Molecular Biology of Mitochondrial Transport Systems: Nato ASI Subseries H:, cartea 83
Editat de Michael Forte, Marco Colombinien Limba Engleză Paperback – 8 dec 2011
The book contains studies utilizing the techniques of biochemistry, physiology, molecular biology and genetics to reveal the structure and function of mitochondrial transport systems.
It is divided into the following six sections:
- Proton Translocation: The Uncoupling Protein and the ATPase; - Carriers and Transporters; - Mitochondrial Ion Channels; Structure of the Outer Mitochondrial Membrane Channel, VDAC; - VDAC, Peripheral Kinases and Energy Utilization; - Mitochondrial Channels in Humans and Relationship to Disease.
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Specificații
ISBN-13: 9783642789380
ISBN-10: 3642789382
Pagini: 428
Ilustrații: XII, 408 p.
Dimensiuni: 155 x 235 x 22 mm
Greutate: 0.59 kg
Ediția:Softcover reprint of the original 1st ed. 1994
Editura: Springer Berlin, Heidelberg
Colecția Springer
Seria Nato ASI Subseries H:
Locul publicării:Berlin, Heidelberg, Germany
ISBN-10: 3642789382
Pagini: 428
Ilustrații: XII, 408 p.
Dimensiuni: 155 x 235 x 22 mm
Greutate: 0.59 kg
Ediția:Softcover reprint of the original 1st ed. 1994
Editura: Springer Berlin, Heidelberg
Colecția Springer
Seria Nato ASI Subseries H:
Locul publicării:Berlin, Heidelberg, Germany
Public țintă
ResearchCuprins
Proton Translocation: The Uncoupling Protein and the Atpase.- Molecular Studies of the Mitochondrial Uncoupling Protein.- Structure-Function Relationship in the Uncoupling Protein of Brown Adipose Tissue.- The Gating and Coupling Function of Mitochondrial H+ ATP Synthase. Role of Fo and F1 Subunits.- Carriers and Transporters.- Extension of the Mitochondrial Transporter Family.- The Tricarboxylate Carrier.- The Mitochondrial Pyruvate Carrier: The Mechanism of Substrate Binding.- Membrane Topology of the ADP/ATP Carrier from Mitochondria.- The Use of Ligand Binding Techniques to Identify Transport Proteins: The Characterization of the [125I]-Iodophenylarsine Oxide Receptor in Rat Mitochondrial Membranes.- Channel Properties of Mitochondrial Carriers.- Mitochondrial ion Channels.- A Minimal Kinetic Model of the Activity of the 107 pS Channel of the Inner Membrane of Mitochondria.- A Channel Model to Explain Regulation of the Mitochondrial Inner Membrane Anion Channel (IMAC).- The Mitochondrial Permeabilization Pore.- Mitochondrial Channels: An Integrated View.- Purification and Patch Clamp Analysis of Two Mitochondrial Channels.- The Mitochondrial Outer Membrane Contains at Least Two Distinct Channels.- ATP-Sensitive K+ Channel in Rat Liver Mitochondria: Functional Characteristics.- Structure of the Outer Mitochondrial Membrane Channel, VDAC.- Probing for the Voltage Sensor in a Mitochondrial Channel, VDAC, Using Site-Directed Mutagenesis.- Insights into the Structure of the Mitochondrial Channel, VDAC, Provided by Electron Microscopy.- Experimental Supports to a Sixteen-Strands Model of Transmembrane Arrangement of Mitochondrial Porin and Preliminary Results Concerning a Multigene Family in Drosophila melanogaster Related to Human Mitochondrial Porin.- VDAC, Peripheral K1Nases and Energy Utilization.- Structure and Function of the VDAC Ion Channel.- The Function of the Mitochondrial Outer Membrane Pore in the Regulation of Peripheral Kinases and Energy Metabolism.- Coordinated Regulation of Cerebral Glycolytic and Oxidative Metabolism Mediated by Mitochondrially Bound Hexokinase.- Influence of Macromolecules on the Permeability of Porin Pores and Dynamic Compartmentation of Adenine Nucleotides in the Mitochondrial Intermembrane Space.- Restrictions of Metabolite Permeation through the Outer Mitochondrial Membrane of Porin-Deficient Yeast Mutant.- Mitochondrial Channels in Humans and Relationship to Disease.- Role of Porin-Kinase Interactions in Disease.- Genes Encoding Human VDAC Proteins: Identification of Multiple Isoforms, Expression in Yeast and Chromosomal Localization.- “Porin 31HL” in the Plasmalemma of Human Cells: A VDAC Discussed as Part of a Chloride Channel Complex in Normal and Cystic Fibrosis B-Lymphocyte Cell Lines.