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· 분류 : 외국도서 > 과학/수학/생태 > 과학 > 생명과학 > 생화학
· ISBN : 9783527328604
· 쪽수 : 296쪽
· 출판일 : 2011-05-16
목차
Preface.
List of Contributors.
1 Interactions of a-Synuclein with Lipids and Artificial Membranes Monitored by ESIPT Probes (Volodymyr V. Shvadchak, Lisandro J. Falomir- Lockhart, Dmytro A. Yushchenko, and Thomas M. Jovin).
1.1 Introduction to Parkinson's Disease and a-Synuclein.
1.2 Structural Biology of a-Synuclein.
1.3 Methods for Studying AS–Lipid Interactions.
1.4 AS–Lipid Interactions.
1.5 Interactions of Monomeric AS with Artificial Membranes Monitored with ESIPT Probes.
1.6 Aggregation of AS and the Effects of Fatty Acids Monitored with ESIPT Probes.
1.7 Concluding Remarks.
References.
2 Structural and Functional Insights into a-Synuclein–Lipid Interactions (Martin Stöckl, Bart D. van Rooijen, Mireille M.A.E Claessens, and Vinod Subramaniam).
2.1 Introduction.
2.2 Interaction of a-Synuclein with Model Membrane Systems.
2.3 Biological Significance.
References.
3 Surfactants and Alcohols as Inducers of Protein Amyloid: Aggregation Chaperones or Membrane Simulators? (Daniel E. Otzen).
3.1 Introduction.
3.2 Aggregation in the Presence of Surfactants.
3.3 Palimpsests of Future Functions: Cytotoxic Protein–Lipid Complexes.
3.4 Aggregation in Fluorinated Organic Solvents.
3.5 From Mimetics to the Real Thing: Aggregation on Lipids.
3.6 Summary.
References.
4 Interaction of hIAPP and Its Precursors with Model and Biological Membranes (Katrin Weise, Rajesh Mishra, Suman Jha, Daniel Sellin, Diana Radovan, Andrea Gohlke, Christoph Jeworrek, Janine Seeliger, Simone Möbitz, and Roland Winter).
4.1 Introduction.
4.2 Results.
4.3 Conclusions.
References.
5 Amyloid Polymorphisms: Structural Basis and Significance in Biology and Molecular Medicine (Massimo Stefani).
5.1 Introduction.
5.2 Only Generic Data Are Currently Available on the Structural Features of Amyloid Oligomers.
5.3 The Plasma Membrane Can Be a Primary Site of Amyloid Oligomer Generation and Interaction.
5.4 Oligomer/Fibril Polymorphism Can Underlie Amyloid Cytotoxicity.
5.5 Amyloid Oligomers Grown Under Different Conditions Can Display Variable Cytotoxicity by Interacting in Different Ways with the Cell Membranes.
5.6 Conclusions.
References.
6 Intracellular Amyloid ß: a Modification to the Amyloid Hypothesis in Alzheimer.s Disease (Yan Zhang).
6.1 Introduction.
6.2 Evidence for the Presence of Intracellular Amyloid.
6.3 Sources of Intracellular Amyloid.
6.4 Relationship Between Intracellular and Extracelluar Amyloid.
6.5 Prevention of Intracellular Amyloid Toxicity.
6.6 Concluding Remarks.
6.7 Disclosure Statement.
References.
7 Lipid Rafts Play a Crucial Role in Protein Interactions and Intracellular Signaling Involved in Neuronal Preservation Against Alzheimer.s Disease (Raquel Marin).
7.1 Lipid Rafts: Keys to Signaling Platforms in Neurons.
7.2 Estrogen Receptors Are Part of Signaling Platforms in Neuronal Rafts.
7.3 Role of Lipid Raft ERa–VDAC Interactions in Neuronal Preservation Against Ab Toxicity.
7.4 Disruption of ERa–VDAC Complex in AD Brains.
7.5 Future Studies.
References.
8 Alzheimer's Disease as a Membrane-Associated Enzymopathy of ß-Amyloid Precursor Protein (APP) Secretases (Saori Hata, Yuhki Saito, and Toshiharu Suzuki).
8.1 Introduction.
8.2 Intramembrane-Cleaving Enzyme of Type I Membrane Proteins.
8.3 Alcadein Processing by ?-Secretase in Alzheimer.s Disease.
References.
9 Impaired Regulation of Glutamate Receptor Channels and Signaling Molecules by ß-Amyloid in Alzheimer's Disease (Zhen Yan).
9.1 Introduction.
9.2 AMPAR-Mediated Synaptic Transmission and Ionic Current are Impaired by Aß.
9.3 CaMKII is Causally Involved in Ab Impairment of AMPAR Trafficking and Function.
9.4 PIP2 Regulation of NMDAR Currents is Lost by Aß.
9.5 The Effect of AChE Inhibitor on NMDAR Response is Impaired in APP Transgenic Mice.
9.6 Aß Impairs PKC-Dependent Signaling and Functions.
9.7 Conclusion.
References.
10 Membrane Changes in BSE and Scrapie (Cecilie Ersdal, Gillian McGovern, and Martin Jeffrey).
10.1 Prion Diseases.
10.2 The Cellular Prion Protein (PrPc) and Conversion to Disease-Associated Prion Protein (PrPd).
10.3 PrPd Accumulation in the Central Nervous System and Lymphatic Tissues.
10.4 Aberrant Endocytosis and Trafficking of PrPd in Neurons and Tingible Body Macrophages.
10.5 Abnormal Maturation Cycle and Immune Complex Trapping of Follicular Dendritic Cells in Lymphoid Germinal Centers.
10.6 Molecular Changes of Plasma Membranes Associated with PrPd Accumulation.
10.7 Transfer of PrPd Between Cells.
10.8 Extracellular Amyloid Form of PrPd.
10.9 Strain-Directed Effects of Prion Infection.
10.10 Conclusion and Perspectives.
10.11 Summary.
References.
11 Interaction of Alzheimer Amyloid Peptide with Cell Surfaces and Artificial Membranes (David A. Bateman and Avijit Chakrabartty).
11.1 Introduction.
11.2 Comparison of the Neurotoxicity of Oligomeric and Fibrillar Alzheimer Amyloid Peptides.
11.3 Aß Oligomerization at the Cell Surface.
11.4 Catalysis of Aß Oligomerization by the Cell Surface.
11.5 Type of Aß Complexes that Form on the Cell Surface.
11.6 Association of Alzheimer Amyloid Peptides with Lipid Particles.
11.7 Future Directions.
References.
12 Experimental Approaches and Technical Challenges for Studying Amyloid–Membrane Interactions (Raz Jelinek and Tania Sheynis).
12.1 Introduction.
12.2 Unilamellar Vesicles and Micelles.
12.3 Black Lipid Membranes.
12.4 Langmuir Monolayers.
12.5 Solid-Supported Bilayers.
12.6 Other Techniques.
12.7 Challenges and Future Work.
References.
Index.
