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Josée Coulombe

Researcher at Ottawa Hospital Research Institute

Publications -  9
Citations -  151

Josée Coulombe is an academic researcher from Ottawa Hospital Research Institute. The author has contributed to research in topics: Ubiquitin & Proteasome. The author has an hindex of 5, co-authored 9 publications receiving 120 citations.

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Evolution of the highly networked deubiquitinating enzymes USP4, USP15, and USP11

TL;DR: The analyses indicate that USP4 and USP15 arose from whole genome duplication prior to the emergence of jawed vertebrates, and it is confirmed that viability is contingent on a functional copy of USP5 or USP6, while USP11 was generated later in vertebrate evolution by small-scale duplication of the USP 4-encoding region.
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Loss of UCHL1 promotes age-related degenerative changes in the enteric nervous system

TL;DR: The mice displayed functional changes and morphological changes in gut neurons that preceded degenerative changes in the brain, and strongly resemble changes reported for elderly humans, and should serve as a useful model of gut aging.
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Protection against murine osteoarthritis by inhibition of the 26S proteasome and lysine-48 linked ubiquitination

TL;DR: The data for the first time identifies a role for ubiquitination and the proteasome in the induction of OA via regulation of inflammatory mediator-induced MMP13 expression and opens avenues of research to determine whether the prote asome, or K48-linked ubiquitinated substrates, are potential therapeutic targets in OA.
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Ubiquitin C-terminal hydrolase L1 deletion ameliorates glomerular injury in mice with ACTN4-associated focal segmental glomerulosclerosis.

TL;DR: The data suggest that UCHL1 upregulation in ACTN4-associated FSGS fuels the proteasome and that UCH l1 deletion may impair proteolysis and thereby preserve K256E/wt-α-actinin-4 heterodimers, maintaining podocyte cytoskeletal integrity and protecting the glomerular filtration barrier.
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Reversible modulation of SIRT1 activity in a mouse strain.

TL;DR: This mouse was created to create a mouse in which the SIRT1 activity could be toggled between on and off states by fusing the estrogen receptor ligand-binding domain (ER) to the C terminus of the Sirt1 protein.