dc.contributor.authorGallart-Palau, Xavier
dc.contributor.authorSerra, Aida
dc.contributor.authorSze, Siu Kwan
dc.date.accessioned2015-12-16T07:07:04Z
dc.date.available2015-12-16T07:07:04Z
dc.date.issued2015
dc.identifier.citationGallart-Palau, X., Serra, A., & Sze, S. K. Uncovering Neurodegenerative Protein Modifications via Proteomic Profiling. International Review of Neurobiology, 121, 87-116.en_US
dc.identifier.urihttp://hdl.handle.net/10220/39090
dc.description.abstractDegenerative protein modifications (DPMs) are caused by nonenzymatic chemical reactions that induce changes in protein structure and function which promote disease initiation, pathological progression and also natural aging. These undesirable DPMs include oxidation, carbonylation, carbamylation, glycation, deamidation, isomerization, nitration, and racemization, which impart deleterious structural and functional changes on extracellular matrix proteins and long-lived cell types such as cardiomyocytes and neurons, leading to impaired overall organ function. Despite the obvious clinical importance of understanding DPM biology, the molecular mechanisms that mediate these modifications remain poorly understood largely due to the technical challenges associated with their study. However, recent advances in mass spectrometry-based proteomics technologies now permit global quantitative proteomic profiling of cell lines, animal models, and human clinical samples from a variety of different patient types. These new methods have not only uncovered changes in global protein expression levels but have also identified specific modifications of particular amino acid residues in protein backbones that are associated with disease progression. The nonenzymatic induction of DPMs as revealed by proteomic profiling can help us to better understand the underlying molecular pathology of protein dysfunction in human diseases and natural aging. This chapter discusses recent progress in understanding how proteomic profiling of patient samples derived from the central nervous system can elucidate the DPM biology of human neurodegenerative diseases.en_US
dc.description.sponsorshipNMRC (Natl Medical Research Council, S’pore)en_US
dc.format.extent36 p.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesInternational Review of Neurobiologyen_US
dc.rights© 2015 Elsevier Inc. This is the author created version of a work that has been peer reviewed and accepted for publication by International Review of Neurobiology, Elsevier Inc. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1016/bs.irn.2015.06.002].en_US
dc.subjectProtein dysfunctionsen_US
dc.subjectNeurodegenerationen_US
dc.subjectDementiaen_US
dc.subjectMass spectrometryen_US
dc.subjectPosttranslational modificationsen_US
dc.titleUncovering Neurodegenerative Protein Modifications via Proteomic Profilingen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1016/bs.irn.2015.06.002
dc.description.versionAccepted versionen_US


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