About: Phosphorylation-dependent binding of cyclin B1 to a Cdc6-like domain of human separase     Goto   Sponge   NotDistinct   Permalink

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  • Sister chromatids are held together by the ring-shaped cohesin complex, which likely entraps both DNA- double strands in its middle. This tie is resolved in anaphase when separase, a giant protease, becomes active and cleaves the kleisin subunit of cohesin. Premature activation of separase and, hence, chromosome missegregation are prevented by at least two inhibitory mechanisms. Although securin has long been appreciated as a direct inhibitor of separase, surprisingly its loss has basically no phenotype in mammals. Phosphorylation-dependent binding of Cdk1 constitutes an alternative way to inhibit vertebrate separase. Its importance is illustrated by the premature loss of cohesion when Cdk1-resistant separase is expressed in mammalian cells without or with limiting amounts of securin. Here, we demonstrate that crucial inhibitory phosphorylations occur within a region of human separase that is also shown to make direct contact with the cyclin B1 subunit of Cdk1. This region exhibits a weak homology to
  • Sister chromatids are held together by the ring-shaped cohesin complex, which likely entraps both DNA- double strands in its middle. This tie is resolved in anaphase when separase, a giant protease, becomes active and cleaves the kleisin subunit of cohesin. Premature activation of separase and, hence, chromosome missegregation are prevented by at least two inhibitory mechanisms. Although securin has long been appreciated as a direct inhibitor of separase, surprisingly its loss has basically no phenotype in mammals. Phosphorylation-dependent binding of Cdk1 constitutes an alternative way to inhibit vertebrate separase. Its importance is illustrated by the premature loss of cohesion when Cdk1-resistant separase is expressed in mammalian cells without or with limiting amounts of securin. Here, we demonstrate that crucial inhibitory phosphorylations occur within a region of human separase that is also shown to make direct contact with the cyclin B1 subunit of Cdk1. This region exhibits a weak homology to (en)
Title
  • Phosphorylation-dependent binding of cyclin B1 to a Cdc6-like domain of human separase
  • Phosphorylation-dependent binding of cyclin B1 to a Cdc6-like domain of human separase (en)
skos:prefLabel
  • Phosphorylation-dependent binding of cyclin B1 to a Cdc6-like domain of human separase
  • Phosphorylation-dependent binding of cyclin B1 to a Cdc6-like domain of human separase (en)
skos:notation
  • RIV/61989592:15310/08:00010598!RIV10-MSM-15310___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • Z(MSM6198959216)
http://linked.open...iv/cisloPeriodika
  • 2
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 386513
http://linked.open...ai/riv/idVysledku
  • RIV/61989592:15310/08:00010598
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • sister-chromatid cohesion; Escherichia-Coli; Xenopus-oocytes; meiosis-I; complex; securin; protein; progression; inhibition; anaphase (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [622E50F9B9E5]
http://linked.open...i/riv/nazevZdroje
  • Journal of Biological Chemistry
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 283
http://linked.open...iv/tvurceVysledku
  • Lenobel, René
  • Boos, Dominik
  • Koerner, Roman
  • Kuffer, Christian
  • Stemmann, Olaf
http://linked.open...n/vavai/riv/zamer
issn
  • 0021-9258
number of pages
http://localhost/t...ganizacniJednotka
  • 15310
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