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Kevin L. Lorick

Researcher at National Institutes of Health

Publications -  10
Citations -  2648

Kevin L. Lorick is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Ubiquitin ligase & Ubiquitin. The author has an hindex of 8, co-authored 10 publications receiving 2563 citations.

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Journal ArticleDOI

RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination

TL;DR: It is suggested that a large number of RING finger-containing proteins, with otherwise diverse structures and functions, may play previously unappreciated roles in modulating protein levels via ubiquitination.
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Mind Bomb Is a Ubiquitin Ligase that Is Essential for Efficient Activation of Notch Signaling by Delta

TL;DR: Cell transplantation studies suggest that mib function is essential in the signaling cell for efficient activation of Notch in neighboring cells, and observations support a model for Notch activation where the Delta-Notch interaction is followed by endocytosis of Delta and transendocyTosis of the Notch extracellular domain by the signalingcell.
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Inhibitors of ubiquitin-activating enzyme (E1), a new class of potential cancer therapeutics.

TL;DR: PYR-41 and related pyrazones provide proof of principle for the capacity to differentially kill transformed cells, suggesting the potential for E1 inhibitors as therapeutics in cancer and can also be valuable tools for studying ubiquitylation.
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RING finger ubiquitin protein ligases: implications for tumorigenesis, metastasis and for molecular targets in cancer

TL;DR: Recent advances in the understanding of RING finger and Ringer finger-related E3s with emphasis on BRCA1 and the tumor autocrine motility factor receptor are summarized and the potential for components of the ubiquitin pathway for proteasomal degradation as molecular targets are discussed.
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E6AP Mediates Regulated Proteasomal Degradation of the Nuclear Receptor Coactivator Amplified in Breast Cancer 1 in Immortalized Cells

TL;DR: It is described that the cellular levels of AIB1 are controlled through regulated proteasomal degradation, and a model is proposed whereby signals promoted by changes in the cellular milieu initiate E6AP-mediated proteasome degradation ofAIB1 and thus contribute to the control of steady-state levels of this protein.