title: Protein folding and misfolding in the neurodegenerative disorders: a review.
abstract: Protein misfolding is an intrinsic aspect of normal folding within the complex cellular environment. Its effects are minimized in living system by the action of a range of protective mechanisms including molecular chaperones and quality control systems. According to the current growing research, protein misfolding is a recognized key feature of most neurodegenerative diseases. Extensive biochemical, neuropathological, and genetic evidence suggest that the cerebral accumulation of amyloid fibrils is the central event in the pathogenesis of neurodegenerative disorders. In the first part of this review we have discussed the general course of action of folding and misfolding of the proteins. Later part of this review gives an outline regarding the role of protein misfolding in the molecular and cellular mechanisms in the pathogenesis of Alzheimer's and Parkinson along with their treatment possibilities. Finally, we have mentioned about the recent findings in neurodegenerative diseases.
authors.affiliation: Laboratory of Biotechnology, Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER), Gauhati Medical College, 781032 Bhangagarh, Guwahati, Assam, India. Electronic address: nbolshette@gmail.com.
authors.forename: N B
authors.initials: NB
authors.lastname: Bolshette
authors.affiliation: Laboratory of Biotechnology, Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER), Gauhati Medical College, 781032 Bhangagarh, Guwahati, Assam, India.
authors.forename: K K
authors.initials: KK
authors.lastname: Thakur
authors.affiliation: Laboratory of Biotechnology, Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER), Gauhati Medical College, 781032 Bhangagarh, Guwahati, Assam, India.
authors.forename: A P
authors.initials: AP
authors.lastname: Bidkar
authors.affiliation: Faculty of Medicine, University of Medicine and Pharmacy"Iuliu Hatieganu", 400349 Cluj-Napoca, Romania.
authors.forename: C
authors.initials: C
authors.lastname: Trandafir
authors.affiliation: Laboratory of Molecular Pharmacology and Toxicology, Department of Pharmacology and Toxicology, National Institute of Pharmaceutical Education and Research (NIPER), Gauhati Medical College, 781032 Guwahati, Assam, India.
authors.forename: P
authors.initials: P
authors.lastname: Kumar
authors.affiliation: Laboratory of Biotechnology, Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER), Gauhati Medical College, 781032 Bhangagarh, Guwahati, Assam, India.
authors.forename: R
authors.initials: R
authors.lastname: Gogoi
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism* / Q000628:therapy; D053829:Amyloid Precursor Protein Secretases / Q000502:physiology; D016229:Amyloid beta-Peptides / Q000378:metabolism; D001343:Autophagy; D006360:Heat-Shock Proteins / Q000502:physiology; D006801:Humans; D018832:Molecular Chaperones / Q000502:physiology; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D019636:Neurodegenerative Diseases / Q000378:metabolism*; D016874:Neurofibrillary Tangles / Q000378:metabolism; D010300:Parkinson Disease / Q000378:metabolism* / Q000628:therapy; D010766:Phosphorylation; D058225:Plaque, Amyloid / Q000378:metabolism; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D054875:Ubiquitination; D056811:Unfolded Protein Response; D051844:alpha-Synuclein / Q000502:physiology
chemical_list: D016229:Amyloid beta-Peptides; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D009419:Nerve Tissue Proteins; D051844:alpha-Synuclein; D053829:Amyloid Precursor Protein Secretases; D046988:Proteasome Endopeptidase Complex
keywords: Alzheimer; Amyloid-β; Amyloïde-β; Molecular chaperone; Protein folding; Protéine chapérone; Repliement de protéine; α-synuclein; α-synucléine