dc.contributor.author | Ranaweera, CB | |
dc.date.accessioned | 2024-05-16T03:08:35Z | |
dc.date.available | 2024-05-16T03:08:35Z | |
dc.date.issued | 2024-03-01 | |
dc.identifier.uri | http://ir.kdu.ac.lk/handle/345/7551 | |
dc.description.abstract | Protein misfolding has been identified as a
contributing factor in several
neurodegenerative conditions, such as
Alzheimer's disease (AD), Huntington's disease
(HD), Amyotrophic Lateral Sclerosis (ALS), and
Parkinson’s disease (PD). One common
characteristic observed among individuals
affected by these illnesses is the aggregation
of deposits consisting of misfolded proteins.
The occurrence of abnormal protein folding
can lead to toxicity by either impairing or
enhancing protein function, or both. One
promising treatment strategy for these
diseases is to use protein-remodeling factors
to correct misfolded proteins and restore
protein structure and function back to its
native state. Hence, the interaction between
chaperones and protein folding/degradation
pathways plays a vital role in developing novel
therapeutic drugs for these neurodegenerative
diseases | en_US |
dc.language.iso | en | en_US |
dc.subject | neurodegenerative conditions, such as Alzheimer's disease (AD), Huntington's disease (HD), Amyotrophic Lateral Sclerosis (ALS), and Parkinson’s disease (PD), Molecular Chaperones, ClpB, Hsp 104, Protein misfolding, Protein aggregation | en_US |
dc.title | Chaperones to the Rescue: Tackling Neurodegenerative Diseases and Potential Therapeutic Applications | en_US |
dc.type | Feature article | en_US |
dc.identifier.faculty | Faculty of Allied Health Sciences | en_US |
dc.identifier.journal | Institute of Biology E news letter | en_US |
dc.identifier.issue | 4 | en_US |
dc.identifier.volume | 4 | en_US |
dc.identifier.database | https://www.iobsl.org/newsletters | en_US |
dc.identifier.pgnos | 22-26 | en_US |