Ligand design for G protein-coupled receptors [[electronic resource] /] / edited by Didier Rognan |
Pubbl/distr/stampa | Weinheim ; ; [Great Britain], : Wiley, 2006 |
Descrizione fisica | 1 online resource (286 p.) |
Disciplina |
541.2242
615.19 |
Altri autori (Persone) | RognanDidier |
Collana | Methods and principles in medicinal chemistry |
Soggetto topico |
Ligands (Biochemistry)
G proteins Drugs - Design |
Soggetto genere / forma | Electronic books. |
ISBN |
1-280-72349-1
9786610723492 3-527-60824-9 3-527-60826-5 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Ligand Design for G Protein-coupled Receptors; Contents; Preface; A Personal Foreword; List of Contributors; 1 G Protein-coupled Receptors in the Human Genome; 1.1 Introduction; 1.2 The Adhesion Family; 1.3 The Secretin Family; 1.4 The Frizzled/Taste 2 Family; 1.4.1 The Frizzled Receptor Cluster; 1.4.2 The Taste 2 Receptor Cluster; 1.5 The Glutamate Family; 1.6 The Rhodopsin Family; 1.6.1 The Rhodopsin α-Group; 1.6.1.1 The Prostaglandin Receptor Cluster; 1.6.1.2 The Amine Receptor Cluster; 1.6.1.3 The Opsin Receptor Cluster; 1.6.1.4 The Melatonin Receptor Cluster
1.6.1.5 The MECA Receptor Cluster1.6.1.6 Other Rhodopsin α-Receptors; 1.6.2 Rhodopsin β-Group; 1.6.3 Rhodopsin γ-Group; 1.6.3.1 The SOG Receptor Cluster; 1.6.3.2 The Melanocyte Concentrating Hormone Receptor Cluster; 1.6.3.3 The Chemokine Receptor Cluster; 1.6.3.4 Other Rhodopsin γ-Receptors; 1.6.4 The Rhodopsin δ-Group; 1.6.4.1 The MAS-related Receptor Cluster; 1.6.4.2 The Glycoprotein Receptor Cluster; 1.6.4.3 The Coagulation Factor Receptor Cluster; 1.6.4.4 The Purinergic Receptor Cluster; 1.6.4.5 The Olfactory Receptor Cluster; 1.6.4.6 Other Rhodopsin α-Receptors; 1.7 Other GPCRs 1.8 Future PerspectiveReferences; 2 Why G Protein-coupled Receptors Databases are Needed; 2.1 Introduction; 2.2 A Non-exhaustive List of the GPCR Data Models; 2.3 Using the Central Dogma of Biology; 2.4 Using the Tree of Life; 2.5 Using a Chemogenomic Approach; 2.6 Conclusion; References; 3 A Novel Drug Screening Assay for G Protein-coupled Receptors; 3.1 Introduction; 3.1.1 History; 3.1.2 Nuclear Translocation of Endogenous GPCRs; 3.1.3 The MOCA Method; 3.2 The MOCA Strategy Demonstrated with the D1 Dopamine Receptor; 3.2.1 Development of the Assay 3.2.2 Concentration-dependent Antagonist Blockade of Nuclear Transport3.2.3 Measurement of Receptor Cell Surface Expression: Antagonist Binding of Receptors at Cell Surface; 3.3 Development of Quantitative Methodology Suitable for High Throughput Analysis; 3.3.1 Nuclear Translocation of Orphan GPCRs; 3.4 Discussion of the MOCA Method; 3.5 Conclusion; References; 4 Importance of GPCR Dimerization for Function: The Case of the Class C GPCRs; 4.1 Introduction; 4.2 Class C GPCRs are Multidomain Proteins; 4.2.1 The VFT; 4.2.2 The CRD; 4.2.3 The HD; 4.2.4 C-Tail 4.3 Class C GPCRs are Constitutive Dimers4.4 Agonists Activate Class C GPCRs by Stabilizing the Closed State of the VFT; 4.5 Dimeric Functioning of the Dimer of VFTs; 4.5.1 Agonist Stoichiometry: Symmetry or Asymmetry?; 4.6 The Heptahelical Domain, the Target of Positive and Negative Allosteric Modulators, Behaves in a Manner Similar to Rhodopsin-like Class A GPCRs; 4.7 Allosteric Coupling Between the Extracellular and Heptahelical Domains within the Dimer; 4.7.1 Molecular Determinants of the Coupling Between the VFT and the HD; 4.7.2 Cis- and Trans-activation Can Exist within Class C GPCRs 4.8 Asymmetric Functioning of the HD Dimer |
Record Nr. | UNINA-9910144274103321 |
Weinheim ; ; [Great Britain], : Wiley, 2006 | ||
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Lo trovi qui: Univ. Federico II | ||
