The Resource Structure and function of calcium release channels, edited by Irina I. Serysheva, (electronic resource)

Structure and function of calcium release channels, edited by Irina I. Serysheva, (electronic resource)

Label
Structure and function of calcium release channels
Title
Structure and function of calcium release channels
Statement of responsibility
edited by Irina I. Serysheva
Contributor
Subject
Genre
Language
  • eng
  • eng
Summary
This volume of Current Topics in Membranes focuses on Membrane Protein Crystallization, beginning with a review of past successes and general trends, then further discussing challenges of mebranes protein crystallization, cell free production of membrane proteins and novel lipids for membrane protein crystallization. This publication also includes tools to enchance membrane protein crystallization, technique advancements, and crystallization strategies used for photosystem I and its complexes, establishing Membrane Protein Crystallization as a needed, practical reference for researche
Member of
Is Subseries of
Cataloging source
MiAaPQ
Dewey number
  • 572.696
  • 574.875
Illustrations
illustrations
Index
index present
Language note
English
LC call number
QH601
LC item number
.S87 2010
Literary form
non fiction
Nature of contents
  • dictionaries
  • bibliography
http://library.link/vocab/relatedWorkOrContributorName
Serysheva, Irina I
Series statement
Current topics in membranes
Series volume
66
http://library.link/vocab/subjectName
  • Ryanodine
  • Membrane proteins
Label
Structure and function of calcium release channels, edited by Irina I. Serysheva, (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; Current Topics in Membranes; Copyright Page; Contents; Contributors; Preface; Previous Volumes in Series; Section 1: RYR Ca2+ Release Channels; Chapter 1: RyRs: Their Disposition, Frequency, and Relationships with Other Proteins of Calcium Release Units; I. Overview; II. Introduction; III. Cardiac CRUs; IV. CRUs in Skeletal and Invertebrate Body Muscles; V. Factors Affecting CRU Assembly in Skeletal and Cardiac Muscles; VI. Isoform-Specific Features of RyR Distribution; VII. Architecture of SR and T Tubule Membranes is Muscle- and Fiber-Type Specific; Acknowledgments; References
  • Chapter 2: Electron Microscopy of Ryanodine ReceptorsI. Overview; II. Introduction; III. Cryo-EM of Macromolecular Complexes; IV. Three-Dimensional Architecture of RyR as Determined by Cryo-EM; V. a-Helices in the TM Region and the Mechanism of Calcium Channel Gating; VI. Synergism of 3D Cryo-EM and Other Biophysical/Biochemical Techniques; VII. Outlook and Perspectives; References; Chapter 3: The Ryanodine Receptor Pore: Is There a Consensus View?; I. Overview; II. Introduction; III. Ion Handling in RyR; IV. Where is the PFR in the RyR Channel?
  • V. Attempts to Identify the Structure of the RyR PFRVI. Theoretical Approaches to Understanding the Mechanisms Underlying Ion Translocation and Discrimination in RyR; VII. Testing Physical and Theoretical Models of the RyR PFR by Residue Substitution; VIII. Concluding Remarks; Acknowledgments; References; Chapter 4: Regulation of RyR Channel Gating by Ca2+, Mg2+ and ATP; I. Overview; II. Introduction; III. RyR2 in Cardiac Contraction and Pacemaking; IV. Four Ca2+ Sensing Mechanisms for RyR2; V. Synergistic Ca2+-Activation via Cytoplasmic and Luminal Facing Binding Sites
  • VI. Channel Open Times and the Role of Ca2+ Feed-ThroughVII. Three Mechanisms for Mg2+-Inhibition of RyR2; VIII. A Model for Ca2+ and Mg2+ Regulation of RyR2; IX. Adenine Neucleotides; X. Regulation of RyR2 in Cardiac E-C Coupling; XI. Concluding Remarks; Acknowledgments; References; Chapter 5: Regulation of Ryanodine Receptor Ion Channels Through Posttranslational Modifications; I. Overview; II. Introduction; III. RyR1 and RyR2 Phosphorylation; IV. RyR Modulation by Reactive Oxygen and Nitrogen Species; V. Conclusions; Acknowledgment; References
  • Chapter 6: Crosstalk via the Sarcoplasmic Gap: The DHPR-RyR InteractionI. Overview; II. DHPR and RyR Arrangement in Skeletal and Cardiac Muscle Membranes-Basis for Differences in the EC Coupling Mechanism; III. Structural Domains Involved in skDHPR-RyR1 Interaction; IV. The Role of Intracellular Molecular Regions Besides the a1S II-III Loop in skDHPR-RyR1 Interaction; V. Intracellular Molecular Regions of a1S Involved in Tetrad Formation; VI. The Role of the Accessory skDHPR Subunits in Interaction with RyR1; VII. Conclusion; References; Chapter 7: Ryanodinopathies: RyR-Linked Muscle Diseases
