robberecht P
Vertongen P
Waelbroeck M
P2860
P304
P356
10.1074/JBC.M007686200
P407
P577
2001-01-01T00:00:00Z