The Resource Membrane proteins as drug targets, edited by Charles A. Lunn, (electronic resource)

Membrane proteins as drug targets, edited by Charles A. Lunn, (electronic resource)

Label
Membrane proteins as drug targets
Title
Membrane proteins as drug targets
Statement of responsibility
edited by Charles A. Lunn
Title variation
Membrane protiens [sic] as drug targets
Contributor
Subject
Genre
Language
  • eng
  • eng
Summary
Membrane proteins continue to be prime drug targets because they perform essential processes in the cell including controlling the flow of information and materials between cells and mediating activities like hormone action and nerve impulses. The study of membrane proteins could lead to new and improved pharmaceutical treatments for a wide range of illnesses such as heart disease, cystic fibrosis and depression. This volume reviews the latest developments in the field. * Discusses new discoveries, approaches, and ideas in the field of membrane proteins and reviews how
Member of
Is Subseries of
Cataloging source
MiAaPQ
Dewey number
  • 615.19
  • 615.7
Illustrations
illustrations
Index
index present
Language note
English
LC call number
RM301.25
LC item number
.M46 2010
Literary form
non fiction
Nature of contents
  • dictionaries
  • bibliography
http://library.link/vocab/relatedWorkOrContributorName
Lunn, Charles A
Series statement
Progress in molecular biology and translational science,
Series volume
v. 91
http://library.link/vocab/subjectName
  • Drug development
  • Membrane proteins
  • Pharmacology
Label
Membrane proteins as drug targets, edited by Charles A. Lunn, (electronic resource)
Instantiates
Publication
Note
Description based upon print version of record
Bibliography note
Includes bibliographical references and index
Carrier category
online resource
Carrier category code
cr
Content category
text
Content type code
txt
Contents
  • Front Cover; Progress in Molecular Biology and Translational Science; Copyright Page; Contents; Contributors; Preface; Chapter 1: Inverse Agonism at Serotonin and Cannabinoid Receptors; I. Serotonin Receptors; II. Constitutive Receptor Activity and Inverse Agonism; III. Ligands Identified In Vitro as Inverse Agonists at 5-HT Receptors; IV. Characteristics of Serotonin2A (5-HT2A) and 5-HT2C Receptors; V. Measurement of Constitutive Activity and Inverse Agonism In Vivo; VI. Inverse Agonism and Constitutive Activity of the Serotonin 5-HT2A Receptor In Vivo
  • VII. Inverse Agonism and Constitutive Activity of the Serotonin 5-HT2C Receptor In VivoVIII. Cannabinoid Receptors; IX. Summary; References; Chapter 2: G Protein-Coupled Receptor Heteromers as New Targets for Drug Development; I. Unique Biochemical Characteristics of GPCR Heteromers; II. Energy Transfer-Based Techniques to Study GPCR Oligomerization; III. Receptor Heteromers as Pharmacological Targets; Acknowledgments; References; Chapter 3: Receptor Activity Modifying Proteins and Their Potential as Drug Targets; I. Introduction; II. RAMPs and Their Discovery
  • III. RAMPs and Their Interaction with GPCRsIV. RAMP Modulation of GPCR Pharmacology; V. RAMPs as Receptor Chaperones; VI. RAMPs and Receptor Internalization; VII. RAMPs and Receptor Signaling; VIII. Posttranslational Modifications of RAMPs-Glycosylation; IX. Correlation of RAMPs with Receptors In Vivo; X. Regulation of RAMPs in Disease; XI. RAMPs as Drug Targets; XII. Concluding Remarks; References; Chapter 4: Regulators of G Protein Signaling Proteins as Targets for Drug Discovery; I. Introduction; II. RGS Protein Families; III. RGS Protein Mechanisms of Actions
  • IV. Biological Functions of RGS ProteinsV. Reaching Specificity-Modulating Specific Receptors and Signaling Pathways; VI. Targeting RGS Proteins in Drug Discovery-From Increased Knowledge to Increased Throughput; VII. Future Prospects; References; Chapter 5: Escorts Take the Lead: Molecular Chaperones as Therapeutic Targets; I. Introduction; II. Molecular Chaperones and Accessory Proteins; III. GPCR Maturation and Postendoplasmic Reticulum Trafficking; IV. Regulated Translocation to Intracellular Compartments and/or the Plasma Membrane; V. GPCR Oligomerization
  • VI. Specific Molecular Chaperones for GPCRsVII. The Melanocortin-2 Receptor and MRAP; VIII. Opioid Receptors and RTP4; IX. Pharmacological Chaperones; X. Conclusions; Acknowledgments; References; Chapter 6: The T1R2/T1R3 Sweet Receptor and TRPM5 Ion Channel: Taste Targets with Therapeutic Potential; I. Ingestive Behaviors as Therapeutic Endpoints; II. Taste Signaling Proteins as Targets for the Drug Discovery Approach; III. Obesity and Diabetes-The Result of Dysfunctional Ingestive Behavior; IV. The T1R2/T1R3 Sweet Receptor; V. The TRPM5 Ion Channel
