The Resource Alzheimer's Disease : Insights into Low Molecular Weight and Cytotoxic Aggregates from in Vitro and Computer Experiments - Molecular Basis of Amyloid-Beta Protein Aggregation and Fibril Formation, (electronic resource)

Alzheimer's Disease : Insights into Low Molecular Weight and Cytotoxic Aggregates from in Vitro and Computer Experiments - Molecular Basis of Amyloid-Beta Protein Aggregation and Fibril Formation, (electronic resource)

Label
Alzheimer's Disease : Insights into Low Molecular Weight and Cytotoxic Aggregates from in Vitro and Computer Experiments - Molecular Basis of Amyloid-Beta Protein Aggregation and Fibril Formation
Title
Alzheimer's Disease
Title remainder
Insights into Low Molecular Weight and Cytotoxic Aggregates from in Vitro and Computer Experiments - Molecular Basis of Amyloid-Beta Protein Aggregation and Fibril Formation
Title variation
  • Alzheimer’s disease
  • Alzheimer''s Disease
  • Molecular Medicine And Medicinal Chemistry vol. 7
  • ALZHEIMER'S DISEASE
Creator
Subject
Genre
Language
eng
Summary
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
Member of
Cataloging source
AU-PeEL
http://library.link/vocab/creatorName
Derreumaux, Philippe
Dewey number
616.831
LC call number
RC523
Nature of contents
dictionaries
Series statement
Molecular Medicine and Medicinal Chemistry
Series volume
v.7
http://library.link/vocab/subjectName
  • Alzheimer's disease -- Molecular aspects
  • Alzheimer's disease -- Treatment
  • Alzheimer's disease
Label
Alzheimer's Disease : Insights into Low Molecular Weight and Cytotoxic Aggregates from in Vitro and Computer Experiments - Molecular Basis of Amyloid-Beta Protein Aggregation and Fibril Formation, (electronic resource)
Instantiates
Publication
Note
Description based upon print version of record
Contents
  • Contents; Preface; Part A. Cellular and In Vitro Aspects of Amyloid-Beta (Aβ) Aggregation; 1. Amyloid Hypothesis:Molecular and Cellular Aspects of Toxicity Rakez Kayed and Cristian A. Lasagna-Reeves; 1.1 Introduction; 1.2 Mechanism Involved in β-Amyloid Oligomer Toxicity; 1.2.1 Receptor-mediated β-amyloid oligomer neurotoxicity; 1.2.2 Impairment of the cellular membrane by β-amyloid oligomers; 1.2.3 Intracellular β-amyloid oligomer toxicity; 1.3 Concluding Remarks; References
  • 2. Models of Wild-Type and Disease-Causing Mutant β-Amyloid Fibrils. Insights from Solid-State Nuclear Magnetic Resonance Spectroscopy Stephen C. Meredith2.1 The Scope of the Problem: Protein Aggregation and Protein Aggregation Diseases; 2.2 Basic Principles of Solid-State Nuclear Magnetic Resonance for Studying Amyloid; 2.3 Information that can be Obtained about Amyloid from Solid-State Nuclear Magnetic Resonance; 2.4 Structures of Wild-Type β-Amyloid Fibrils from Solid-State Nuclear Magnetic Resonance
  • 2.5 Structures of Wild-Type β-Amyloid Oligomers from Solid-State Nuclear Magnetic Resonance2.6 A Core Domain of β-Amyloid Peptides?; 2.7 Disease-Causing Mutations within β-Amyloid Itself; (a) Dutch mutation, E693Q-APP (E22Q-Aβ); (b) Arctic mutation, E693G-APP (E22G-Aβ); (c) Italian mutation, E693K-APP (E22K-Aβ); (d) Flemish mutation, A692G-APP (A21G-Aβ); (e) Iowa mutation, D694N-APP (D23N-Aβ); (f ) Japanese mutation E693-APP, (E22-Aβ); (g) English mutation, H677R-APP (H6R-Aβ), and Tottorimutation, D678NAPP(D7N-Aβ)
  • 2.8 Solid-State Nuclear Magnetic Resonance Spectroscopy of Mutant β-Amyloid Peptides(a) The Iowa mutation, D23N-Aβ; (b) The Italian mutation, E22K-Aβ; (c) The Japanese mutation, E22-Aβ; References; 3. Biophysical Characterization of Aβ Assembly Eric Y. Hayden and David B. Teplow; 3.1 Preface; 3.2 Introduction; 3.3 The Amyloid Fibril; 3.3.1 Fibril morphology; 3.3.2 X-ray fiber diffraction; 3.3.3 X-ray crystallography; 3.3.4 Nuclear magnetic resonance spectroscopy; 3.3.5 Hydrogen/deuterium exchange; 3.3.6 Secondary structure of fibrils; 3.3.7 Toxicity of fibrils; 3.4 Protofibrils
