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Amyloid Proteins
The Beta Sheet Conformation and Disease
2-Volume Set
edited by Jean D. Sipe

Amyloid Proteins is a first-stop reference on proteins associated with amyloidosis.


  • Present a systematic overview of all known fibril-forming proteins, including their biochemical characteristics and pathophysiology
  • Considers the clinically recognized amyloid proteins that are known to be associated with the amyloid protein folding disorders
  • 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


Amyloidosis and Amyloid Proteins: Brief History and Definitions

  • Early History.
  • Amyloid Proteins – Modern History.
  • Classification of Amyloid Diseases.
  • What is Amyloid

Anatomic and Clinical Clues to In Vivo Mechanisms of Amyloidogenesis

  • AA Amyloidogenesis.
  • β2-Microglobulin (β2M) and the Amyloid Deposition in Hemodialysis.
  • Other Amyloid Proteins Display Unique Tissue Specificity.
  • Local Production of Amyloidogenic Protein can Dictate the Occurrence of Localized Amyloidosis

The β-pleated Sheet Conformation and Protein Folding: A Brief History

  • The β-pleated Sheet Structure of the Amyloid Fibril
  • Polypeptide Backbone Folding: Steric Considerations
  • Polypeptide Backbone Folding: The Environment

Thermodynamics and Protein Folding

  • Thermodynamic versus Kinetic Control of Protein Folding
  • What Thermodynamic Forces are Responsible for the Exceptional Stability of Amyloid Aggregates
  • Single Polypeptide Chain–Multiple β-Sheet-rich Abnormal Isoforms
  • Does the Process of Prion Propagation Differ from Formation of Ordered Amyloid Aggregate
  • Prion Propagation is an Autocatalytic Process
  • Conformational Diversity of Self-propagating Prion Aggregates
  • High Species Specificity of Prion Propagation

Role of Post-translational Chemical Modifications in Amyloid Fibril Formation

  • Common Modifications that May Play a Significant Role In Vivo
  • Proposed Mechanisms by which Chemical Modifications may Affect Amyloid Deposition

Lipid Modulators of Protein Misfolding and Aggregation

  • Protein Folding and Aggregation at Lipid Surfaces
  • Lipid Oxidation and Amyloid Formation
  • Apolipoproteins and Amyloid
  • The Effect of Lipids on the Stability of Apolipoproteins

Extracellular Matrix Heparan Sulfate Proteoglycans

  • Protein Folding and Glycosaminoglycans
  • β-Sheets
  • Proteoglycans
  • Heparin, Heparan Sulfate and Other Glycosaminoglycans
  • Heparin–Heparan Sulfate Interactions with Protein
  • Amyloid Proteins and Peptides
  • Heparan Sulfate and Amyloid

Serum Amyloid P Component

  • Structure of SAP
  • Lectin and Other Biological Activities of SAP
  • SAP: Its Physiological Role in Health
  • SAP: Its Role in Disease

Serum amyloid P Component – Structural Features and Amyloid Recognition

  • Amyloid Fibrils and their Formation
  • The Structure of SAP
  • The Calcium-binding Site
  • Comparative studies of CRP
  • SAP Structure in the Absence of Calcium
  • Binding of Small Molecule Ligands to SAP
  • The Role of Glycosaminoglycans (GAGs)
  • SAP, Protein Folding and Amyloid Fibril Formation

Apolipoprotein E: Structural and Functional Interactions with Amyloid &beta

  • ApoΕ Background
  • ApoΕ and A&beta
  • Other Aβ Binding Proteins

Pathways to Amyloid Fibril Formation: Partially Folded Intermediates in the Fibrillation of Natively Unfolded Proteins

  • Molecular Mechanisms of Amyloid Fibril Formation by a Natively Unfolded Protein: α-Synuclein
  • Fibrillogenesis of Natively Unfolded Proteins Requires Partial Folding
  • Fibrillation of Proteins Unrelated to Conformational Disease

Structural Intermediates of Globular Proteins as Precursors to Amyloid Formation

  • Protein Folding
  • Folding Intermediates as Precursors to Protein Aggregation
  • Structural Intermediates in Amyloid Formation
  • Factors that Favor the Formation of Amyloidogenic Intermediates
  • Mechanism of Amyloid Formation
  • An “Eye” for an “I”: Inhibiting the Formation of Intermediates

Computational Approaches and Tools for Establishing Structural Models for Short Amyloid-forming Peptides

  • Computational Tools in the Service of Amyloid Structure Prediction
  • Constructing Amyloid Models
  • The Calcitonin Pentapeptide System: Bulk Organization and Interactions
  • Calcitonin Mutation Study: Simulation and Prediction of Specific Changes in Amino Acids
  • DFNKF Amyloid Seed and its Stability and Dynamics

