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http://purl.uniprot.org/citations/22200570http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22200570http://www.w3.org/2000/01/rdf-schema#comment"Abstract Hyperhomocysteinemia has recently been identified as an important risk factor for Alzheimer's disease (AD). One of the potential mechanisms underlying harmful effects of homocysteine (Hcy) is site-specific acylation of proteins at lysine residues by homocysteine thiolactone (HCTL). The accumulation of amyloid β-peptide (Aβ) in the brain is a neuropathological hallmark of AD. In the present study we were interested to investigate the effects of N-homocysteinylation on the aggregation propensity and neurotoxicity of Aβ(1-42). By coupling several techniques, we demonstrated that the homocysteinylation of lysine residues increase the neurotoxicity of the Aβ peptide by stabilizing soluble oligomeric intermediates."xsd:string
http://purl.uniprot.org/citations/22200570http://purl.org/dc/terms/identifier"doi:10.1016/j.febslet.2011.12.018"xsd:string
http://purl.uniprot.org/citations/22200570http://purl.uniprot.org/core/author"Ahmadian S."xsd:string
http://purl.uniprot.org/citations/22200570http://purl.uniprot.org/core/author"Aryapour H."xsd:string
http://purl.uniprot.org/citations/22200570http://purl.uniprot.org/core/author"Hoveizi E."xsd:string
http://purl.uniprot.org/citations/22200570http://purl.uniprot.org/core/author"Karima O."xsd:string
http://purl.uniprot.org/citations/22200570http://purl.uniprot.org/core/author"Khodadadi S."xsd:string
http://purl.uniprot.org/citations/22200570http://purl.uniprot.org/core/author"Riazi G.H."xsd:string
http://purl.uniprot.org/citations/22200570http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22200570http://purl.uniprot.org/core/name"FEBS Lett"xsd:string
http://purl.uniprot.org/citations/22200570http://purl.uniprot.org/core/pages"127-131"xsd:string
http://purl.uniprot.org/citations/22200570http://purl.uniprot.org/core/title"Effect of N-homocysteinylation on physicochemical and cytotoxic properties of amyloid beta-peptide."xsd:string
http://purl.uniprot.org/citations/22200570http://purl.uniprot.org/core/volume"586"xsd:string
http://purl.uniprot.org/citations/22200570http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22200570
http://purl.uniprot.org/citations/22200570http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22200570
http://purl.uniprot.org/uniprot/P05067#attribution-E0D5EA728AA8BE887FB9D4D403D67AE8http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/22200570
http://purl.uniprot.org/uniprot/#_A0A0A0MRG2-mappedCitation-22200570http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22200570
http://purl.uniprot.org/uniprot/#_A0A140VJC8-mappedCitation-22200570http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22200570
http://purl.uniprot.org/uniprot/#_A0A218KGR2-mappedCitation-22200570http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22200570
http://purl.uniprot.org/uniprot/#_A0A8F9R5D5-mappedCitation-22200570http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22200570
http://purl.uniprot.org/uniprot/#_B4DGD0-mappedCitation-22200570http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22200570
http://purl.uniprot.org/uniprot/#_B4DMD5-mappedCitation-22200570http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22200570
http://purl.uniprot.org/uniprot/#_B4DQM1-mappedCitation-22200570http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22200570
http://purl.uniprot.org/uniprot/#_B4DM00-mappedCitation-22200570http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22200570