  • 3.4.1 Protofibril structure and growth3.4.2 Biological activity of protofibrils; 3.5 Oligomers; 3.5.1 Oligomers and sodium dodecyl sulfate-polyacrylamide gel electrophoresis; 3.5.2 Quantitative determination of the oligomer size frequency distribution; 3.5.3 Studying Aβ assembly in the gas phase; 3.5.4 Oligomer structure-activity relationships; 3.5.5 The "oligomer cascade hypothesis"; 3.5.6 Statistical biophysics and "the most toxic oligomer"; 3.6 Conformational Dynamics of the Aβ Monomer; 3.6.1 The Aβ(21-30) turn region; 3.6.2 Differences in Aβ40 and Aβ42 monomer dynamics
  • 3.6.3 Scanning Tyr mutagenesis
Dimensions
unknown
Extent
1 online resource (465 p.)
Form of item
electronic
Isbn
9781848167544
Specific material designation
remote
System control number
  • (CKB)2560000000099447
  • (EBL)1143306
  • (OCoLC)830162414
Label
Alzheimer's Disease : Insights into Low Molecular Weight and Cytotoxic Aggregates from in Vitro and Computer Experiments - Molecular Basis of Amyloid-Beta Protein Aggregation and Fibril Formation, (electronic resource)
Publication
Note
Description based upon print version of record
Contents
  • Contents; Preface; Part A. Cellular and In Vitro Aspects of Amyloid-Beta (Aβ) Aggregation; 1. Amyloid Hypothesis:Molecular and Cellular Aspects of Toxicity Rakez Kayed and Cristian A. Lasagna-Reeves; 1.1 Introduction; 1.2 Mechanism Involved in β-Amyloid Oligomer Toxicity; 1.2.1 Receptor-mediated β-amyloid oligomer neurotoxicity; 1.2.2 Impairment of the cellular membrane by β-amyloid oligomers; 1.2.3 Intracellular β-amyloid oligomer toxicity; 1.3 Concluding Remarks; References
  • 2. Models of Wild-Type and Disease-Causing Mutant β-Amyloid Fibrils. Insights from Solid-State Nuclear Magnetic Resonance Spectroscopy Stephen C. Meredith2.1 The Scope of the Problem: Protein Aggregation and Protein Aggregation Diseases; 2.2 Basic Principles of Solid-State Nuclear Magnetic Resonance for Studying Amyloid; 2.3 Information that can be Obtained about Amyloid from Solid-State Nuclear Magnetic Resonance; 2.4 Structures of Wild-Type β-Amyloid Fibrils from Solid-State Nuclear Magnetic Resonance
  • 2.5 Structures of Wild-Type β-Amyloid Oligomers from Solid-State Nuclear Magnetic Resonance2.6 A Core Domain of β-Amyloid Peptides?; 2.7 Disease-Causing Mutations within β-Amyloid Itself; (a) Dutch mutation, E693Q-APP (E22Q-Aβ); (b) Arctic mutation, E693G-APP (E22G-Aβ); (c) Italian mutation, E693K-APP (E22K-Aβ); (d) Flemish mutation, A692G-APP (A21G-Aβ); (e) Iowa mutation, D694N-APP (D23N-Aβ); (f ) Japanese mutation E693-APP, (E22-Aβ); (g) English mutation, H677R-APP (H6R-Aβ), and Tottorimutation, D678NAPP(D7N-Aβ)
  • 2.8 Solid-State Nuclear Magnetic Resonance Spectroscopy of Mutant β-Amyloid Peptides(a) The Iowa mutation, D23N-Aβ; (b) The Italian mutation, E22K-Aβ; (c) The Japanese mutation, E22-Aβ; References; 3. Biophysical Characterization of Aβ Assembly Eric Y. Hayden and David B. Teplow; 3.1 Preface; 3.2 Introduction; 3.3 The Amyloid Fibril; 3.3.1 Fibril morphology; 3.3.2 X-ray fiber diffraction; 3.3.3 X-ray crystallography; 3.3.4 Nuclear magnetic resonance spectroscopy; 3.3.5 Hydrogen/deuterium exchange; 3.3.6 Secondary structure of fibrils; 3.3.7 Toxicity of fibrils; 3.4 Protofibrils
  • 3.4.1 Protofibril structure and growth3.4.2 Biological activity of protofibrils; 3.5 Oligomers; 3.5.1 Oligomers and sodium dodecyl sulfate-polyacrylamide gel electrophoresis; 3.5.2 Quantitative determination of the oligomer size frequency distribution; 3.5.3 Studying Aβ assembly in the gas phase; 3.5.4 Oligomer structure-activity relationships; 3.5.5 The "oligomer cascade hypothesis"; 3.5.6 Statistical biophysics and "the most toxic oligomer"; 3.6 Conformational Dynamics of the Aβ Monomer; 3.6.1 The Aβ(21-30) turn region; 3.6.2 Differences in Aβ40 and Aβ42 monomer dynamics
  • 3.6.3 Scanning Tyr mutagenesis
Dimensions
unknown
Extent
1 online resource (465 p.)
Form of item
electronic
Isbn
9781848167544
Specific material designation
remote
System control number
  • (CKB)2560000000099447
  • (EBL)1143306
  • (OCoLC)830162414

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