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dc.contributor.authorRanaweera, CB
dc.date.accessioned2024-05-16T03:08:35Z
dc.date.available2024-05-16T03:08:35Z
dc.date.issued2024-03-01
dc.identifier.urihttp://ir.kdu.ac.lk/handle/345/7551
dc.description.abstractProtein 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 diseasesen_US
dc.language.isoenen_US
dc.subjectneurodegenerative 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 aggregationen_US
dc.titleChaperones to the Rescue: Tackling Neurodegenerative Diseases and Potential Therapeutic Applicationsen_US
dc.typeFeature articleen_US
dc.identifier.facultyFaculty of Allied Health Sciencesen_US
dc.identifier.journalInstitute of Biology E news letteren_US
dc.identifier.issue4en_US
dc.identifier.volume4en_US
dc.identifier.databasehttps://www.iobsl.org/newslettersen_US
dc.identifier.pgnos22-26en_US


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