Guide Misbehaving Proteins: Protein (MIS) Folding, Aggregation, and Stability

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Therefore, pathogenesis of neurodegenerative diseases is commonly driven by the dysfunction of corresponding IDPs, and the normal and pathogenic behavior of such disease-related IDPs are controlled by other IDPs.

Misbehaving Proteins

The author declares that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. I am thankful to Alexey Uversky for careful reading and editing this manuscript. Ajroud-Driss, S. Sporadic and hereditary amyotrophic lateral sclerosis ALS. Acta , — Barmada, S. Bellotti, V. Biological activity and pathological implications of misfolded proteins. Life Sci. Bentmann, E. FEBS J. Bonda, D. The sirtuin pathway in ageing and Alzheimer disease: mechanistic and therapeutic considerations.

Lancet Neurol. Breydo, L. Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases. Metallomics 3, — Bukau, B. Molecular chaperones and protein quality control.

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Cell , — Buljan, M. Alternative splicing of intrinsically disordered regions and rewiring of protein interactions. Tissue-specific splicing of disordered segments that embed binding motifs rewires protein interaction networks. Cell 46, — Chatr-Aryamontri, A. Nucleic Acids Res. Collins, M. Phosphoproteomic analysis of the mouse brain cytosol reveals a predominance of protein phosphorylation in regions of intrinsic sequence disorder. Proteomics 7, — Costantini, S. Genealogy of an ancient protein family: the Sirtuins, a family of disordered members. BMC Evol. Cozzetto, D. The contribution of intrinsic disorder prediction to the elucidation of protein function.

Cuanalo-Contreras, K. Role of protein misfolding and proteostasis deficiency in protein misfolding diseases and aging. Cell Biol. Dev, K. Part II: alpha-synuclein and its molecular pathophysiological role in neurodegenerative disease. Neuropharmacology 45, 14— Dobson, C. Protein misfolding, evolution and disease.

Trends Biochem. Dosztanyi, Z. Disorder and sequence repeats in hub proteins and their implications for network evolution.


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Proteome Res. Dunker, A. Flexible nets: the roles of intrinsic disorder in protein interaction networks. Intrinsically disordered protein. Dyson, H. Intrinsically unstructured proteins and their functions.

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Ekman, D. What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae?


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    Misbehaving Proteins: Protein (Mis)Folding, Aggregation, and Stability / Edition 1

    Hasegawa, T. Haynes, C. Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes. PLoS Comput. Hipp, M. Proteostasis impairment in protein-misfolding and -aggregation diseases. Trends Cell Biol. Hsu, W. Exploring the binding diversity of intrinsically disordered proteins involved in one-to-many binding. Protein Sci. Jeong, H. Kelly, J. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Kurotani, A.

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    Prions-What are they ? Protein Misfolding Mechanism

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    BMC Genomics 9 Suppl.

    This provides a safe, isolated place for the protein to refold before being ejected. Instead, Hartl says, chaperones that sequester unfolded proteins from the distracting, packed environment inside the cell act more like a catalyst. He suspects that the structural intermediates adopted by proteins on the way to their final 3-D conformation that scientists have observed in test tubes are likely also present during the folding process inside GroEL.