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http://purl.uniprot.org/citations/36493755http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/36493755http://www.w3.org/2000/01/rdf-schema#comment"The ATP-dependent ring-shaped chaperonin TRiC/CCT is essential for cellular proteostasis. To uncover why some eukaryotic proteins can only fold with TRiC assistance, we reconstituted the folding of β-tubulin using human prefoldin and TRiC. We find unstructured β-tubulin is delivered by prefoldin to the open TRiC chamber followed by ATP-dependent chamber closure. Cryo-EM resolves four near-atomic-resolution structures containing progressively folded β-tubulin intermediates within the closed TRiC chamber, culminating in native tubulin. This substrate folding pathway appears closely guided by site-specific interactions with conserved regions in the TRiC chamber. Initial electrostatic interactions between the TRiC interior wall and both the folded tubulin N domain and its C-terminal E-hook tail establish the native substrate topology, thus enabling C-domain folding. Intrinsically disordered CCT C termini within the chamber promote subsequent folding of tubulin's core and middle domains and GTP-binding. Thus, TRiC's chamber provides chemical and topological directives that shape the folding landscape of its obligate substrates."xsd:string
http://purl.uniprot.org/citations/36493755http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2022.11.014"xsd:string
http://purl.uniprot.org/citations/36493755http://purl.uniprot.org/core/author"Chiu W."xsd:string
http://purl.uniprot.org/citations/36493755http://purl.uniprot.org/core/author"Ma B."xsd:string
http://purl.uniprot.org/citations/36493755http://purl.uniprot.org/core/author"Park J."xsd:string
http://purl.uniprot.org/citations/36493755http://purl.uniprot.org/core/author"Zhao Y."xsd:string
http://purl.uniprot.org/citations/36493755http://purl.uniprot.org/core/author"Leitner A."xsd:string
http://purl.uniprot.org/citations/36493755http://purl.uniprot.org/core/author"Roh S.H."xsd:string
http://purl.uniprot.org/citations/36493755http://purl.uniprot.org/core/author"Frydman J."xsd:string
http://purl.uniprot.org/citations/36493755http://purl.uniprot.org/core/author"Pintilie G."xsd:string
http://purl.uniprot.org/citations/36493755http://purl.uniprot.org/core/author"Collier M."xsd:string
http://purl.uniprot.org/citations/36493755http://purl.uniprot.org/core/author"Gestaut D."xsd:string
http://purl.uniprot.org/citations/36493755http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/36493755http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/36493755http://purl.uniprot.org/core/pages"4770-4787.e20"xsd:string
http://purl.uniprot.org/citations/36493755http://purl.uniprot.org/core/title"Structural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT."xsd:string
http://purl.uniprot.org/citations/36493755http://purl.uniprot.org/core/volume"185"xsd:string
http://purl.uniprot.org/citations/36493755http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/36493755
http://purl.uniprot.org/citations/36493755http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/36493755
http://purl.uniprot.org/uniprot/#_P61758-mappedCitation-36493755http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/36493755
http://purl.uniprot.org/uniprot/#_O15212-mappedCitation-36493755http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/36493755
http://purl.uniprot.org/uniprot/#_P40227-mappedCitation-36493755http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/36493755
http://purl.uniprot.org/uniprot/#_P17987-mappedCitation-36493755http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/36493755
http://purl.uniprot.org/uniprot/#_P50990-mappedCitation-36493755http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/36493755