Amyloid Proteins: The Beta Sheet Conformation and Disease 2 Volume Set

There is increasing evidence that a significant number of clinical disorders involve changes in protein folding. The hallmark of these diseases is the formation of intracellular protein aggregates, the so–called amyloid plaques or fibrils. Progress in amyloid research has now finally provided the link between biochemical cause and pathological effect, opening up new ways of diagnosis and treatment of these severe disorders.
This is the first book to present a systematic overview of all known fibril–forming proteins, including their biochemical characteristics and pathophysiology. It considers the clinically recognized amyloid proteins that are known to be associated with the amyloid protein folding disorders, dealing with their common structural and thermodynamic features that lead to amyloid fibril formation and disease. Emphasis is on the thermodynamics of protein folding, the structure and physiologic effects of common oligomeric and subfibrillar intermediates and the influence of the extracellular matrix and cellular trafficking and metabolism on the genesis and catabolism of beta pleated sheet proteins.
From the contents:Overview of Amyloidosis and Amyloid ProteinsProtein Structure and the Beta Pleated Sheet ConformationProtein Folding, Unfolding and RefoldingPathway to Amyloid Fibril FormationPathophysiology of Amyloid Fibril FormationAmyloid Proteins –– Brain, Systemic, Hormone
The chapters on specific amyloid proteins all follow a common structure, allowing quick access to the desired biochemical and medical data, making this a first–stop reference for clinicians and researchers alike.

Spis treści:
Volume 1.
Preface.
List of Contributors.
Part I: Overview of Amyloidosis and Amyloid Proteins.
1 Amyloidosis and Amyloid Proteins: Brief History and Definitions (Per Westermark).
1.1 Early History.
1.2 Amyloid P roteins – Modern History.
1.3 Classification of Amyloid Diseases.
1.4 What is Amyloid?
Acknowledgments.
References.
2 Anatomic and Clinical Clues to In Vivo Mechanisms of Amyloidogenesis (Vittorio Bellotti, Laura Obici, Robert Kisilevsky and Giampaolo Merlini).
2.1 Introduction.
2.2 AA Amyloidogenesis.
2.3 β<sub>2</sub>–Microglobulin (β<sub>2</sub>M) and the Amyloid Deposition in Hemodialysis.
2.4 Other Amyloid Proteins Display Unique Tissue Specificity.
2.5 Local Production of Amyloidogenic Protein can Dictate the Occurrence of Localized Amyloidosis.
2.6 Conclusions.
Acknowledgments.
References.
Part II: Protein Structure and the Beta Pleated Sheet Conformation.
3 The β–pleated Sheet Conformation and Protein Folding: A Brief History (Jean D. Sipe).
3.1 Introduction.
3.2 The β–pleated Sheet Structure of the Amyloid Fibril.
3.3 Polypeptide Backbone Folding: Steric Considerations.
3.4 Polypeptide Backbone Folding: The Environment.
3.5 Conclusion.
References.
Part III: Protein Folding, Unfolding and Refolding.
4 Thermodynamics and Protein Folding (Ilia V Baskakov).
4.1 Introduction.
4.2 Thermodynamic versus Kinetic Control of Protein Folding.
4.3 What Thermodynamic Forces are Responsible for the Exceptional Stability of Amyloid Aggregates?
4.4 Single Polypeptide Chain–Multiple β–Sheet–rich Abnormal Isoforms.
4.5 Does the Process of Prion Propagation Differ from Formation of Ordered Amyloid Aggregates?
4.6 Prion Propagation is an Autocatalytic Process.
4.7 Conformational Diversity of Self–propagating Prion Aggregates.
4.8 High Species Specificity of Prion Propagation.
4.9 Conclusions.
References.
5 Role of Post–transla tional Chemical Modifications in Amyloid Fibril Formation (Melanie R. Nilsson).
5.1 Introduction.
5.2 Common Modifications that May Play a Significant Role In Vivo.
5.3 Proposed Mechanisms by which Chemical Modifications may Affect Amyloid Deposition.
5.4 Conclusions and Future Directions.
Acknowledgments.
