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http://purl.uniprot.org/SHA-384/810746655D19B04F8DC9B4FA89255893A3D9B2185BC3BE098367277B0AD703123D489DA50FCEDC1E97112288E6C2CD6Bhttp://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/810746655D19B04F8DC9B4FA89255893A3D9B2185BC3BE098367277B0AD703123D489DA50FCEDC1E97112288E6C2CD6Bhttp://www.w3.org/2000/01/rdf-schema#comment"Inhibition of chaperone ATPase (Hsp104) by gadolinium chloride (GdHCl) leads to reduced aggregation of the protein. Under in vitro conditions trehalose is able to restore the GdHCl-induced loss of ATPase activity of recombinant Hsp104 to its original level. Inactivation of Hsp104 at the stage when oligomers have already been formed increases the rate of formation of aggregates by inhibiting disaggregation of oligomers."xsd:string
http://purl.uniprot.org/uniprot/#_1F0339C0550004DA0311D9255287F134F6FBD3C9D9F26EAE9F3E6EBEFC01282A0B84F89C2CB53B16F16E5816373AB81Bhttp://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/810746655D19B04F8DC9B4FA89255893A3D9B2185BC3BE098367277B0AD703123D489DA50FCEDC1E97112288E6C2CD6B
http://purl.uniprot.org/uniprot/P31539http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/810746655D19B04F8DC9B4FA89255893A3D9B2185BC3BE098367277B0AD703123D489DA50FCEDC1E97112288E6C2CD6B
http://purl.uniprot.org/uniprot/#_P31539-mappedCitation-29860440http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/810746655D19B04F8DC9B4FA89255893A3D9B2185BC3BE098367277B0AD703123D489DA50FCEDC1E97112288E6C2CD6B