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Times Cited: 572
Times Cited: 572
Times Cited
Times Co-cited
Similarity
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy.
Michael Lazarou, Danielle A Sliter, Lesley A Kane, Shireen A Sarraf, Chunxin Wang, Jonathon L Burman, Dionisia P Sideris, Adam I Fogel, Richard J Youle. Nature 2015
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Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells.
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Nix is a selective autophagy receptor for mitochondrial clearance.
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Bcl-2-like protein 13 is a mammalian Atg32 homologue that mediates mitophagy and mitochondrial fragmentation.
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Ubiquitin is phosphorylated by PINK1 to activate parkin.
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Ceramide targets autophagosomes to mitochondria and induces lethal mitophagy.
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The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's disease.
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Microtubule-associated protein 1 light chain 3 (LC3) interacts with Bnip3 protein to selectively remove endoplasmic reticulum and mitochondria via autophagy.
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Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation.
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The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy.
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NIX is required for programmed mitochondrial clearance during reticulocyte maturation.
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Essential role for Nix in autophagic maturation of erythroid cells.
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PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity.
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Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance.
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Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism.
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Phosphorylation of the mitochondrial autophagy receptor Nix enhances its interaction with LC3 proteins.
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PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65.
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PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria.
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Mitophagy receptor FUNDC1 regulates mitochondrial dynamics and mitophagy.
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PINK1 is selectively stabilized on impaired mitochondria to activate Parkin.
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PINK1 cleavage at position A103 by the mitochondrial protease PARL.
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PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy.
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NDPK-D (NM23-H4)-mediated externalization of cardiolipin enables elimination of depolarized mitochondria by mitophagy.
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Basal Mitophagy Occurs Independently of PINK1 in Mouse Tissues of High Metabolic Demand.
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Parkin and PINK1 mitigate STING-induced inflammation.
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Parkin interacts with Ambra1 to induce mitophagy.
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MUL1 acts in parallel to the PINK1/parkin pathway in regulating mitofusin and compensates for loss of PINK1/parkin.
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The PINK1, synphilin-1 and SIAH-1 complex constitutes a novel mitophagy pathway.
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Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL.
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Building and decoding ubiquitin chains for mitophagy.
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Co-cited is the co-citation frequency, indicating how many articles cite the article together with the query article. Similarity is the co-citation as percentage of the times cited of the query article or the article in the search results, whichever is the lowest. These numbers are calculated for the last 100 citations when articles are cited more than 100 times.