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Prions and Diseases (Record no. 103229)

MARC details
000 -LEADER
fixed length control field 05805nam a22005175i 4500
001 - CONTROL NUMBER
control field 978-3-031-20565-1
003 - CONTROL NUMBER IDENTIFIER
control field DE-He213
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20240729135749.0
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 221228s2023 sz | s |||| 0|eng d
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
ISBN 9783031205651
-- 978-3-031-20565-1
072 #7 - SUBJECT CATEGORY CODE
Subject category code PSAN
Source bicssc
072 #7 - SUBJECT CATEGORY CODE
Subject category code MED057000
Source bisacsh
072 #7 - SUBJECT CATEGORY CODE
Subject category code PSAN
Source thema
245 10 - TITLE STATEMENT
Title Prions and Diseases
250 ## - EDITION
Edition statement 2nd ed. 2023.
264 #1 - PRODUCTION, PUBLICATION, DISTRIBUTION, MANUFACTURE, AND COPYRIGHT NOTICE
Place of production, publication, distribution, manufacture Cham :
Name of producer, publisher, distributor, manufacturer Springer International Publishing :
-- Imprint: Springer,
Date of production, publication, distribution, manufacture, or copyright notice 2023.
300 ## - PHYSICAL DESCRIPTION
Physical description XII, 793 p. 81 illus., 62 illus. in color.
Other physical details online resource.
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
505 0# - CONTENTS
Contents Part I: HISTORY -- Chapter 1: Transmissible Spongiform Encephalopathy: from its beginnings to Daniel Carleton Gajdusek -- Part II: GENERAL ASPECTS OF PRIONS -- Chapter 2: The Rich Chemistry of the Copper and Zinc Sites in Cellular Prion Protein -- Chapter 3: Mammalian Prion Structures -- Chapter 4: Insoluble Cellular Prion Protein and Other Neurodegeneration-related Misfolded Protein Aggregates in the Brain of Asymptomatic Individuals -- Part III: CONVERSION AND STRAIN OF PRIONS -- Chapter 5: Prion Conversion and Deformed Templating -- Chapter 6: Prion Strain Interference -- Chapter 7: Molecular Mechanisms Encoding Strains of Prions and Prion-Like Misfolded Proteins -- Chapter 8: Cofactor Involvement in Prion Propagation -- Chapter 9: Prion Protein Conversion and Lipids -- Part IV: ENVIRONMENT AND TRANSMISSION OF PRIONS -- Chapter 10: Prions in the Environment -- Chapter 11: Environmentally Acquired Transmissible Spongiform Encephalopathy -- Chapter 12: Risk of Transmission of Creutzfeldt-Jakob Disease by Blood Transfusion -- Chapter 13: Species Barriers in Prion Disease -- Part V: MODELLING OF PRIONS -- Chapter 14: Modeling the Cell Biology of Prions -- Chapter 15: Transgenic Mice Modelling in Prion Diseases -- Chapter 16: Stem Cell Models in Prion Research -- Chapter 17: Drosophila Models of Prion Diseases -- Part VI: HUMAN PRION DISEASES AND OTHER PATHOLOGIES -- Chapter 18: Human Sporadic Prion Diseases -- Chapter 19 Genetic Creutzfeldt-Jakob and Gerstmann-Str�ussler-Scheinker Diseases -- Chapter 20: Glycoform-selective Prions in Sporadic and Inherited Variably Protease-sensitive Prionopathies -- Chapter 21: The Spectrum of Tau Pathology in Human Prion Disease -- Chapter 22: Prion Protein Complex with mGluR5 Mediates Amyloid-� Synaptic Loss in Alzheimer's Disease -- Chapter 23: Prion and Cancers -- Chapter 24: Protective Role of Cellular Prion Protein in Tissue Ischemic/Reperfusion Injury -- Part VII: ANIMAL PRION DISEASES -- Chapter 25: Bovine Spongiform Encephalopathy -- Chapter 26: Classical and Atypical Scrapie in Sheep and Goats -- Chapter 27: Research models for studying chronic wasting disease -- Part VIII: YEAST PRIONS -- Chapter 28: Introduction to Yeast and Fungal Prions -- Chapter 29: Yeast Prions Are Folded, In-Register Parallel Amyloids Subject to Multiple Anti-prion Systems -- Part IX: DIAGNOSIS AND HUMAN PRION SURVEILLANCE -- Chapter 30: Real-time quaking-induced conversion (QuIC) assays for the detection and diagnosis of human prion diseases -- Chapter 31: Protein Misfolding Cyclic Amplification -- Chapter 32: Skin Misfolded Proteins as Biomarkers for Diagnosis of Prion and Prion-like Diseases -- Chapter 33: Diagnosis of Prion Disease: Conventional Approaches -- Chapter 34: Human Prion Disease Surveillance -- Part X: TREATMENT -- Chapter 35: Overview on Treatment of Prion Diseases and Decontamination of Prions -- Chapter 36: Gene Therapy Strategies for Prophylactic and Therapeutic Treatments of Human Prion Diseases -- Chapter 37: Immunomodulation.
