C
Clement A. Gautier
Researcher at Brigham and Women's Hospital
Publications - 25
Citations - 5895
Clement A. Gautier is an academic researcher from Brigham and Women's Hospital. The author has contributed to research in topics: PINK1 & Parkin. The author has an hindex of 19, co-authored 25 publications receiving 5202 citations. Previous affiliations of Clement A. Gautier include University of Texas Health Science Center at Houston & French Institute of Health and Medical Research.
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Journal ArticleDOI
PINK1 is selectively stabilized on impaired mitochondria to activate Parkin.
Derek P. Narendra,Seok Min Jin,Atsushi Tanaka,Der-Fen Suen,Clement A. Gautier,Jie Shen,Mark R. Cookson,Richard J. Youle +7 more
TL;DR: The authors suggest that PINK1 and Parkin form a pathway that senses damaged mitochondria and selectively targets them for degradation.
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PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
Noriyuki Matsuda,Shigeto Sato,Kahori Shiba,Kei Okatsu,Keiko Saisho,Clement A. Gautier,Yu-shin Sou,Shinji Saiki,Sumihiro Kawajiri,Fumiaki Sato,Mayumi Kimura,Masaaki Komatsu,Nobutaka Hattori,Keiji Tanaka +13 more
TL;DR: Defective mitochondrial quality control is shown to be a mechanism for neurodegeneration in some forms of Parkinson's disease.
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Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress
TL;DR: It is demonstrated that mammalian Pink1 is important for mitochondrial function and provides critical protection against both intrinsic and environmental stress, suggesting a pathogenic mechanism by which loss of PINK1 may lead to nigrostriatal degeneration in PD.
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Absence of nigral degeneration in aged parkin/DJ-1/PINK1 triple knockout mice.
TL;DR: It is found that triple knockout mice lacking Parkin, DJ‐1, and PINK1 have normal morphology and numbers of dopaminergic and noradrenergic neurons in the substantia nigra and locus coeruleus, respectively, at the ages of 3, 16, and 24 months.
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Endothelial nitric oxide synthase reduces nitrite anions to NO under anoxia.
TL;DR: The reaction suggests a new pathway for fast NO delivery under hypoxia, precisely when the vasodilating properties of nitric oxide are most needed.