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Thomas Macartney

Researcher at University of Dundee

Publications -  83
Citations -  4650

Thomas Macartney is an academic researcher from University of Dundee. The author has contributed to research in topics: Ubiquitin ligase & Kinase. The author has an hindex of 30, co-authored 72 publications receiving 3771 citations. Previous affiliations of Thomas Macartney include Medical Research Council.

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PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65

TL;DR: These results provide the first evidence that PINK1 is activated following Δψm depolarization and suggest that Pink1 directly phosphorylates and activates Parkin, and indicate that monitoring phosphorylation of Parkin at Ser65 and/or Pinks1 at Thr257 represent the first biomarkers for examining activity of the PINK 1-Parkin signalling pathway in vivo.
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14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization

TL;DR: The results suggest that mutation of Ser910 and/or Ser935 to disrupt 14-3-3 binding does not affect intrinsic protein kinase activity, but induces LRRK2 to accumulate within discrete cytoplasmic pools, perhaps resembling inclusion bodies.
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Coordination of structure-specific nucleases by human SLX4/BTBD12 is required for DNA repair.

TL;DR: The identification of human SLX4, a scaffold for DNA repair nucleases XPF-ERCC1, MUS81-EME1, and SLX1 is described and data show thatSLX4 is a regulator of structure-specific nucleases and that SLX 4 and SLx1 are important regulators of genome stability in human cells.
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Identification of KIAA1018/FAN1, a DNA Repair Nuclease Recruited to DNA Damage by Monoubiquitinated FANCD2

TL;DR: A highly conserved protein is described, KIAA1018/MTMR15/FAN1, that interacts with, and is recruited to sites of DNA damage by, the monoubiquitinated form of FANCD2, which at least partly explains how ubiquitination of FANSCD2 promotes DNA repair.
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The CUL3–KLHL3 E3 ligase complex mutated in Gordon's hypertension syndrome interacts with and ubiquitylates WNK isoforms: disease-causing mutations in KLHL3 and WNK4 disrupt interaction

TL;DR: How mutations that disrupt the ability of an E3 ligase to interact with and ubiquitylate a critical cellular substrate such as WNK isoforms can trigger a chronic disease such as hypertension is revealed.