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of outstanding interest. A morphological examination of peroxisome degradation by both macroautophagy and microautophagy. The isolation of pag mutants defective in three different steps of the microautophagic degradation process was performed.
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Sakai, Y.1
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Isolation and characterization of mutants impaired in the selective degradation of peroxisomes in the yeast Hansenula polymorpha
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13
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A membrane associated complex containing the Vps15 protein kinase and the Vps34 PI 3-kinase is essential for protein sorting to the yeast lysosome-like vacuole
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Staak JH, Hormon PK, Sohu PV, Emr SD. A membrane associated complex containing the Vps15 protein kinase and the Vps34 PI 3-kinase is essential for protein sorting to the yeast lysosome-like vacuole. EMBO J. 12:1993;2195-2204.
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Glucose induced microautophagy in Pichia pastoris requires the α-subunit of phosphofructokinase
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of outstanding interest. This paper describes the cloning of GSA1, which codes for the alpha subunit of phosphofructokinase (PFK1). The catalytic site of PFK1 is not required for peroxisomal degradation, suggesting that the protein acts independently of its role in glycolysis.
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Yuan WY, Tuttle DL, Shi Y-J, Ralph GS, Dunn WA Jr. Glucose induced microautophagy in Pichia pastoris requires the α-subunit of phosphofructokinase. of outstanding interest J Cell Sci. 110:1997;1935-1945 This paper describes the cloning of GSA1, which codes for the alpha subunit of phosphofructokinase (PFK1). The catalytic site of PFK1 is not required for peroxisomal degradation, suggesting that the protein acts independently of its role in glycolysis.
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Yuan, W.Y.1
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0027304446
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Inactivation of YME1, a member of the ftsH-SEC18-PAS1-CDC48 family of putative ATPase-encoding genes, causes increased escape of DNA from mitochondria in Saccharomyces cerevisiae
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Thorsness PE, White KH, Fox TD. Inactivation of YME1, a member of the ftsH-SEC18-PAS1-CDC48 family of putative ATPase-encoding genes, causes increased escape of DNA from mitochondria in Saccharomyces cerevisiae. Mol Cell Biol. 13:1993;5418-5426.
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Isolation of degradation-deficient mutants defective in the targeting of fructose-1,6-bisphosphatase into the vacuole for degradation in Saccharomyces cerevisiae
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Identification of novel vesicles in the cytosol to vacuole degradation pathway
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of outstanding interest. This paper describes the purification of vesicles involved in the vacuolar delivery of the glycolytic enzyme fructose-1,6-bisphosphatase.
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Huang P-H, Chiang H-L. Identification of novel vesicles in the cytosol to vacuole degradation pathway. of outstanding interest J Cell Biol. 136:1997;803-810 This paper describes the purification of vesicles involved in the vacuolar delivery of the glycolytic enzyme fructose-1,6-bisphosphatase.
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Vid24p, a novel protein localized to the fructose-1,6-bisphosphatase-containing vesicles, regulates targeting of fructose-1,6-bisphosphatase from the vesicles to the vacuole for degradation in S. cerevisiae
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of outstanding interest. This paper describes the first characterization of a mutant involved in fructose-1,6-bisphosphatase degradation. Vid24p is localized to fructose-1,6-bisphosphatase-containing vesicles, and functional Vid24p is required for the delivery of these vesicles to the vacuole.
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Chiang M-C, Chiang H-L. Vid24p, a novel protein localized to the fructose-1,6-bisphosphatase-containing vesicles, regulates targeting of fructose-1,6-bisphosphatase from the vesicles to the vacuole for degradation in S. cerevisiae. of outstanding interest J Cell Biol. 140:1998;1347-1356 This paper describes the first characterization of a mutant involved in fructose-1,6-bisphosphatase degradation. Vid24p is localized to fructose-1,6-bisphosphatase-containing vesicles, and functional Vid24p is required for the delivery of these vesicles to the vacuole.
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0032488997
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In vitro reconstitution of glucose-induced targeting of fructose-1,6-bisphosphatase into the vacuole in semi-intact yeast cells
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of outstanding interest. The authors describe the development of the first in vitro assay for the vacuolar uptake of fructose-1,6-bisphosphatase. The in vitro targeting event is stimulated in cells treated with glucose, suggesting that it represents the in vivo targeting event.
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Shieh H-L, Chiang H-L. In vitro reconstitution of glucose-induced targeting of fructose-1,6-bisphosphatase into the vacuole in semi-intact yeast cells. of outstanding interest J Biol Chem. 273:1998;3381-3387 The authors describe the development of the first in vitro assay for the vacuolar uptake of fructose-1,6-bisphosphatase. The in vitro targeting event is stimulated in cells treated with glucose, suggesting that it represents the in vivo targeting event.
