| http://purl.uniprot.org/citations/19469552 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19469552 | http://www.w3.org/2000/01/rdf-schema#comment | "Human PDCD5 protein is a novel programmed cell death-promoting molecule. However, the function of Ymr074cP, a S. cerevisiae homologue of hPDCD5, is still unknown. Heteronuclear NMR methods were used to determine the solution structure of the N-terminal 116-residue fragment (N116) of Ymr074cP protein. N116 is shown to be a heterogeneous ensemble of flexibly folded conformations, adopting an extended triple-helix bundle fold that is connected to a mobile but structured alpha-helix in the N-terminus by means of a lengthy highly flexible linker. By the nitroxide spin label, attached to the mutant cysteine residue at position 7 or 11, significant transient interactions were probed between the N-terminal helical portion and the core moiety plus several residues in the C-terminal tail. The topology of the triple-helix bundle is encoded mainly by hydrophobic interactions, and the N-terminal helical structure has a unique electrostatic potential character. A comparison of the solution structures of PDCD5-related proteins indicates that the structure of the triple-helix bundle is significantly conserved during evolution. We are the first to demonstrate that YMR074c overexpression promotes H(2)O(2)-induced apoptosis in yeast, not only in a metacaspase Yca1-dependent manner but also in a Yca1-independent manner and that deletion of the N-terminal helical portion greatly attenuates the apoptosis-promoting activity of this protein."xsd:string |
| http://purl.uniprot.org/citations/19469552 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi900488n"xsd:string |
| http://purl.uniprot.org/citations/19469552 | http://purl.uniprot.org/core/author | "Liu Z."xsd:string |
| http://purl.uniprot.org/citations/19469552 | http://purl.uniprot.org/core/author | "Hong J."xsd:string |
| http://purl.uniprot.org/citations/19469552 | http://purl.uniprot.org/core/author | "Shi Y."xsd:string |
| http://purl.uniprot.org/citations/19469552 | http://purl.uniprot.org/core/author | "Wu J."xsd:string |
| http://purl.uniprot.org/citations/19469552 | http://purl.uniprot.org/core/author | "Qin S."xsd:string |
| http://purl.uniprot.org/citations/19469552 | http://purl.uniprot.org/core/author | "Zhang J."xsd:string |
| http://purl.uniprot.org/citations/19469552 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19469552 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/19469552 | http://purl.uniprot.org/core/pages | "6824-6834"xsd:string |
| http://purl.uniprot.org/citations/19469552 | http://purl.uniprot.org/core/title | "Solution structure of S. cerevisiae PDCD5-like protein and its promoting role in H(2)O(2)-induced apoptosis in yeast."xsd:string |
| http://purl.uniprot.org/citations/19469552 | http://purl.uniprot.org/core/volume | "48"xsd:string |
| http://purl.uniprot.org/citations/19469552 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19469552 |
| http://purl.uniprot.org/citations/19469552 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19469552 |
| http://purl.uniprot.org/uniprot/#_Q04773-mappedCitation-19469552 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19469552 |
| http://purl.uniprot.org/uniprot/Q04773 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/19469552 |