| http://purl.uniprot.org/citations/23551356 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23551356 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23551356 | http://www.w3.org/2000/01/rdf-schema#comment | "The enzyme l-asparaginase of Pyrococcus furiosus (PfA) functions as a dimer with each monomer consisting of distinct N- and C-terminal domains (NPfA and CPfA, respectively), connected by a linker. Here we present data to show that NPfA functions as a non-specific molecular chaperone. Independently expressed NPfA refolded spontaneously whereas CPfA formed insoluble aggregates. However, when mixed and refolded together, NPfA augmented CPfA to fold with ~90% recovery. NPfA also protected a variety of substrate proteins from thermal and refolding-mediated aggregation as monitored by a reduction in light scattering. The co-appearance of substrate protein with NPfA in antibody pull-down assays as well as in eluted gel filtration peaks indicated direct protein-protein interaction. These interactions were hydrophobic in nature as determined by 8-anilino-1-naphthalene sulfonic acid fluorescence. NPfA inhibited polyglutamine-mediated amyloid formation and also facilitated disintegration of preformed amyloid fibrils of amyloid-β (1-42) as determined by reverse-phase HPLC-based sedimentation assay and thioflavin T binding assays, respectively. Dynamic light scattering experiments suggested that NPfA readily assembled into polydispersed oligomeric species. With no sequence similarity to α-crystallin or any known molecular chaperone, we present here NPfA as a novel molecular chaperone."xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.org/dc/terms/identifier | "doi:10.1111/febs.12271"xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.org/dc/terms/identifier | "doi:10.1111/febs.12271"xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/author | "Mishra R."xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/author | "Mishra R."xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/author | "Garg D.K."xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/author | "Garg D.K."xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/author | "Kundu B."xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/author | "Kundu B."xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/author | "Thakur A.K."xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/author | "Thakur A.K."xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/author | "Tomar R."xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/author | "Tomar R."xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/name | "FEBS J."xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/name | "FEBS J."xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/pages | "2688-2699"xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/pages | "2688-2699"xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/title | "N-terminal domain of Pyrococcus furiosus L-asparaginase functions as a non-specific, stable, molecular chaperone."xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/title | "N-terminal domain of Pyrococcus furiosus L-asparaginase functions as a non-specific, stable, molecular chaperone."xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/volume | "280"xsd:string |
| http://purl.uniprot.org/citations/23551356 | http://purl.uniprot.org/core/volume | "280"xsd:string |