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http://purl.uniprot.org/citations/14741212http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14741212http://www.w3.org/2000/01/rdf-schema#comment"The cystatins were the first amyloidogenic proteins to be shown to oligomerize through a 3D domain swapping mechanism. Here we show that, under conditions leading to the formation of amyloid deposits, the domain-swapped dimer of chicken cystatin further oligomerizes to a tetramer, prior to fibrillization. The tetramer has a very similar circular dichroism and fluorescence signature to the folded monomer and dimer structures, but exhibits some loss of dispersion in the 1H-NMR spectrum. 8-Anilino-1-naphthalene sulfonate fluorescence enhancement indicates an increase in the degree of disorder. While the dimerization reaction is bimolecular and most likely limited by the availability of a predominantly unfolded form of the monomer, the tetramerization reaction is first-order. The tetramer is formed slowly (t(1/2)=six days at 85 degrees C), dimeric cystatin is the precursor to tetramer formation, and thus the rate is limited by structural rearrangement within the dimer. Some higher-order oligomerization events parallel tetramer formation while others follow from the tetrameric form. Thus, the tetramer is a transient intermediate within the pathway of large-scale oligomerization."xsd:string
http://purl.uniprot.org/citations/14741212http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2003.12.011"xsd:string
http://purl.uniprot.org/citations/14741212http://purl.uniprot.org/core/author"Conroy M.J."xsd:string
http://purl.uniprot.org/citations/14741212http://purl.uniprot.org/core/author"Hounslow A.M."xsd:string
http://purl.uniprot.org/citations/14741212http://purl.uniprot.org/core/author"Sanders A."xsd:string
http://purl.uniprot.org/citations/14741212http://purl.uniprot.org/core/author"Waltho J.P."xsd:string
http://purl.uniprot.org/citations/14741212http://purl.uniprot.org/core/author"Giannini S."xsd:string
http://purl.uniprot.org/citations/14741212http://purl.uniprot.org/core/author"Higgins L.D."xsd:string
http://purl.uniprot.org/citations/14741212http://purl.uniprot.org/core/author"Staniforth R.A."xsd:string
http://purl.uniprot.org/citations/14741212http://purl.uniprot.org/core/author"Jeremy Craven C."xsd:string
http://purl.uniprot.org/citations/14741212http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14741212http://purl.uniprot.org/core/name"J Mol Biol"xsd:string
http://purl.uniprot.org/citations/14741212http://purl.uniprot.org/core/pages"165-178"xsd:string
http://purl.uniprot.org/citations/14741212http://purl.uniprot.org/core/title"Cystatin forms a tetramer through structural rearrangement of domain-swapped dimers prior to amyloidogenesis."xsd:string
http://purl.uniprot.org/citations/14741212http://purl.uniprot.org/core/volume"336"xsd:string
http://purl.uniprot.org/citations/14741212http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14741212
http://purl.uniprot.org/citations/14741212http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/14741212
http://purl.uniprot.org/uniprot/#_P01038-mappedCitation-14741212http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/14741212
http://purl.uniprot.org/uniprot/P01038http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/14741212