Protein accumulation in the endoplasmic reticulum as a non-equilibrium phase transition (Articolo in rivista)

Type
Label
  • Protein accumulation in the endoplasmic reticulum as a non-equilibrium phase transition (Articolo in rivista) (literal)
Anno
  • 2014-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1038/ncomms4620 (literal)
Alternative label
  • Budrikis Z.; Costantini G.; La Porta C.A.M.; Zapperi S. (2014)
    Protein accumulation in the endoplasmic reticulum as a non-equilibrium phase transition
    in Nature communications
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Budrikis Z.; Costantini G.; La Porta C.A.M.; Zapperi S. (literal)
Pagina inizio
  • 3620 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://www.nature.com/ncomms/2014/140411/ncomms4620/full/ncomms4620.html (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 5 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 8 (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • Scopu (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1,4 : Institute for Scientific Interchange Foundation, Via Alassio 11/C, Torino 10126, Italy / 2,4 : Istituto per l'Energetica e le Interfasi, CNR-Consiglio Nazionale Delle Ricerche, Via R. Cozzi 53, Milano 20125, Italy / 3 : Department of Biosciences, University of Milano, via Celoria 26, Milano 20133, Italy (literal)
Titolo
  • Protein accumulation in the endoplasmic reticulum as a non-equilibrium phase transition (literal)
Abstract
  • Several neurological disorders are associated with the aggregation of aberrant proteins, often localized in intracellular organelles such as the endoplasmic reticulum. Here we study protein aggregation kinetics by mean-field reactions and three dimensional Monte carlo simulations of diffusion-limited aggregation of linear polymers in a confined space, representing the endoplasmic reticulum. By tuning the rates of protein production and degradation, we show that the system undergoes a non-equilibrium phase transition from a physiological phase with little or no polymer accumulation to a pathological phase characterized by persistent polymerization. A combination of external factors accumulating during the lifetime of a patient can thus slightly modify the phase transition control parameters, tipping the balance from a long symptomless lag phase to an accelerated pathological development. The model can be successfully used to interpret experimental data on amyloid-beta clearance from the central nervous system. (literal)
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