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Michele Pagano

Researcher at Howard Hughes Medical Institute

Publications -  313
Citations -  47383

Michele Pagano is an academic researcher from Howard Hughes Medical Institute. The author has contributed to research in topics: Ubiquitin ligase & Cell cycle. The author has an hindex of 97, co-authored 306 publications receiving 42211 citations. Previous affiliations of Michele Pagano include New York University & University of Palermo.

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Molecular mechanisms of cell death: recommendations of the Nomenclature Committee on Cell Death 2018.

Lorenzo Galluzzi, +186 more
TL;DR: The Nomenclature Committee on Cell Death (NCCD) has formulated guidelines for the definition and interpretation of cell death from morphological, biochemical, and functional perspectives.
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Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27

TL;DR: Compared with proliferating cells, quiescent cells exhibited a smaller amount of p27 ubiquitinating activity, which accounted for the marked increase of p 27 half-life measured in these cells, indicating that the abundance of p26 in cells is regulated by degradation.
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Cyclin D1 is a nuclear protein required for cell cycle progression in G1.

TL;DR: Results demonstrate that cyclin D1 is a critical target of proliferative signals in G1, a putative G1 cyclin, in normal diploid human fibroblasts.
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SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27.

TL;DR: It is shown that the F-box protein SKP2 specifically recognizes p27 in a phosphorylation-dependent manner that is characteristic of an F- box-protein–substrate interaction and is subject to dual control by the accumulation of bothSKP2 and cyclins following mitogenic stimulation.
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Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex.

TL;DR: The structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF complex suggests that Cul1 may contribute to catalysis through the positioning of the substrate and the ubiquitin-conjugating enzyme, and this model is supported by Cul1 mutations designed to eliminate the rigidity of the scaffold.