//]]>

Folding for the Synapse (Record no. 17303)

000 -LEADER
fixed length control field 04613nam a22004815i 4500
003 - CONTROL NUMBER IDENTIFIER
control field OSt
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20140310150234.0
007 - PHYSICAL DESCRIPTION FIXED FIELD--GENERAL INFORMATION
fixed length control field cr nn 008mamaa
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 130531s2011 xxu| s |||| 0|eng d
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
International Standard Book Number 9781441970619
978-1-4419-7061-9
050 #4 - LIBRARY OF CONGRESS CALL NUMBER
Classification number RC321-580
082 04 - DEWEY DECIMAL CLASSIFICATION NUMBER
Classification number 612.8
Edition number 23
264 #1 -
-- Boston, MA :
-- Springer US :
-- Imprint: Springer,
-- 2011.
912 ## -
-- ZDB-2-SBL
100 1# - MAIN ENTRY--PERSONAL NAME
Personal name Wyttenbach, Andreas.
Relator term editor.
245 10 - IMMEDIATE SOURCE OF ACQUISITION NOTE
Title Folding for the Synapse
Medium [electronic resource] /
Statement of responsibility, etc edited by Andreas Wyttenbach, Vincent O'Connor.
300 ## - PHYSICAL DESCRIPTION
Extent VIII, 318p. 57 illus., 37 illus. in color.
Other physical details online resource.
505 0# - FORMATTED CONTENTS NOTE
Formatted contents note Introduction,- Protein Folding and Molecular Chaperones -- Transport of Proteins and Vesicles to the Synapse -- Protein Synthesis, Folding and Degradation in the Synaptic Compartment -- Synaptic Protein Interactions/Reguatlion by Molecular Chaperones -- Folding/Misfolding and Synaptic Dysfunction During Chronic Neurodegeration.
520 ## - SUMMARY, ETC.
Summary, etc Folding for the Synapse addresses the current view on how protein folding/misfolding and its regulation by molecular chaperones contribute to synapse function and dysfunction. Molecular chaperones control de novo protein folding. However, there is increasing awareness that chaperones physiologically function to regulate protein-protein interaction cascades. This book will introduce the concept of folding machineries and also give examples of the biological relevance of further chaperone modality. Chaperones prevent misfolded proteins from accumulating into toxic intra-or extracellular aggregates in Alzheimer’s, Parkinson’s, Huntington’s, prion, and motor neuron diseases (proteinopathies). The various disease-defining protein aggregates in these proteinopathies are indicative of overstretched chaperone-and altered protein degradation systems. The consequence of this for neuronal function is discussed in several contributing chapters. Synapses regulate cell-to-cell communication in the nervous system as relatively discrete compartments that are dysfunctional during proteinopathies. Due to their partial autarky, synapses have evolved intrinsic protein folding and homeostatic capabilities that are discussed in the book. The book servesced undergraduates, graduate students and (clinical) neuroscientists who want to develop an understanding of protein folding in health and disease. About the Editors: Dr. Andreas Wyttenbach holds a lectureship in Neuroscience at the University of Southampton (UK). After graduating in Biology at the University of Basel (Switzerland) he completed a PhD in Genetics and Evolution (University of Lausanne, Switzerland). During his postdoctoral research in the Departments of Medical Genetics and Biochemistry at the University of Cambridge (UK), he became inspired by the question of how protein misfolding in the CNS causes neuronal death, associated with neurological diseases. His current research concentrates on understanding how protein aggregation damages cells, with the motivation to provide a basis for therapeutic approaches that could prevent neurodegeneration. Dr. Vincent O’Connor holds a readership at the University of Southampton. After his undergraduate studies in Physiology and Biochemistry at Reading University (UK), he trained at University College London (UK), graduating with a PhD in Neurochemistry. His postdoctoral time was spent at the Max Planck Institute for Brain Research (Frankfurt, Germany) and the National Institute for Medical Research (London, UK) investigating mechanisms of neurotransmitter release and synaptic plasticity. His current efforts focus on translating the knowledge of basic synaptic mechanisms into understanding CNS disease processes and the concept of “synaptopathies”
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Medicine.
Topical term or geographic name as entry element Neurosciences.
Topical term or geographic name as entry element Biochemistry.
Topical term or geographic name as entry element Cytology.
Topical term or geographic name as entry element Neurobiology.
Topical term or geographic name as entry element Biomedicine.
Topical term or geographic name as entry element Neurosciences.
Topical term or geographic name as entry element Molecular Medicine.
Topical term or geographic name as entry element Neurobiology.
Topical term or geographic name as entry element Cell Biology.
Topical term or geographic name as entry element Biochemistry, general.
700 1# - ADDED ENTRY--PERSONAL NAME
Personal name O'Connor, Vincent.
Relator term editor.
710 2# - ADDED ENTRY--CORPORATE NAME
Corporate name or jurisdiction name as entry element SpringerLink (Online service)
773 0# - HOST ITEM ENTRY
Title Springer eBooks
776 08 - ADDITIONAL PHYSICAL FORM ENTRY
Display text Printed edition:
International Standard Book Number 9781441970602
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier http://dx.doi.org/10.1007/978-1-4419-7061-9
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Source of classification or shelving scheme
Item type E-Book
Copies
Price effective from Permanent location Date last seen Not for loan Date acquired Source of classification or shelving scheme Koha item type Damaged status Lost status Withdrawn status Current location Full call number
2014-04-04AUM Main Library2014-04-04 2014-04-04 E-Book   AUM Main Library612.8
Languages: 
English |
العربية