Alzheimer's disease : (Record no. 708830)

MARC details
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001 - CONTROL NUMBER
control field ocn830162414
003 - CONTROL NUMBER IDENTIFIER
control field OCoLC
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20240925154536.0
006 - FIXED-LENGTH DATA ELEMENTS--ADDITIONAL MATERIAL CHARACTERISTICS
fixed length control field m d
007 - PHYSICAL DESCRIPTION FIXED FIELD--GENERAL INFORMATION
fixed length control field cr mn|||||||||
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 130316t20132013si a ob 001 0 eng d
040 ## - CATALOGING SOURCE
Original cataloging agency EBLCP
Language of cataloging eng
Description conventions rda
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Transcribing agency EBLCP
Modifying agency OCLCO
-- YDXCP
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066 ## - CHARACTER SETS PRESENT
Alternate G0 or G1 character set (S
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
International Standard Book Number 9781848167551
Qualifying information (electronic bk.)
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
International Standard Book Number 1848167555
Qualifying information (electronic bk.)
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
Canceled/invalid ISBN 9781848167544
Qualifying information (cloth)
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
Canceled/invalid ISBN 1848167547
Qualifying information (cloth)
035 ## - SYSTEM CONTROL NUMBER
System control number 545493
-- (N$T)
035 ## - SYSTEM CONTROL NUMBER
System control number (OCoLC)830162414
050 #4 - LIBRARY OF CONGRESS CALL NUMBER
Classification number RC523
060 #4 - NATIONAL LIBRARY OF MEDICINE CALL NUMBER
Classification number WT 155
072 #7 - SUBJECT CATEGORY CODE
Subject category code HEA
Subject category code subdivision 039140
Source bisacsh
072 #7 - SUBJECT CATEGORY CODE
Subject category code MED
Subject category code subdivision 056000
Source bisacsh
082 04 - DEWEY DECIMAL CLASSIFICATION NUMBER
Classification number 616.831
049 ## - LOCAL HOLDINGS (OCLC)
Holding library MAIN
245 00 - TITLE STATEMENT
Title Alzheimer's disease :
Remainder of title insights into low molecular weight and cytotoxic aggregates from in vitro and computer experiments - molecular basis of amyloid-beta protein aggregation and fibril formation /
Statement of responsibility, etc. Philippe Derreumaux, University of Paris 7, France, editor.
264 #1 - PRODUCTION, PUBLICATION, DISTRIBUTION, MANUFACTURE, AND COPYRIGHT NOTICE
Place of production, publication, distribution, manufacture Singapore :
Name of producer, publisher, distributor, manufacturer World Scientific Publishing Company,
Date of production, publication, distribution, manufacture, or copyright notice [2013]
264 #4 - PRODUCTION, PUBLICATION, DISTRIBUTION, MANUFACTURE, AND COPYRIGHT NOTICE
Date of production, publication, distribution, manufacture, or copyright notice ©2013
300 ## - PHYSICAL DESCRIPTION
Extent 1 online resource (xix, 444 pages) :
Other physical details illustrations.
336 ## - CONTENT TYPE
Content type term text
Content type code txt
Source rdacontent
337 ## - MEDIA TYPE
Media type term computer
Media type code c
Source rdamedia
338 ## - CARRIER TYPE
Carrier type term online resource
Carrier type code cr
Source rdacarrier
490 1# - SERIES STATEMENT
Series statement Molecular Medicine and Medicinal Chemistry ;
Volume/sequential designation v. 7
504 ## - BIBLIOGRAPHY, ETC. NOTE
Bibliography, etc Includes bibliographical references and index.
588 ## - SOURCE OF DESCRIPTION NOTE
Source of description note Description based on print version record.
520 ## - SUMMARY, ETC.
Summary, etc. Alzheimer's disease is the most common form of senile dementia, affecting more than 24 million people worldwide. It is characterised pathologically by abnormally high levels of neurofibrillary tangles resulting from the accumulation of tau protein in dead and dying neurons, and by elevated numbers of senile plaques in the cortex and hippocampus of the brain. The major component of senile plaques is a small protein of 39-43 amino acids called amyloid-? (A?). Thus far, no treatment has been shown to slow the progression of sporadic and familial Alzheimer's disease. A large body of evidence points.
590 ## - LOCAL NOTE (RLIN)
Local note WorldCat record variable field(s) change: 650
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Alzheimer's disease
General subdivision Molecular aspects.
9 (RLIN) 80252
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Alzheimer's disease.
9 (RLIN) 86843
650 12 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Alzheimer Disease
9 (RLIN) 80242
650 #6 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Maladie d'Alzheimer
General subdivision Aspect moléculaire.
9 (RLIN) 1020710
650 #6 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Maladie d'Alzheimer.
9 (RLIN) 969985
650 #7 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element HEALTH & FITNESS
General subdivision Diseases
-- Alzheimer's & Dementia.
Source of heading or term bisacsh
650 #7 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element MEDICAL
General subdivision Neurology.
