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Eden Fussner

Researcher at University of Toronto

Publications -  10
Citations -  2479

Eden Fussner is an academic researcher from University of Toronto. The author has contributed to research in topics: Chromatin & Induced pluripotent stem cell. The author has an hindex of 10, co-authored 10 publications receiving 2040 citations. Previous affiliations of Eden Fussner include Lunenfeld-Tanenbaum Research Institute.

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Phase Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles

TL;DR: It is demonstrated that the disordered tails of Ddx4, a primary constituent of nuage or germ granules, form phase-separated organelles both in live cells and in vitro, and proposed that phase separation of disordered proteins containing weakly interacting blocks is a general mechanism for forming regulated, membraneless organlles.
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Genome-wide dynamics of replication timing revealed by in vitro models of mouse embryogenesis

TL;DR: A model in which a distinct set of replication domains undergoes a form of "autosomal Lyonization" in the epiblast that is difficult to reprogram and coincides with an epigenetic commitment to differentiation prior to germ layer specification is supported.
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Global chromatin architecture reflects pluripotency and lineage commitment in the early mouse embryo.

TL;DR: Examination of large-scale chromatin structural changes during the transition from one-cell to early postimplantation stage embryos shows that an open chromatin architecture is established in the embryonic lineages during development and is sufficient to distinguish pluripotent cells from tissue-restricted progenitor cells.
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Open and closed domains in the mouse genome are configured as 10‐nm chromatin fibres

TL;DR: Three‐dimensional images are generated, revealing that both open and closed chromatin domains in mouse somatic cells comprise 10‐nm fibres, indicating that the 30‐nm chromatin model does not reflect the true regulatory structure in vivo.
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CEP120 and SPICE1 cooperate with CPAP in centriole elongation.

TL;DR: It is shown that CEP120 and SPICE1 are required to localize CEP135 (but not SASS6, STIL, or CPAP) to procentrioles, and a shared function for these proteins in centriole length control is identified.