LC3 conjugation system in mammalian autophagy (Q28278334)

International Journal of Biochemistry & Cell Biology

Europe PubMed Central

title

LC3 conjugation system in mammalian autophagy (English)

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Isei Tanida

1

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Takashi Ueno

series ordinal

2

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Eiki Kominami

series ordinal

3

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language of work or name

English

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publication date

December 2004

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published in

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volume

36

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issue

12

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page(s)

2503-18

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cites work

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Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae

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MAP-LC3, a promising autophagosomal marker, is processed during the differentiation and recovery of podocytes from PAN nephrosis.

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Human autophagins, a family of cysteine proteinases potentially implicated in cell degradation by autophagy

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Role of autophagy in temozolomide-induced cytotoxicity for malignant glioma cells

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Glucose-induced autophagy of peroxisomes in Pichia pastoris requires a unique E1-like protein

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The loss of Drosophila APG4/AUT2 function modifies the phenotypes of cut and Notch signaling pathway mutants

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Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network

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Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p

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Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy

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In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker

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Mammalian Apg12p, but not the Apg12p.Apg5p conjugate, facilitates LC3 processing

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Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor

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The mouse APG10 homologue, an E2-like enzyme for Apg12p conjugation, facilitates MAP-LC3 modification

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Coronavirus replication complex formation utilizes components of cellular autophagy

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The UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase gene is mutated in recessive hereditary inclusion body myopathy

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Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: an autophagy-like origin for virus-induced vesicles

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Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice

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A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy

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The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3

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Macroautophagy is required for multicellular development of the social amoeba Dictyostelium discoideum

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Apg14p and Apg6/Vps30p form a protein complex essential for autophagy in the yeast, Saccharomyces cerevisiae

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Mouse Apg10 as an Apg12-conjugating enzyme: analysis by the conjugation-mediated yeast two-hybrid method

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Autophagy in the eukaryotic cell

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Mouse Apg16L, a novel WD-repeat protein, targets to the autophagic isolation membrane with the Apg12-Apg5 conjugate

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LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing

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Molecular dissection of autophagy: two ubiquitin-like systems

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Murine Apg12p has a substrate preference for murine Apg7p over three Apg8p homologs

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Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells

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Apg7p/Cvt2p: A novel protein-activating enzyme essential for autophagy

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Porphyromonas gingivalis traffics to autophagosomes in human coronary artery endothelial cells

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Huntington's disease: the mystery unfolds?

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Structure and function of the yeast vacuole and its role in autophagy

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The reversible modification regulates the membrane-binding state of Apg8/Aut7 essential for autophagy and the cytoplasm to vacuole targeting pathway

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Structural and functional analyses of APG5, a gene involved in autophagy in yeast

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Ultrastructural studies on autolysosomes in rat hepatocytes after leupeptin treatment

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Coxiella burnetii localizes in a Rab7-labeled compartment with autophagic characteristics

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10.1016/J.BIOCEL.2004.05.009

Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

15325588

1 reference

Consolidated OpenCitations Corpus – April 2017