|
Ligand design for G protein-coupled receptors [[electronic resource] /] / edited by Didier Rognan |
Pubbl/distr/stampa | Weinheim ; ; [Great Britain], : Wiley, 2006 |
Descrizione fisica | 1 online resource (286 p.) |
Disciplina |
541.2242
615.19 |
Altri autori (Persone) | RognanDidier |
Collana | Methods and principles in medicinal chemistry |
Soggetto topico |
Ligands (Biochemistry)
G proteins Drugs - Design |
ISBN |
1-280-72349-1
9786610723492 3-527-60824-9 3-527-60826-5 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Ligand Design for G Protein-coupled Receptors; Contents; Preface; A Personal Foreword; List of Contributors; 1 G Protein-coupled Receptors in the Human Genome; 1.1 Introduction; 1.2 The Adhesion Family; 1.3 The Secretin Family; 1.4 The Frizzled/Taste 2 Family; 1.4.1 The Frizzled Receptor Cluster; 1.4.2 The Taste 2 Receptor Cluster; 1.5 The Glutamate Family; 1.6 The Rhodopsin Family; 1.6.1 The Rhodopsin α-Group; 1.6.1.1 The Prostaglandin Receptor Cluster; 1.6.1.2 The Amine Receptor Cluster; 1.6.1.3 The Opsin Receptor Cluster; 1.6.1.4 The Melatonin Receptor Cluster
1.6.1.5 The MECA Receptor Cluster1.6.1.6 Other Rhodopsin α-Receptors; 1.6.2 Rhodopsin β-Group; 1.6.3 Rhodopsin γ-Group; 1.6.3.1 The SOG Receptor Cluster; 1.6.3.2 The Melanocyte Concentrating Hormone Receptor Cluster; 1.6.3.3 The Chemokine Receptor Cluster; 1.6.3.4 Other Rhodopsin γ-Receptors; 1.6.4 The Rhodopsin δ-Group; 1.6.4.1 The MAS-related Receptor Cluster; 1.6.4.2 The Glycoprotein Receptor Cluster; 1.6.4.3 The Coagulation Factor Receptor Cluster; 1.6.4.4 The Purinergic Receptor Cluster; 1.6.4.5 The Olfactory Receptor Cluster; 1.6.4.6 Other Rhodopsin α-Receptors; 1.7 Other GPCRs 1.8 Future PerspectiveReferences; 2 Why G Protein-coupled Receptors Databases are Needed; 2.1 Introduction; 2.2 A Non-exhaustive List of the GPCR Data Models; 2.3 Using the Central Dogma of Biology; 2.4 Using the Tree of Life; 2.5 Using a Chemogenomic Approach; 2.6 Conclusion; References; 3 A Novel Drug Screening Assay for G Protein-coupled Receptors; 3.1 Introduction; 3.1.1 History; 3.1.2 Nuclear Translocation of Endogenous GPCRs; 3.1.3 The MOCA Method; 3.2 The MOCA Strategy Demonstrated with the D1 Dopamine Receptor; 3.2.1 Development of the Assay 3.2.2 Concentration-dependent Antagonist Blockade of Nuclear Transport3.2.3 Measurement of Receptor Cell Surface Expression: Antagonist Binding of Receptors at Cell Surface; 3.3 Development of Quantitative Methodology Suitable for High Throughput Analysis; 3.3.1 Nuclear Translocation of Orphan GPCRs; 3.4 Discussion of the MOCA Method; 3.5 Conclusion; References; 4 Importance of GPCR Dimerization for Function: The Case of the Class C GPCRs; 4.1 Introduction; 4.2 Class C GPCRs are Multidomain Proteins; 4.2.1 The VFT; 4.2.2 The CRD; 4.2.3 The HD; 4.2.4 C-Tail 4.3 Class C GPCRs are Constitutive Dimers4.4 Agonists Activate Class C GPCRs by Stabilizing the Closed State of the VFT; 4.5 Dimeric Functioning of the Dimer of VFTs; 4.5.1 Agonist Stoichiometry: Symmetry or Asymmetry?; 4.6 The Heptahelical Domain, the Target of Positive and Negative Allosteric Modulators, Behaves in a Manner Similar to Rhodopsin-like Class A GPCRs; 4.7 Allosteric Coupling Between the Extracellular and Heptahelical Domains within the Dimer; 4.7.1 Molecular Determinants of the Coupling Between the VFT and the HD; 4.7.2 Cis- and Trans-activation Can Exist within Class C GPCRs 4.8 Asymmetric Functioning of the HD Dimer |
Record Nr. | UNINA-9910831167703321 |
Weinheim ; ; [Great Britain], : Wiley, 2006 | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
|
