| http://purl.uniprot.org/citations/21771883 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21771883 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21771883 | http://www.w3.org/2000/01/rdf-schema#comment | "Two distinct pathways for meiotic crossover formation coexist in most eukaryotes. The Arabidopsis SHOC1 protein is required for class I crossovers and shows sequence similarity with the XPF endonuclease family. Active XPF endonucleases form a heterodimer with ERCC1 proteins. Here, we show that PTD, an ERCC1-like protein, is required for class-I-interfering crossovers along with SHOC1, MSH4, MSH5, MER3 and MLH3. SHOC1 interacts with PTD in a two-hybrid assay, through its XPF-like nuclease-(HhH)(2) domain. We propose that a XPF-ERCC1-like heterodimer, represented by SHOC1 and PTD in Arabidopsis, involving Zip2 in Saccharomyces cerevisiae and C9orf84 in human, is required for formation of class I crossovers."xsd:string |
| http://purl.uniprot.org/citations/21771883 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.088229"xsd:string |
| http://purl.uniprot.org/citations/21771883 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.088229"xsd:string |
| http://purl.uniprot.org/citations/21771883 | http://purl.uniprot.org/core/author | "Vignard J."xsd:string |
| http://purl.uniprot.org/citations/21771883 | http://purl.uniprot.org/core/author | "Vignard J."xsd:string |
| http://purl.uniprot.org/citations/21771883 | http://purl.uniprot.org/core/author | "Mercier R."xsd:string |
| http://purl.uniprot.org/citations/21771883 | http://purl.uniprot.org/core/author | "Mercier R."xsd:string |
| http://purl.uniprot.org/citations/21771883 | http://purl.uniprot.org/core/author | "Macaisne N."xsd:string |
| http://purl.uniprot.org/citations/21771883 | http://purl.uniprot.org/core/author | "Macaisne N."xsd:string |
| http://purl.uniprot.org/citations/21771883 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21771883 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21771883 | http://purl.uniprot.org/core/name | "J. Cell Sci."xsd:string |
| http://purl.uniprot.org/citations/21771883 | http://purl.uniprot.org/core/name | "J. Cell Sci."xsd:string |
| http://purl.uniprot.org/citations/21771883 | http://purl.uniprot.org/core/pages | "2687-2691"xsd:string |
| http://purl.uniprot.org/citations/21771883 | http://purl.uniprot.org/core/pages | "2687-2691"xsd:string |
| http://purl.uniprot.org/citations/21771883 | http://purl.uniprot.org/core/title | "SHOC1 and PTD form an XPF-ERCC1-like complex that is required for formation of class I crossovers."xsd:string |
| http://purl.uniprot.org/citations/21771883 | http://purl.uniprot.org/core/title | "SHOC1 and PTD form an XPF-ERCC1-like complex that is required for formation of class I crossovers."xsd:string |
| http://purl.uniprot.org/citations/21771883 | http://purl.uniprot.org/core/volume | "124"xsd:string |
| http://purl.uniprot.org/citations/21771883 | http://purl.uniprot.org/core/volume | "124"xsd:string |
| http://purl.uniprot.org/citations/21771883 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21771883 |
| http://purl.uniprot.org/citations/21771883 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21771883 |
| http://purl.uniprot.org/citations/21771883 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/21771883 |
| http://purl.uniprot.org/citations/21771883 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/21771883 |