Molecular basis for mitochondrial signaling

Author(s)

    • Rostovtseva, Tatiana

Bibliographic Information

Molecular basis for mitochondrial signaling

Tatiana K. Rostovtseva, editor

(Biological and medical physics, biomedical engineering)

Springer, c2017

Available at  / 3 libraries

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Note

Includes bibliographical references and index

Description and Table of Contents

Description

This book covers recent advances in the study of structure, function, and regulation of metabolite, protein and ion translocating channels, and transporters in mitochondria. A wide array of cutting-edge methods are covered, ranging from electrophysiology and cell biology to bioinformatics, as well as structural, systems, and computational biology. At last, the molecular identity of two important channels in the mitochondrial inner membrane, the mitochondrial calcium uniporter and the mitochondrial permeability transition pore have been established. After years of work on the physiology and structure of VDAC channels in the mitochondrial outer membrane, there have been multiple discoveries on VDAC permeation and regulation by cytosolic proteins. Recent breakthroughs in structural studies of the mitochondrial cholesterol translocator reveal a set of novel unexpected features and provide essential clues for defining therapeutic strategies. Molecular Basis for Mitochondrial Signaling covers these and many more recent studies of mitochondria function, their communication with other organelles, and their critical roles in development, aging, and in a plethora of stressful or degenerative events. Authored by leading researchers in the field, this volume will be an indispensable reference resource for graduate students and academics working in related areas of biophysics and cell biology as well as for professionals within industry.

Table of Contents

  • Mitochondrial Calcium Signaling.- Systems approaches to mitochondrial calcium signaling.- The mitochondrial Calcium Uniporter: Molecular Composition And Physiological Role.- Molecular Mechanisms of Mitochondrial Ca2+ Uptake.- Ca2+ uniporter and male fertility.- The Mitochondrial Permeability Transition pore: Finally Structure Meets Function.- ATP synthase forms the Mitochondrial Permeability Transition Pore.- C-subunit ring of the ATP synthase is the mitochondrial permeability transition pore.- Mitochondrial Outer Membrane Transport Systems: Structure, Function, and Physiological Implications.- VDAC and tubulin in regulation of mitochondrial metabolism.- Warburg revised: regulation of mitochondrial metabolism by VDAC in cancer cells.- VDAC isoforms in mammals.- Plant VDAC: function, structure, computational studies.- VDAC 1, 2 structure and structure-guided simulations of ATP translocation and VDAC gating.- MD simulations of VDAC selectivity and gating.- TSPO interacts with VDAC1 and triggers a ROS mediated inhibition of mitochondrial quality control.- VDAC/Hexokinase complex as a generator of the mitochondrial outer membrane potential.- TOM complex, Tom40 - protein translocator complex of the mitochondrial outer membrane.- Mitochondria And Cellular Signaling Network.- Mitochondrial Interactosome: mitochondria and cytoskeleton
  • cardiac mitochondria.- Mitochondrial respiration and ROS.- Diversity of Mitochondria Outer Membrane Permeabilization (MOMP) Pathways: Structure and Mechanism.- Molecular identity of mitochondrial apoptosis-induced channels (MAC).- Ceramide channels in the mitochondrial outer membrane.- Bax regulates ceramide synthase and ceramide-induced apoptosis.- Biophysical changes in bilayer properties following Bax insertion into a membrane.- A new view of the lethal apoptotic pore (Bax).- Other Mitochondrial Channels.- K(ATP) channels in the inner membrane.

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Details

  • NCID
    BB24276437
  • ISBN
    • 9783319555379
  • LCCN
    2017938879
  • Country Code
    sz
  • Title Language Code
    eng
  • Text Language Code
    eng
  • Place of Publication
    Cham
  • Pages/Volumes
    xiv, 386 p.
  • Size
    24 cm
  • Classification
  • Subject Headings
  • Parent Bibliography ID
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