520 ## - ABSTRACT
Abstract Transmissible spongiform encephalopathies (TSE), now known as prion diseases, have been recognized for nearly 300 years in animals and almost 100 years in humans. Modern studies, including protein-misfolding cyclic amplification (PMCA), have greatly advanced our understanding of the pathogenesis of prion diseases and facilitated the identification of new prion diseases in animals and humans. In the second edition of Prions and Diseases, more than 60 leading researchers and clinicians worldwide provide an up-to-date discussion of these unique infectious pathogens and their associated diseases. The book provides up-to-date knowledge about the etiology, pathogenesis, classification, histopathological, and clinical aspects of the full range of animal and human prion diseases. As a result, the book contains the most authoritative views about the past, present, and future of prions and prion diseases covering fresh perspectives on important emerging topics such as inherited human prion disease, stem-cell models in prion research, human prion disease surveillance, and gene therapy strategies.
650 #0 - SUBJECT HEADINGS
Subject term Neurosciences.
650 #0 - SUBJECT HEADINGS
Subject term Human physiology.
650 #0 - SUBJECT HEADINGS
Subject term Neurology�.
650 #0 - SUBJECT HEADINGS
Subject term Life sciences.
650 #0 - SUBJECT HEADINGS
Subject term Physiology.
9 (RLIN) 7429
650 14 - SUBJECT HEADINGS
Subject term Neuroscience.
650 24 - SUBJECT HEADINGS
Subject term Human Physiology.
650 24 - SUBJECT HEADINGS
Subject term Neurology.
650 24 - SUBJECT HEADINGS
Subject term Life Sciences.
650 24 - SUBJECT HEADINGS
Subject term Animal Physiology.
650 24 - SUBJECT HEADINGS
Subject term Life Sciences.
700 1# - ADDED PERSONAL NAME
Added personal author Zou, Wen-Quan.
Relator term editor.
700 1# - ADDED PERSONAL NAME
Added personal author Gambetti, Pierluigi.
Relator term editor.
710 2# - ADDED CORPORATE NAME
Added corporate author SpringerLink (Online service)
856 ## - ONLINE RESOURCE
Uniform Resource Identifier <a href="#gotoholdings">#gotoholdings</a>
Link text Access resource
245 ## - TITLE STATEMENT
Medium [E-Book]
347 ## - DIGITAL FILE CHARACTERISTICS
File type text file
Encoding format PDF
Source rda
912 ## -
-- ZDB-2-SBL
912 ## -
-- ZDB-2-SXB
Holdings
Withdrawn status Lost status Damaged status Not for loan Home library Current library Shelving location Date acquired Source of acquisition Total Checkouts Date last seen Uniform Resource Identifier Price effective from Koha item type
        Hillingdon Hospitals Library Services (Hillingdon Hospitals NHS Foundation) Hillingdon Hospitals Library Services (Hillingdon Hospitals NHS Foundation) Online 02/05/2024 Springer BiomedLifeSc_2023   02/05/2024 https://go.openathens.net/redirector/nhs?url=https://doi.org/10.1007/978-3-031-20565-1 02/05/2024 Electronic book
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