Protein folding and misfolding: neurodegenerative diseases
The main focus of this volume is to review the molecular events initiated by unfolded or misfolded proteins leading to conformational human diseases, with special emphasis on the macromolecular homo- and heteroassociations of the malfolded proteins into characteristic ultrastructures found primarily in Parkinson's and Alzheimer's diseases. This book reviews the structural knowledge accumulated for well-studied and for newly discovered proteins involved in paradigmatic conformational disorders with the aim to broaden our understanding of the pathomechanisms of neurodegeneration, which is crucial for finding effective therapeutic interventions that could prevent or circumvent the development of neurodegenerative disorders in humans.
1. Structural Disorder and Its Connection with Misfolding Diseases; Veronika Csizmok and Peter Tompa. 1.1 The Concept of Protein Disorder. 1.2 Biophysical and Bioinformatics Characterization of Disorder. 1.2.1 Biophysical Techniques 1.2.2 Bioinformatics Techniques. 1.3 Disorder in Vivo, the Effect of Crowding? 1.4 Disorder and Aggregation. 1.5 Disorder in Neurodegenerative Diseases. 1.6 Physiological Prions. 1.7 Structural Transition to Amyloid: Partially Folded Intermediates. 1.8 The Structure of Amyloid: Cross-Beta Models and Flexibility. 1.9 Conclusions. References. 2 Intrinsic Disorder in Proteins Associated with Neurodegenerative Diseases Vladimir N. Uversky. 2.1 Neurodegenerative Diseases as Proteinopathies. 2.2 Introducing Intrinsically Disordered Proteins. 2.2.1 Concept. 2.2.2 Experimental Techniques for IDP Detection. 2.2.3 Sequence Peculiarities of IDPs and Predictors of Intrinsic Disorder. 2.2.4 Abundance of IDPs and their Functions. 2.3Abundance of IDPs in Neurodegenerative Diseases. Evidence from the Bioinformatics Analyses. 2.4 Intrinsic Disorder in Proteins Associated with -Protein and Alzheimer's Disease. 2.4.2 Neurodegenerative Diseases. 2.4.1 Amyloid Tau Protein in Alzheimer's Disease and Other Tauopathies. 2.4.3 Prion Protein and Prion Diseases. 2.4.4 Synucleins - and Synuclein and Synucleinopathies. 2.4.5 Parkinson's Disease and Dementia with Lewy Bodies. 2.4.6 Polyglutamine Repeat Diseases and Huntingtin, Ataxin-1, Ataxin-3, androgen Receptor and Atrophin-1. 2.4.7 Abri Peptide and Familial British Dementia. 2.4.8 Adan in Familial Danish Dementia. 2.4.9 Glial Fibrillary Acidic Protein and Alexander and Alpers Disease. 2.4.11DNA Disease. 2.4.10 Mitochondrial DNA Polymerase Excision Repair Protein ERCC-6 and Cockayne Syndrome. 2.4.12 Survival of Motor Neurons Protein and Spinal Muscular Atrophy. 2.5 Concluding Remarks: Another Illustration of the D2 Concept. References. 3 Dynamic Role of Ubiquitination in the Management of Misfolded Proteins
- 2009, 278 Seiten, Maße: 16 x 24,1 cm, Gebunden, Englisch
- Herausgegeben:Ovádi, Judit; Orosz, Ferenc
- Herausgegeben: Ferenc Orosz, Judit Ovádi
- Verlag: Springer Netherlands
- ISBN-10: 1402094337
- ISBN-13: 9781402094330
- Erscheinungsdatum: 15.01.2009
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