Oligomers and Cellular Toxicity

  • Aggregation
  • Cellular Mechanisms of Oligomeric Toxicity
  • Loss of Function Hypothesis
  • Receptors for Advanced End-products of Glycation (RAGE) Receptors
  • Oxidative Stress
  • The Channel Hypothesis
  • A&beta
  • PrP106–126
  • IAPP
  • ANP
  • SAA
  • AS
  • β2M
  • AL Amyloidosis
  • PG
  • HypF
  • Calcitonin (CT)
  • Lysozyme

The Future of Molecular Diagnostics and Targeted Therapeutics in the Amyloidoses

  • Early Diagnosis of Amyloid Diseases
  • Accurate Classification of Amyloid Diseases
  • Non-invasive Staging of Amyloid Diseases
  • Targeted Therapeutics of Amyloid Diseases
  • Amyloid Disease Prevention

Brain Dysfunction Associated with Amyloid Fibrils and Other Aggregated Proteins

  • Neuropathology
  • The Neurotoxic Proteins

The Amyloid β Protein

  • Aβ, AD and Amyloid
  • Pathogenetic Process – Biology
  • Normal Physiologic Function of AβPP and A&beta
  • Genetic Evidence for a Role of Aβ in AD
  • Pathogenetic Process – Biophysics
  • Identification of Therapeutic Targets
  • Current Therapies for AD

Prion Protein

  • Conformations of PrPC and PrPSc.
  • Stability and Unfolding/Folding of PrPC in vitro
  • Mechanisms of Prion Replication In Vivo

Familial British and Danish Dementias

  • FBD and FDD
  • A Novel Gene BRI2
  • BRI2 Mutations Generate Two New Amyloid Subunits, ABri and ADan
  • Biochemical Properties of Amyloid Subunits ABri and ADan
  • Soluble Forms of ABri and ADan in Biological Fluid
  • Unique Features of FBD or FDD
  • Potential Implications of FBD and FDD for Alzheimer’s Disease


  • Amyloidosis (AL)
  • Physicochemistry of Antibody Light Chains
  • Database of Dyscrasia-related Variable Domain Sequences
  • Amyloidosis (AH)
  • Immunoproteomics


  • Gene Structure and Regulation
  • Function
  • Three-dimensional Structure of TTR
  • TTR Amyloidosis (ATTR)
  • TTR Amyloid Inhibitors
  • Ligand Binding
  • Post-translational Modifications
  • Evolution

High-Density Lipoprotein Amyloid Proteins

  • SAA [Secondary, Reactive, Amyloid A (AA) Amyloidosis]
  • ApoAI Amyloidosis
  • ApoAII Amyloidosis


  • Physiology, Pathology and Genetics
  • Mechanism of Amyloid Formation by Gelsolin


  • Lysozyme in Healthy Subjects
  • Clinical Manifestations of Lysozyme Amyloidosis
  • Characteristics of Ex Vivo and In Vitro Amyloid Fibrils
  • In Vitro Studies of the Properties of the Variant Lysozymes
  • Mechanism of Fibril Formation


  • Clinical Manifestations
  • The Fibrinogen Molecule
  • The Various AFib Mutations and Related Peptides
  • Mechanisms of AFib Amyloidosis


  • Current Knowledge of the Mechanism of Development of DRA In Vivo
  • Structure and Morphology of β2M Amyloid Fibrils
  • Structural Characteristics of Monomeric Fibril Precursor States

Cystatin C

  • Biochemical and Physiological Characteristics
  • Cystatin C Oligomers In Vivo and In Vitro
  • The Phenomenon of Three-dimensional Domain Swapping
  • The Cystatin Fold
  • Three-dimensional Domain Swapping in Full-length Cystatin C
  • Three-dimensional Domain Swapping in N-truncated Cystatin C
  • Structural Implications for L68Q Cystatin C
  • Higher Oligomers Observed by Crystallography and Other Methods
  • In Vivo Amyloid Deposits Containing Cystatin C
  • Formation of Cystatin C Amyloid Fibrils In Vitro
  • Inhibition of Dimerization and Fibril Formation by Protein Engineering
  • Inhibition of Dimerization by Monoclonal Antibodies and Carboxymethylpapain

Endocrine Amyloid

  • Nomenclature for Endocrine Amyloid
  • When and Why do Proteins form Amyloid
  • Amyloid in Cardiac Atria
  • Endocrine Amyloid in the Thyroid
  • Amyloid Deposits in the Pituitary
  • Endocrine Amyloid in the Islets of Langerhans
  • Insulin as an Amyloid-forming Protein
  • Can Other Islet Hormones Aggregate and Form Amyloid
  • Other Amyloids with Possible Endocrine Origin


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Amyloid Proteins
The Beta Sheet Conformation and Disease
2-Volume Set
edited by Jean D. Sipe

2005 • 799 pages • $469.00 + shipping
Texas residents please add 6.75 % sales tax

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