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Rev Neurol (Paris). 2014 Mar;170(3):151-61. doi: 10.1016/j.neurol.2013.11.002. Epub 2014 Mar 7.

Protein folding and misfolding in the neurodegenerative disorders: a review.

Author information

1
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.
2
Laboratory of Biotechnology, Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER), Gauhati Medical College, 781032 Bhangagarh, Guwahati, Assam, India.
3
Faculty of Medicine, University of Medicine and Pharmacy"Iuliu Hatieganu", 400349 Cluj-Napoca, Romania.
4
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.

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.

KEYWORDS:

Alzheimer; Amyloid-β; Amyloïde-β; Molecular chaperone; Protein folding; Protéine chapérone; Repliement de protéine; α-synuclein; α-synucléine

PMID:
24613386
DOI:
10.1016/j.neurol.2013.11.002
[Indexed for MEDLINE]
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