Ligand design for G protein-coupled receptors / / edited by Didier Rognan |
Pubbl/distr/stampa | Weinheim ; ; [Great Britain], : Wiley, 2006 |
Descrizione fisica | 1 online resource (286 p.) |
Disciplina | 541.2242 |
Altri autori (Persone) | RognanDidier |
Collana | Methods and principles in medicinal chemistry |
Soggetto topico |
Ligands (Biochemistry)
G proteins Drugs - Design |
ISBN |
1-280-72349-1
9786610723492 3-527-60824-9 3-527-60826-5 |
Formato | Materiale a stampa ![]() |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Ligand Design for G Protein-coupled Receptors; Contents; Preface; A Personal Foreword; List of Contributors; 1 G Protein-coupled Receptors in the Human Genome; 1.1 Introduction; 1.2 The Adhesion Family; 1.3 The Secretin Family; 1.4 The Frizzled/Taste 2 Family; 1.4.1 The Frizzled Receptor Cluster; 1.4.2 The Taste 2 Receptor Cluster; 1.5 The Glutamate Family; 1.6 The Rhodopsin Family; 1.6.1 The Rhodopsin α-Group; 1.6.1.1 The Prostaglandin Receptor Cluster; 1.6.1.2 The Amine Receptor Cluster; 1.6.1.3 The Opsin Receptor Cluster; 1.6.1.4 The Melatonin Receptor Cluster
1.6.1.5 The MECA Receptor Cluster1.6.1.6 Other Rhodopsin α-Receptors; 1.6.2 Rhodopsin β-Group; 1.6.3 Rhodopsin γ-Group; 1.6.3.1 The SOG Receptor Cluster; 1.6.3.2 The Melanocyte Concentrating Hormone Receptor Cluster; 1.6.3.3 The Chemokine Receptor Cluster; 1.6.3.4 Other Rhodopsin γ-Receptors; 1.6.4 The Rhodopsin δ-Group; 1.6.4.1 The MAS-related Receptor Cluster; 1.6.4.2 The Glycoprotein Receptor Cluster; 1.6.4.3 The Coagulation Factor Receptor Cluster; 1.6.4.4 The Purinergic Receptor Cluster; 1.6.4.5 The Olfactory Receptor Cluster; 1.6.4.6 Other Rhodopsin α-Receptors; 1.7 Other GPCRs 1.8 Future PerspectiveReferences; 2 Why G Protein-coupled Receptors Databases are Needed; 2.1 Introduction; 2.2 A Non-exhaustive List of the GPCR Data Models; 2.3 Using the Central Dogma of Biology; 2.4 Using the Tree of Life; 2.5 Using a Chemogenomic Approach; 2.6 Conclusion; References; 3 A Novel Drug Screening Assay for G Protein-coupled Receptors; 3.1 Introduction; 3.1.1 History; 3.1.2 Nuclear Translocation of Endogenous GPCRs; 3.1.3 The MOCA Method; 3.2 The MOCA Strategy Demonstrated with the D1 Dopamine Receptor; 3.2.1 Development of the Assay 3.2.2 Concentration-dependent Antagonist Blockade of Nuclear Transport3.2.3 Measurement of Receptor Cell Surface Expression: Antagonist Binding of Receptors at Cell Surface; 3.3 Development of Quantitative Methodology Suitable for High Throughput Analysis; 3.3.1 Nuclear Translocation of Orphan GPCRs; 3.4 Discussion of the MOCA Method; 3.5 Conclusion; References; 4 Importance of GPCR Dimerization for Function: The Case of the Class C GPCRs; 4.1 Introduction; 4.2 Class C GPCRs are Multidomain Proteins; 4.2.1 The VFT; 4.2.2 The CRD; 4.2.3 The HD; 4.2.4 C-Tail 4.3 Class C GPCRs are Constitutive Dimers4.4 Agonists Activate Class C GPCRs by Stabilizing the Closed State of the VFT; 4.5 Dimeric Functioning of the Dimer of VFTs; 4.5.1 Agonist Stoichiometry: Symmetry or Asymmetry?; 4.6 The Heptahelical Domain, the Target of Positive and Negative Allosteric Modulators, Behaves in a Manner Similar to Rhodopsin-like Class A GPCRs; 4.7 Allosteric Coupling Between the Extracellular and Heptahelical Domains within the Dimer; 4.7.1 Molecular Determinants of the Coupling Between the VFT and the HD; 4.7.2 Cis- and Trans-activation Can Exist within Class C GPCRs 4.8 Asymmetric Functioning of the HD Dimer |
Record Nr. | UNINA-9910877725303321 |
Weinheim ; ; [Great Britain], : Wiley, 2006 | ||
![]() | ||
Lo trovi qui: Univ. Federico II | ||
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