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                  <mods:namePart>Suja, José A</mods:namePart>
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                  <mods:namePart>Instituto de Salud Carlos III</mods:namePart>
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                  <mods:namePart>Ministerio de Ciencia e Innovación. Centro de Excelencia Severo Ochoa (España)</mods:namePart>
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               <mods:identifier type="citation">EMBO Rep  . 2020;21(6):e49273.</mods:identifier>
               <mods:identifier type="doi">10.15252/embr.201949273</mods:identifier>
               <mods:identifier type="e-issn">1469-3178</mods:identifier>
               <mods:identifier type="journal">EMBO reports</mods:identifier>
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               <mods:identifier type="uri">http://hdl.handle.net/20.500.12105/17656</mods:identifier>
               <mods:abstract>Cohesin cofactors regulate the loading, maintenance, and release of cohesin complexes from chromosomes during mitosis but little is known on their role during vertebrate meiosis. One such cofactor is PDS5, which exists as two paralogs in somatic and germline cells, PDS5A and PDS5B, with unclear functions. Here, we have analyzed their distribution and functions in mouse spermatocytes. We show that simultaneous excision of Pds5A and Pds5B results in severe defects during early prophase I while their individual depletion does not, suggesting their functional redundancy. Shortened axial/lateral elements and a reduction of early recombination nodules are observed after the strong depletion of PDS5A/B proteins. Moreover, telomere integrity and their association to the nuclear envelope are severely compromised. As these defects occur without detectable reduction in chromosome-bound cohesin, we propose that the dynamic behavior of the complex, mediated by PDS5 proteins, is key for successful completion of meiotic prophase I.</mods:abstract>
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                  <mods:title>PDS5 proteins regulate the length of axial elements and telomere integrity during male mouse meiosis.</mods:title>
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