Results 321 to 330 of about 92,511 (354)
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Trends in Biotechnology, 2005
G protein-coupled receptors (GPCRs) are targets for 60-70% of drugs in development today. Traditionally, the drug discovery process has relied on screening of chemical compounds to identify novel and more-efficient drug molecules. Structure-based drug design, however, provides a targeted approach but has been severely hampered by limited knowledge of ...
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G protein-coupled receptors (GPCRs) are targets for 60-70% of drugs in development today. Traditionally, the drug discovery process has relied on screening of chemical compounds to identify novel and more-efficient drug molecules. Structure-based drug design, however, provides a targeted approach but has been severely hampered by limited knowledge of ...
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2010
There are a total of 33 members of adhesion G protein-coupled receptors (GPCRs) in humans and 30 members in mice and rats. More than half of these receptors are expressed in the central nervous system (CNS), indicating their possible roles in the development and function of the CNS.
Natalie, Strokes, Xianhua, Piao
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There are a total of 33 members of adhesion G protein-coupled receptors (GPCRs) in humans and 30 members in mice and rats. More than half of these receptors are expressed in the central nervous system (CNS), indicating their possible roles in the development and function of the CNS.
Natalie, Strokes, Xianhua, Piao
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Privileged Structures in GPCRs
2007Certain 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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Current Opinion in Structural Biology, 2019
Molecular switches in GPCRs enable passing the signal from the agonist binding site, usually located close to the extracellular surface, to the intracellular part of the receptor. The switches are usually associated with conserved structural motifs on transmembrane helices (TMs), and they are accompanied by adjacent residues which provide the signal to
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Molecular switches in GPCRs enable passing the signal from the agonist binding site, usually located close to the extracellular surface, to the intracellular part of the receptor. The switches are usually associated with conserved structural motifs on transmembrane helices (TMs), and they are accompanied by adjacent residues which provide the signal to
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Nature Methods, 2010
Researchers solve a high-resolution structure of a seven-helix transmembrane protein using nuclear magnetic resonance (NMR) spectroscopy.
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Researchers solve a high-resolution structure of a seven-helix transmembrane protein using nuclear magnetic resonance (NMR) spectroscopy.
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GPCR drug discovery: new agents, targets and indications
Nature reviews. Drug discoveryJavier Sánchez Lorente +5 more
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GPCRdb in 2021: integrating GPCR sequence, structure and function
Nucleic Acids Research, 2021Albert Jelke Kooistra +2 more
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