Home
About
Overview
Sharing Data
ORCID
Help
History (1)
Crystal structure of the PAC1R extracellular domain unifies a consensus fold for hormone recognition by class B G-protein coupled receptors.
See All Pages
Find People
Find Everything
Login
to edit your profile (add a photo, awards, links to other websites, etc.)
Edit My Profile
My Person List (
0
)
Return to Top
Crystal structure of the PAC1R extracellular domain unifies a consensus fold for hormone recognition by class B G-protein coupled receptors.
Crystal structure of the PAC1R extracellular domain unifies a consensus fold for hormone recognition by class B G-protein coupled receptors. PLoS One. 2011; 6(5):e19682.
View in:
PubMed
subject areas
Consensus Sequence
Consensus Sequence
Crystallography, X-Ray
Crystallography, X-Ray
Cyclic AMP
Cyclic AMP
Extracellular Matrix
Extracellular Matrix
Hormones
Hormones
Humans
Humans
Magnetic Resonance Spectroscopy
Magnetic Resonance Spectroscopy
Pituitary Adenylate Cyclase-Activating Polypeptide
Pituitary Adenylate Cyclase-Activating Polypeptide
Protein Conformation
Protein Conformation
Protein Folding
Protein Folding
Receptors, G-Protein-Coupled
Receptors, G-Protein-Coupled
Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I
Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I
authors with profiles
Augen A Pioszak