  • I. Overview
Dimensions
unknown
Extent
1 online resource (389 p.)
Form of item
online
Isbn
9786612770142
Media category
computer
Media type code
c
Specific material designation
remote
System control number
  • (CKB)2670000000047824
  • (EBL)632003
  • (OCoLC)813296137
  • (SSID)ssj0000429010
  • (PQKBManifestationID)12174773
  • (PQKBTitleCode)TC0000429010
  • (PQKBWorkID)10424560
  • (PQKB)10212011
  • (MiAaPQ)EBC632003
  • (EXLCZ)992670000000047824
Label
Structure and function of calcium release channels, edited by Irina I. Serysheva, (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; Current Topics in Membranes; Copyright Page; Contents; Contributors; Preface; Previous Volumes in Series; Section 1: RYR Ca2+ Release Channels; Chapter 1: RyRs: Their Disposition, Frequency, and Relationships with Other Proteins of Calcium Release Units; I. Overview; II. Introduction; III. Cardiac CRUs; IV. CRUs in Skeletal and Invertebrate Body Muscles; V. Factors Affecting CRU Assembly in Skeletal and Cardiac Muscles; VI. Isoform-Specific Features of RyR Distribution; VII. Architecture of SR and T Tubule Membranes is Muscle- and Fiber-Type Specific; Acknowledgments; References
  • Chapter 2: Electron Microscopy of Ryanodine ReceptorsI. Overview; II. Introduction; III. Cryo-EM of Macromolecular Complexes; IV. Three-Dimensional Architecture of RyR as Determined by Cryo-EM; V. a-Helices in the TM Region and the Mechanism of Calcium Channel Gating; VI. Synergism of 3D Cryo-EM and Other Biophysical/Biochemical Techniques; VII. Outlook and Perspectives; References; Chapter 3: The Ryanodine Receptor Pore: Is There a Consensus View?; I. Overview; II. Introduction; III. Ion Handling in RyR; IV. Where is the PFR in the RyR Channel?
  • V. Attempts to Identify the Structure of the RyR PFRVI. Theoretical Approaches to Understanding the Mechanisms Underlying Ion Translocation and Discrimination in RyR; VII. Testing Physical and Theoretical Models of the RyR PFR by Residue Substitution; VIII. Concluding Remarks; Acknowledgments; References; Chapter 4: Regulation of RyR Channel Gating by Ca2+, Mg2+ and ATP; I. Overview; II. Introduction; III. RyR2 in Cardiac Contraction and Pacemaking; IV. Four Ca2+ Sensing Mechanisms for RyR2; V. Synergistic Ca2+-Activation via Cytoplasmic and Luminal Facing Binding Sites
  • VI. Channel Open Times and the Role of Ca2+ Feed-ThroughVII. Three Mechanisms for Mg2+-Inhibition of RyR2; VIII. A Model for Ca2+ and Mg2+ Regulation of RyR2; IX. Adenine Neucleotides; X. Regulation of RyR2 in Cardiac E-C Coupling; XI. Concluding Remarks; Acknowledgments; References; Chapter 5: Regulation of Ryanodine Receptor Ion Channels Through Posttranslational Modifications; I. Overview; II. Introduction; III. RyR1 and RyR2 Phosphorylation; IV. RyR Modulation by Reactive Oxygen and Nitrogen Species; V. Conclusions; Acknowledgment; References
  • Chapter 6: Crosstalk via the Sarcoplasmic Gap: The DHPR-RyR InteractionI. Overview; II. DHPR and RyR Arrangement in Skeletal and Cardiac Muscle Membranes-Basis for Differences in the EC Coupling Mechanism; III. Structural Domains Involved in skDHPR-RyR1 Interaction; IV. The Role of Intracellular Molecular Regions Besides the a1S II-III Loop in skDHPR-RyR1 Interaction; V. Intracellular Molecular Regions of a1S Involved in Tetrad Formation; VI. The Role of the Accessory skDHPR Subunits in Interaction with RyR1; VII. Conclusion; References; Chapter 7: Ryanodinopathies: RyR-Linked Muscle Diseases
  • I. Overview
Dimensions
unknown
Extent
1 online resource (389 p.)
Form of item
online
Isbn
9786612770142
Media category
computer
Media type code
c
Specific material designation
remote
System control number
  • (CKB)2670000000047824
  • (EBL)632003
  • (OCoLC)813296137
  • (SSID)ssj0000429010
  • (PQKBManifestationID)12174773
  • (PQKBTitleCode)TC0000429010
  • (PQKBWorkID)10424560
  • (PQKB)10212011
  • (MiAaPQ)EBC632003
  • (EXLCZ)992670000000047824

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