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Apg7p/Cvt2p: A novel protein-activating enzyme essential for autophagy.
Tanida I, Mizushima N, Kiyooka M, Ohsumi M, Ueno T, Ohsumi Y, Kominami E. Tanida I, et al. Mol Biol Cell. 1999 May;10(5):1367-79. doi: 10.1091/mbc.10.5.1367. Mol Biol Cell. 1999. PMID: 10233150 Free PMC article.
Cells expressing mutant Apg7ps, Apg7pG333A, or Apg7pC507A showed defects in autophagy and cytoplasm-to-vacuole targeting of aminopeptidase I. ...
Cells expressing mutant Apg7ps, Apg7pG333A, or Apg7pC507A showed defects in autophagy and cytoplasm-to-vacuole targeting of aminopeptidase …
Autolysosomal membrane-associated betaine homocysteine methyltransferase. Limited degradation fragment of a sequestered cytosolic enzyme monitoring autophagy.
Ueno T, Ishidoh K, Mineki R, Tanida I, Murayama K, Kadowaki M, Kominami E. Ueno T, et al. J Biol Chem. 1999 May 21;274(21):15222-9. doi: 10.1074/jbc.274.21.15222. J Biol Chem. 1999. PMID: 10329731
A lysosomal proteinase, the late infantile neuronal ceroid lipofuscinosis gene (CLN2) product, is essential for degradation of a hydrophobic protein, the subunit c of ATP synthase.
Ezaki J, Tanida I, Kanehagi N, Kominami E. Ezaki J, et al. J Neurochem. 1999 Jun;72(6):2573-82. doi: 10.1046/j.1471-4159.1999.0722573.x. J Neurochem. 1999. PMID: 10349869
The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3.
Tanida I, Tanida-Miyake E, Ueno T, Kominami E. Tanida I, et al. J Biol Chem. 2001 Jan 19;276(3):1701-6. doi: 10.1074/jbc.C000752200. Epub 2000 Nov 28. J Biol Chem. 2001. PMID: 11096062
Each of three human Apg8p counterparts, i.e. the Golgi-associated ATPase enhancer of 16 kDa, GABA(A) receptor-associated protein, and microtubule-associated protein light chain 3, coimmunoprecipitates with hApg7p and conjugates with mutant hApg7p(C572S) to form a stable in …
Each of three human Apg8p counterparts, i.e. the Golgi-associated ATPase enhancer of 16 kDa, GABA(A) receptor-associated protein, and …
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.
Tanida I, Tanida-Miyake E, Komatsu M, Ueno T, Kominami E. Tanida I, et al. J Biol Chem. 2002 Apr 19;277(16):13739-44. doi: 10.1074/jbc.M200385200. Epub 2002 Feb 1. J Biol Chem. 2002. PMID: 11825910
., Tanida, I., Kominami, E., Ohsumi, M., Noda, T., and Ohsumi, Y. (2000) Nature 408, 488-492). In this study, the cloning of a human Apg3p homologue (hApg3p) as an E2 enzyme essential for human Apg8p homologues (i.e. ...
., Tanida, I., Kominami, E., Ohsumi, M., Noda, T., and Ohsumi, Y. (2000) Nature 408, 488-492). In this study, the cloning of a …
Murine Apg12p has a substrate preference for murine Apg7p over three Apg8p homologs.
Tanida I, Tanida-Miyake E, Nishitani T, Komatsu M, Yamazaki H, Ueno T, Kominami E. Tanida I, et al. Biochem Biophys Res Commun. 2002 Mar 22;292(1):256-62. doi: 10.1006/bbrc.2002.6645. Biochem Biophys Res Commun. 2002. PMID: 11890701
Mammalian Apg12p, but not the Apg12p.Apg5p conjugate, facilitates LC3 processing.
Tanida I, Nishitani T, Nemoto T, Ueno T, Kominami E. Tanida I, et al. Biochem Biophys Res Commun. 2002 Sep 6;296(5):1164-70. doi: 10.1016/s0006-291x(02)02057-0. Biochem Biophys Res Commun. 2002. PMID: 12207896
GATE-16 and GABARAP are authentic modifiers mediated by Apg7 and Apg3.
Tanida I, Komatsu M, Ueno T, Kominami E. Tanida I, et al. Biochem Biophys Res Commun. 2003 Jan 17;300(3):637-44. doi: 10.1016/s0006-291x(02)02907-8. Biochem Biophys Res Commun. 2003. PMID: 12507496
When Apg7p and Apg3p are expressed, GATE-16-I and GABARAP-I are modified to a secondary ubiquitin-like modified form, GATE-16-II and GABARAP-II, respectively. GATE-16-I and GABARAP-I, but not LC3-I, localize to membrane compartments before their …
When Apg7p and Apg3p are expressed, GATE-16-I and GABARAP-I are modified to a secondary ubiquitin-like modified form, GATE-16- …
MAP-LC3, a promising autophagosomal marker, is processed during the differentiation and recovery of podocytes from PAN nephrosis.
Asanuma K, Tanida I, Shirato I, Ueno T, Takahara H, Nishitani T, Kominami E, Tomino Y. Asanuma K, et al. FASEB J. 2003 Jun;17(9):1165-7. doi: 10.1096/fj.02-0580fje. Epub 2003 Apr 22. FASEB J. 2003. PMID: 12709412
LC3-I, the cytosolic form, is modified to LC3-II, the membrane-bound form, by a mechanism similar to ubiquitylation by E1- and E2-like enzymes, Apg7p and Apg3p, respectively. In the present study, we found that LC3-I is processed to LC3-II during the differentiation …
LC3-I, the cytosolic form, is modified to LC3-II, the membrane-bound form, by a mechanism similar to ubiquitylation by E1- and E2-lik …
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