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Atg3-Mediated Lipidation of Atg8 Is Involved in Encystation of Acanthamoeba
Eun-Kyung Moon, Dong-Il Chung, Yeonchul Hong, Hyun-Hee Kong
Korean J Parasitol. 2011;49(2):103-108.   Published online 2011 June 14    DOI: https://doi.org/10.3347/kjp.2011.49.2.103

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The amino-terminal region of Atg3 is essential for association with phosphatidylethanolamine in Atg8 lipidation
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A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation
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Atg3 promotes Atg8 lipidation via altering lipid diffusion and rearrangement
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ATG8 lipidation and ATG8-mediated autophagy in Arabidopsis require ATG12 expressed from the differentially controlled ATG12A AND ATG12B loci
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The Crystal Structure of Atg3, an Autophagy-related Ubiquitin Carrier Protein (E2) Enzyme that Mediates Atg8 Lipidation
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Autophagy-related Protein 8 (Atg8) Family Interacting Motif in Atg3 Mediates the Atg3-Atg8 Interaction and Is Crucial for the Cytoplasm-to-Vacuole Targeting Pathway
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Acanthamoeba castellanii: Proteins involved in actin dynamics, glycolysis, and proteolysis are regulated during encystation
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Atg8L/Apg8L is the fourth mammalian modifier of mammalian Atg8 conjugation mediated by human Atg4B, Atg7 and Atg3
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Activation and targeting of ATG8 protein lipidation
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Regulation of Interferon-stimulated Gene (<italic>ISG</italic>)<italic>12</italic>, <italic>ISG15</italic>, and <italic>MX1</italic> and <italic>MX2</italic> by Conceptus Interferons (IFNTs) in Bovine Uterine Epithelial Cells
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