  • VI. Morphological and Functional Characteristics of Type II Taste Cells
Dimensions
unknown
Extent
1 online resource (260 p.)
Form of item
online
Isbn
9786612770173
Media category
computer
Media type code
c
Specific material designation
remote
System control number
  • (CKB)2670000000048169
  • (EBL)631986
  • (OCoLC)668969901
  • (SSID)ssj0000439528
  • (PQKBManifestationID)12140832
  • (PQKBTitleCode)TC0000439528
  • (PQKBWorkID)10464295
  • (PQKB)10984408
  • (MiAaPQ)EBC631986
  • (EXLCZ)992670000000048169
Label
Membrane proteins as drug targets, edited by Charles A. Lunn, (electronic resource)
Publication
Note
Description based upon print version of record
Bibliography note
Includes bibliographical references and index
Carrier category
online resource
Carrier category code
cr
Content category
text
Content type code
txt
Contents
  • Front Cover; Progress in Molecular Biology and Translational Science; Copyright Page; Contents; Contributors; Preface; Chapter 1: Inverse Agonism at Serotonin and Cannabinoid Receptors; I. Serotonin Receptors; II. Constitutive Receptor Activity and Inverse Agonism; III. Ligands Identified In Vitro as Inverse Agonists at 5-HT Receptors; IV. Characteristics of Serotonin2A (5-HT2A) and 5-HT2C Receptors; V. Measurement of Constitutive Activity and Inverse Agonism In Vivo; VI. Inverse Agonism and Constitutive Activity of the Serotonin 5-HT2A Receptor In Vivo
  • VII. Inverse Agonism and Constitutive Activity of the Serotonin 5-HT2C Receptor In VivoVIII. Cannabinoid Receptors; IX. Summary; References; Chapter 2: G Protein-Coupled Receptor Heteromers as New Targets for Drug Development; I. Unique Biochemical Characteristics of GPCR Heteromers; II. Energy Transfer-Based Techniques to Study GPCR Oligomerization; III. Receptor Heteromers as Pharmacological Targets; Acknowledgments; References; Chapter 3: Receptor Activity Modifying Proteins and Their Potential as Drug Targets; I. Introduction; II. RAMPs and Their Discovery
  • III. RAMPs and Their Interaction with GPCRsIV. RAMP Modulation of GPCR Pharmacology; V. RAMPs as Receptor Chaperones; VI. RAMPs and Receptor Internalization; VII. RAMPs and Receptor Signaling; VIII. Posttranslational Modifications of RAMPs-Glycosylation; IX. Correlation of RAMPs with Receptors In Vivo; X. Regulation of RAMPs in Disease; XI. RAMPs as Drug Targets; XII. Concluding Remarks; References; Chapter 4: Regulators of G Protein Signaling Proteins as Targets for Drug Discovery; I. Introduction; II. RGS Protein Families; III. RGS Protein Mechanisms of Actions
  • IV. Biological Functions of RGS ProteinsV. Reaching Specificity-Modulating Specific Receptors and Signaling Pathways; VI. Targeting RGS Proteins in Drug Discovery-From Increased Knowledge to Increased Throughput; VII. Future Prospects; References; Chapter 5: Escorts Take the Lead: Molecular Chaperones as Therapeutic Targets; I. Introduction; II. Molecular Chaperones and Accessory Proteins; III. GPCR Maturation and Postendoplasmic Reticulum Trafficking; IV. Regulated Translocation to Intracellular Compartments and/or the Plasma Membrane; V. GPCR Oligomerization
  • VI. Specific Molecular Chaperones for GPCRsVII. The Melanocortin-2 Receptor and MRAP; VIII. Opioid Receptors and RTP4; IX. Pharmacological Chaperones; X. Conclusions; Acknowledgments; References; Chapter 6: The T1R2/T1R3 Sweet Receptor and TRPM5 Ion Channel: Taste Targets with Therapeutic Potential; I. Ingestive Behaviors as Therapeutic Endpoints; II. Taste Signaling Proteins as Targets for the Drug Discovery Approach; III. Obesity and Diabetes-The Result of Dysfunctional Ingestive Behavior; IV. The T1R2/T1R3 Sweet Receptor; V. The TRPM5 Ion Channel
  • VI. Morphological and Functional Characteristics of Type II Taste Cells
Dimensions
unknown
Extent
1 online resource (260 p.)
Form of item
online
Isbn
9786612770173
Media category
computer
Media type code
c
Specific material designation
remote
System control number
  • (CKB)2670000000048169
  • (EBL)631986
  • (OCoLC)668969901
  • (SSID)ssj0000439528
  • (PQKBManifestationID)12140832
  • (PQKBTitleCode)TC0000439528
  • (PQKBWorkID)10464295
  • (PQKB)10984408
  • (MiAaPQ)EBC631986
  • (EXLCZ)992670000000048169

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