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dc.contributor.authorRyan, Philip
dc.contributor.authorXu, Mingming
dc.contributor.authorDavey, Andrew K
dc.contributor.authorDanon, Jonathan J
dc.contributor.authorMellick, George D
dc.contributor.authorKassiou, Michael
dc.contributor.authorRudrawar, Santosh
dc.date.accessioned2019-09-10T02:45:53Z
dc.date.available2019-09-10T02:45:53Z
dc.date.issued2019
dc.identifier.issn1948-7193
dc.identifier.doi10.1021/acschemneuro.9b00143
dc.identifier.urihttp://hdl.handle.net/10072/387158
dc.description.abstractPost-translational modifications (PTMs) of proteins are becoming the focus of intense research due to their implications in a broad spectrum of neurodegenerative diseases. Various PTMs have been identified to alter the toxic profiles of proteins which play critical roles in disease etiology. In Alzheimer’s disease (AD), dysregulated phosphorylation is reported to promote pathogenic processing of the microtubule-associated tau protein. Among the PTMs, the enzymatic addition of N-acetyl-d-glucosamine (GlcNAc) residues to Ser/Thr residues is reported to deliver protective effects against the pathogenic processing of both amyloid precursor protein (APP) and tau. Modification of tau with as few as one single O-GlcNAc residue inhibits its toxic self-assembly. This modification also has the same effect on the assembly of the Parkinson’s disease (PD) associated α-synuclein (ASyn) protein. In fact, O-GlcNAcylation (O-linked GlcNAc modification) affects the processing of numerous proteins implicated in AD, PD, amyotrophic lateral sclerosis (ALS), and Huntington’s disease (HD) in a similar manner. As such, manipulation of a protein’s O-GlcNAcylation status has been proposed to offer therapeutic routes toward addressing multiple neurodegenerative pathologies. Here we review the various effects that O-GlcNAc modification, and its modulated expression, have on pathogenically significant proteins involved in neurodegenerative disease.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherAmerican Chemical Society
dc.relation.ispartofpagefrom2209
dc.relation.ispartofpageto2221
dc.relation.ispartofissue5
dc.relation.ispartofjournalACS Chemical Neuroscience
dc.relation.ispartofvolume10
dc.subject.fieldofresearchMedicinal and Biomolecular Chemistry
dc.subject.fieldofresearchcode0304
dc.subject.keywordsScience & Technology
dc.subject.keywordsLife Sciences & Biomedicine
dc.subject.keywordsBiochemistry & Molecular Biology
dc.subject.keywordsChemistry, Medicinal
dc.subject.keywordsNeurosciences
dc.titleO-GlcNAc Modification Protects against Protein Misfolding and Aggregation in Neurodegenerative Disease
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationRyan, P; Xu, M; Davey, AK; Danon, JJ; Mellick, GD; Kassiou, M; Rudrawar, S, O-GlcNAc Modification Protects against Protein Misfolding and Aggregation in Neurodegenerative Disease, ACS Chemical Neuroscience, 2019, 10 (5), pp. 2209-2221
dc.date.updated2019-09-10T02:43:44Z
gro.hasfulltextNo Full Text
gro.griffith.authorRudrawar, Santosh
gro.griffith.authorXu, Manny
gro.griffith.authorDavey, Andrew
gro.griffith.authorMellick, George


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