Source of heading or term bisacsh
650 #7 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Alzheimer's disease
General subdivision Molecular aspects.
Source of heading or term fast
Authority record control number (OCoLC)fst00806550
9 (RLIN) 80252
655 #0 - INDEX TERM--GENRE/FORM
Genre/form data or focus term Electronic books.
9 (RLIN) 396
700 1# - ADDED ENTRY--PERSONAL NAME
Personal name Derreumaux, Philippe,
Relator term editor.
9 (RLIN) 678584
776 08 - ADDITIONAL PHYSICAL FORM ENTRY
Relationship information Print version:
Title Alzheimer's disease.
Place, publisher, and date of publication London : Imperial College Press, [2013]
International Standard Book Number 9781848167544
Record control number (DLC) 2013427093
-- (OCoLC)829952915
830 #0 - SERIES ADDED ENTRY--UNIFORM TITLE
Uniform title Molecular medicine and medicinal chemistry.
9 (RLIN) 583454
856 40 - ELECTRONIC LOCATION AND ACCESS
Materials specified EBSCOhost
Uniform Resource Identifier <a href="https://search.ebscohost.com/login.aspx?direct=true&scope=site&db=nlebk&db=nlabk&AN=545493">https://search.ebscohost.com/login.aspx?direct=true&scope=site&db=nlebk&db=nlabk&AN=545493</a>
880 0# - ALTERNATE GRAPHIC REPRESENTATION
Linkage 505-00/(S
a Amyloid hypothesis: molecular and cellular aspects of toxicity / Rakez Kayed and Cristian A. Lasagna-Reeves -- Models of wild-type and disease-causing mutant β-amyloid fibrils. Insights from solid-state nuclear magnetic resonance spectroscopy / Stephen C. Meredith -- Biophysical characterization of Aβ assembly / Eric Y. Hayden and David B. Teplow -- Coordination of metal ions to β-amyloid peptide: impact on Alzheimer's disease / Peter Faller, Giovanni La Penna, Christelle Hureau and Sara Furlan -- Amyloidogenesis, neurogenesis, learning, and memory in Alzheimer's disease: lessons from transgenic mouse models / Laure Vennet and Claire Rampon -- Inhibitor design against cytotoxic β-amyloid species / Andrew J. Doig -- Kinetics of amyloid growth / Jessica Nasica-Labouze and Normand Mousseau -- Probing the stability of fibril and tubular species using all-atom molecular dynamics simulations in solution: insight into polymorphism / Yifat Miller, Buyong Ma and Ruth Nussinov -- Mechanisms of growth of β-amyloid fibrils and binding of non-steroidal anti-inflammatory drug ligands / Takako Takeda and Dmitri Klimov -- Exploring the structures of β-amyloid oligomers in aqueous solution using coarse-grained protein models / Yassmine Chebaro and Philippe Derreumaux -- Pathways of amyloid fibril formation using a simplified peptide model / Riccardo Pellarin -- From disordered amyloid β-proteins to soluble oligomers and protofibrils using discrete molecular dynamics / Mark Betnel, Nikolay V. Dokholyan and Brigita Urbanc -- Aβ proteins-lipid membrane interaction: computational simulation study / Yuguang Mu -- Molecular insights into the assembly of β-amyloid on surfaces and carbon nanotubes / Guanghong Wei, Yin Luo and Zhaoming Fu -- Inhibiting peptide and protein self-aggregation: what can simulations tell us? / Joan-Emma Shea and Giorgio Colombo.
880 ## - ALTERNATE GRAPHIC REPRESENTATION
Linkage 520-00/(S
a Alzheimer's disease is the most common form of senile dementia, affecting more than 24 million people worldwide. It is characterised pathologically by abnormally high levels of neurofibrillary tangles resulting from the accumulation of tau protein in dead and dying neurons, and by elevated numbers of senile plaques in the cortex and hippocampus of the brain. The major component of senile plaques is a small protein of 39-43 amino acids called amyloid-β (Aβ). Thus far, no treatment has been shown to slow the progression of sporadic and familial Alzheimer's disease.A large body of evidence points, however, to the early Aβ-formed oligomers as the primary toxic species in Alzheimer's disease. A powerful strategy for developing pharmaceutical treatments against Alzheimer's is to elucidate the pathways of oligomer formation and determine the structures of the toxic aggregates.This book provides a panoramic view across recent in vitro and in vivo studies along with state-of-the-art computer simulations, designed to increase the readers' understanding of Aβ oligomerisation and fibril formation. At the same time, the book delves into the pathogenesis of familial and sporadic Alzheimer's disease at the atomic level of detail.Written by leading authors in their respective fields, this book will be valuable to all scientists working on Alzheimer's disease.
938 ## -
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938 ## -
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-- YANK
-- 10258425
994 ## -
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Holdings
Withdrawn status Lost status Damaged status Not for loan Collection code Home library Current library Date acquired Total Checkouts Date last seen Price effective from Koha item type
  Not Lost     EBSCO Medical e-Library e-Library 25/09/2024   25/09/2024 25/09/2024 eBook

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