Results 311 to 320 of about 113,722 (335)
G Protein Selectivity in Dopamine Receptors is Determined before GDP Release. [PDF]
Tawfeeq C+5 more
europepmc +1 more source
Quantitative approaches for studying G protein-coupled receptor signalling and pharmacology.
Pearce A+9 more
europepmc +1 more source
GRKs phosphorylate GPCR C-terminal peptides in a hierarchical manner
Löbbert A+5 more
europepmc +1 more source
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Life Sciences, 2003
The concept that GPCRs exist and potentially function as dimers and/or higher oligomers has progressed recently from hypothesis to being widely accepted. A range of techniques has contributed to this understanding, including co-immunoprecipitation and various forms of fluorescence and bioluminescence resonance energy transfer.
Graeme, Milligan+3 more
openaire +2 more sources
The concept that GPCRs exist and potentially function as dimers and/or higher oligomers has progressed recently from hypothesis to being widely accepted. A range of techniques has contributed to this understanding, including co-immunoprecipitation and various forms of fluorescence and bioluminescence resonance energy transfer.
Graeme, Milligan+3 more
openaire +2 more sources
Production of GPCR and GPCR complexes for structure determination
Current Opinion in Structural Biology, 2013Since the first high-resolution structure of the beta 2 adrenergic receptor (b2AR) in 2007, we have seen a growing number of G-protein-coupled receptor (GPCR) structures coming to the repertory, providing a significant progress in our understanding of the structural basis of their function.
Gebhard F. X. Schertler+2 more
openaire +3 more sources
2007
Many GPCR models have been built over the years for many different purposes, of which drug-design undoubtedly has been the most frequent one. The release of the structure of bovine rhodopsin in August 2000 enabled us to analyze models built before that period to learn things for the models we build today.
Paiva, A.C.+4 more
openaire +3 more sources
Many GPCR models have been built over the years for many different purposes, of which drug-design undoubtedly has been the most frequent one. The release of the structure of bovine rhodopsin in August 2000 enabled us to analyze models built before that period to learn things for the models we build today.
Paiva, A.C.+4 more
openaire +3 more sources
Molecular Pharmacology, 2005
The conserved "DRY" motif (Asp-Arg-Tyr) at the cytosolic surface of rhodopsin-like G protein-coupled receptors has been the subject of much work attempting to understand the mechanisms of receptor activation and interaction with G proteins. Both the acidic (Asp) and basic (Arg) residues of this motif are important for isomerization of receptors between
openaire +3 more sources
The conserved "DRY" motif (Asp-Arg-Tyr) at the cytosolic surface of rhodopsin-like G protein-coupled receptors has been the subject of much work attempting to understand the mechanisms of receptor activation and interaction with G proteins. Both the acidic (Asp) and basic (Arg) residues of this motif are important for isomerization of receptors between
openaire +3 more sources
GPCR-Interacting Proteins, Major Players of GPCR Function
2011G protein-coupled receptors (GPCRs) are, with approximately 800 members, among the most abundant membrane proteins in humans. They are responding to a plethora of ligands and are involved in the transmission of extracellular signals inside the cell. GPCRs are synthesized in the endoplasmatic reticulum and are then transported to the cell surface where ...
Ralf Jockers+15 more
openaire +4 more sources
A hypothesis for GPCR activation
Journal of Molecular Modeling, 2005Growing evidence that rhodopsin (RD) and related G protein-coupled receptors form functional dimers/oligomers, followed by direct proof (using atomic force microscopy) that in the retina disc membrane RD associates into a paracrystalline network of rows of dimers, need models of the RD-transducin (Gt) complex that would envision an optimal RD dimer ...
Jerzy Ciarkowski+2 more
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Privileged Structures in GPCRs [PDF]
Certain kinds of ligand substructures recur frequently in pharmacologically successful synthetic compounds. For this reason they are called privileged structures. In seeking an explanation for this phenomenon, it is observed that the privileged structure represents a generic substructure that matches commonly recurring conserved structural motifs in ...
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