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dc.contributor.authorKabir, Md Tanvir
dc.contributor.authorUddin, Md Sahab
dc.contributor.authorAbdeen, Ahmed
dc.contributor.authorAshraf, Ghulam Md
dc.contributor.authorPerveen, Asma
dc.contributor.authorHafeez, Abdul
dc.contributor.authorBin-Jumah, May N
dc.contributor.authorAbdel-Daim, Mohamed M
dc.date.accessioned2022-05-02T22:52:15Z
dc.date.available2022-05-02T22:52:15Z
dc.date.issued2020
dc.identifier.issn1568-0266
dc.identifier.doi10.2174/1568026620666200618114924
dc.identifier.urihttp://hdl.handle.net/10072/414229
dc.description.abstractSeveral proteolytic systems including ubiquitin (Ub)-proteasome system (UPS), chaperone-mediated autophagy (CMA), and macroautophagy are used by the mammalian cells to remove misfolded proteins (MPs). UPS mediates degradation of most of the MPs, where Ub-conjugated substrates are deu-biquitinated, unfolded, and passed through the proteasome’s narrow chamber, and eventually break into smaller peptides. It has been observed that the substrates that show a specific degradation signal, the KFERQ sequence motif, can be delivered to and go through CMA-mediated degradation in lysosomes. Macroautophagy can help in the degradation of substrates that are prone to aggregation and resistant to both the CMA and UPS. In the aforesaid case, cargoes are separated into autophagosomes before lysosomal hydrolase-mediated degradation. Even though the majority of the aggregated and MPs in the human proteome can be removed via cellular protein quality control (PQC), some mutant and native proteins tend to aggregate into β-sheet-rich oligomers that exhibit resistance to all identified proteolytic processes and can, therefore, grow into extracellular plaques or inclusion bodies. Indeed, the buildup of protease-resistant aggregated and MPs is a usual process underlying various protein misfolding disorders, including neurodegenerative diseases (NDs) for example Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, amyotrophic lateral sclerosis, and prion diseases. In this article, we have focused on the contribution of PQC in the degradation of pathogenic proteins in NDs.
dc.description.peerreviewedYes
dc.languageEnglish
dc.publisherBentham Science Publishers
dc.relation.ispartofpagefrom2025
dc.relation.ispartofpageto2043
dc.relation.ispartofissue23
dc.relation.ispartofjournalCurrent Topics in Medicinal Chemistry
dc.relation.ispartofvolume20
dc.subject.fieldofresearchMedicinal and biomolecular chemistry
dc.subject.fieldofresearchPharmacology and pharmaceutical sciences
dc.subject.fieldofresearchcode3404
dc.subject.fieldofresearchcode3214
dc.subject.keywordsScience & Technology
dc.subject.keywordsLife Sciences & Biomedicine
dc.subject.keywordsChemistry, Medicinal
dc.subject.keywordsPharmacology & Pharmacy
dc.subject.keywordsProtein misfolding
dc.titleEvidence linking protein misfolding to quality control in progressive neurodegenerative diseases
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationKabir, MT; Uddin, MS; Abdeen, A; Ashraf, GM; Perveen, A; Hafeez, A; Bin-Jumah, MN; Abdel-Daim, MM, Evidence linking protein misfolding to quality control in progressive neurodegenerative diseases, Current Topics in Medicinal Chemistry, 2020, 20 (23), pp. 2025-2043
dcterms.dateAccepted2020-05-05
dc.date.updated2022-04-27T05:38:13Z
gro.hasfulltextNo Full Text
gro.griffith.authorKabir, Md. Tanvir


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