References.
6 Lipid Modulators of Protein Misfolding and Aggregation (Christopher A. MacRaild and Geoffrey J. Howlett).
6.1 Introduction.
6.2 Protein Folding and Aggregation at Lipid Surfaces.
6.3 Lipid Oxidation and Amyloid Formation.
6.4 Apolipoproteins and Amyloid.
6.5 The Effect of Lipids on the Stability of Apolipoproteins.
6.6 Summary.
Acknowledgments.
References.
7 Extracellular Matrix Heparan Sulfate Proteoglycans (Peter J. Neame and John T. Gallagher).
7.1 Introduction.
7.2 Protein Folding and Glycosaminoglycans.
7.3 β–Sheets.
7.4 Proteoglycans.
7.5 Heparin, Heparan Sulfate and Other Glycosaminoglycans.
7.6 Heparin–Heparan Sulfate Interactions with Protein.
7.7 Amyloid Proteins and Peptides.
7.8 Heparan Sulfate and Amyloid.
7.9 Conclusion.
7.10 Future Directions.
Acknowledgments.
References.
8 Serum Amyloid P Component (David C. Kilpatrick).
8.1 Introduction to Pentraxins.
8.2 Structure of SAP.
8.3 Lectin and Other Biological Activities of SAP.
8.4 SAP: Its Physiological Role in Health.
8.5 SAP: Its Role in Disease.
References.
9 Serum amyloid P Component – Structural Features and Amyloid Recognition (S. P. Wood and A. R. Coker).
9.1 Introduction.
9.2 Amyloid Fibrils and their Formation.
9.3 The Structure of SAP.
9.4 The Calcium–binding Site.
9.5 Comparative studies of CRP.
9.6 SAP Structure in the Absence of Calcium.
9.7 Binding of Small Molecule Ligands to SAP.
9.8 The Role of Glycosaminoglycans (GAGs).
9.9 SAP , Protein Folding and Amyloid Fibril Formation.
9.10 Perspective.
References.
10 Apolipoprotein E: Structural and Functional Interactions with Amyloid β (W. Blaine Stine Jr. and Mary Jo LaDu).
10.1 Introduction.
10.2 ApoΕ Background.
10.3 ApoΕ and Aβ.
10.4 Other Aβ Binding Proteins.
Acknowledgments.
References.
Part IV: Pathway to Amyloid Fibril Formation.
11 Pathways to Amyloid Fibril Formation: Partially Folded Intermediates in the Fibrillation of Natively Unfolded Proteins (Vladimir N. Uversky and Anthony L. Fink).
11.1 Introduction.
11.2 Molecular Mechanisms of Amyloid Fibril Formation by a Natively Unfolded Protein: α–Synuclein.
11.3 Fibrillogenesis of Natively Unfolded Proteins Requires Partial Folding.
11.4 Fibrillation of Proteins Unrelated to Conformational Disease.
11.5 Conclusions.
Acknowledgments.
References.
12 Structural Intermediates of Globular Proteins as Precursors to Amyloid Formation (Daniel F. Moriarty and Wilfredo Colón).
12.1 Introduction.
12.2 Protein Folding.
12.3 Folding Intermediates as Precursors to Protein Aggregation.
12.4 Structural Intermediates in Amyloid Formation.
12.5 Factors that Favor the Formation of Amyloidogenic Intermediates.
12.6 Mechanism of Amyloid Formation.
12.7 An “Eye” for an “I”: Inhibiting the Formation of Intermediates.
12.8 Conclusion.
References.
13 Computational Approaches and Tools for Establishing Structural Models for Short Amyloid–forming Peptides (Nurit Haspel, David Zanuy, Hui–Hsu (Gavin) Tsai, Buyong Ma, Haim Wolfson and Ruth Nussinov).
13.1 Introduction.
13.2 Computational Tools in the Service of Amyloid Structure Prediction.
13.3 Constructing Amyloid Models.
13.4 The Calcitonin Pentapeptide System: Bulk Organizati