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Ultrastructural and biochemical characterization of autophagy in higher plant cells subjected to carbon deprivation: Control by the supply of mitochondria with respiratory substrates
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Aubert S, Gout E, Bligny R, Marty-Mazars D, Barrieu F, Alabouvette J, Marty F, Douce R. Ultrastructural and biochemical characterization of autophagy in higher plant cells subjected to carbon deprivation: control by the supply of mitochondria with respiratory substrates. J Cell Biol. 133:1996;1251-1263.
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Wolf, D.H.7
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Structural and functional analyses of APG5, a gene involved in autophagy in yeast
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Kametaka S, Matsuura A, Wada Y, Ohsumi Y. Structural and functional analyses of APG5, a gene involved in autophagy in yeast. Gene. 178:1996;139-143.
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Funakoshi T, Matsuura A, Noda T, Oshumi Y. Analysis of APG13 gene involved in autophagy in yeast, Saccharomyces cerevisiae. Gene. 192:1997;207-213.
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AUT1, a gene essential for autophagocytosis in the yeast Saccharomyces cerevisiae
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of special interest. The authors describe the cloning of AUT1, which codes for a novel protein required for both autophagy and aminopeptidase I transport.
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Schlumpberger M, Schaeffeler E, Straub M, Bredschneider M, Wolf DH, Thumm M. AUT1, a gene essential for autophagocytosis in the yeast Saccharomyces cerevisiae. of special interest J Bacteriol. 179:1997;1068-1076 The authors describe the cloning of AUT1, which codes for a novel protein required for both autophagy and aminopeptidase I transport.
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J Bacteriol
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Schlumpberger, M.1
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Straub, M.3
Bredschneider, M.4
Wolf, D.H.5
Thumm, M.6
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34
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0030983504
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Apg1p, a novel protein kinase required for the autophagic process in Saccharomyces cerevisiae
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of special interest. This paper describes the cloning of APG1, which codes for a novel serine/threonine protein kinase.
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Matsuura A, Tsukada M, Wada Y, Ohsumi Y. Apg1p, a novel protein kinase required for the autophagic process in Saccharomyces cerevisiae. of special interest Gene. 192:1997;245-250 This paper describes the cloning of APG1, which codes for a novel serine/threonine protein kinase.
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Gene
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Matsuura, A.1
Tsukada, M.2
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Ohsumi, Y.4
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0031452311
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Mutational analysis of Csc1/Vps4p: Involvement of endosome in regulation of autophagy in yeast
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of outstanding interest. The isolation of two complementation groups of mutants that constitutively undergo autophagic delivery is described. The cloning of CSC1 revealed that it is identical to VPS4, suggesting a role for the endosome in regulating autophagy.
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Shirahama K, Noda T, Oshumi Y. Mutational analysis of Csc1/Vps4p: involvement of endosome in regulation of autophagy in yeast. of outstanding interest Cell Struct Funct. 22:1997;501-509 The isolation of two complementation groups of mutants that constitutively undergo autophagic delivery is described. The cloning of CSC1 revealed that it is identical to VPS4, suggesting a role for the endosome in regulating autophagy.
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Shirahama, K.1
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Houri J-J3
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Blommaart EF, Luiken JJ, Blommaart PJ, van Woerkom GM, Meijer AJ. Phosphorylation of ribosomal protein S6 is inhibitory for autophagy in isolated rat hepatocytes. J Biol Chem. 270:1995;2320-2326.
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41
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0032512636
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Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast
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of special interest. The findings of the authors implicate Tor, a yeast phosphatidylinositol kinase homologue, in the regulation of autophagy in yeast.
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Noda T, Ohsumi Y. Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast. of special interest J Biol Chem. 273:1998;3963-3966 The findings of the authors implicate Tor, a yeast phosphatidylinositol kinase homologue, in the regulation of autophagy in yeast.
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Martinez E, Jimenez MA, Segui-Real B, Vandekerckhove J, Sandoval IV. Folding of the presequence of yeast pAPI into an amphipathic helix determines transport of the protein from the cytosol to the vacuole. J Mol Biol. 267:1997;1124-1138.
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45
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Transport of a large oligomeric protein by the cytoplasm to vacuole protein targeting pathway
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of outstanding interest. This paper characterized the structure of amino peptidase I during transport Amino peptidase I was found to be assembled into a dodecamer ??? approximately 732 kDa immediately after synthesis, and was maintained ??? the oligomeric form throughout the targeting process.
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Kim J, Scott SV, Oda MN, Klionsky DJ. Transport of a large oligomeric protein by the cytoplasm to vacuole protein targeting pathway. of outstanding interest J Cell Biol. 137:1997;609-618 This paper characterized the structure of amino peptidase I during transport Amino peptidase I was found to be assembled into a dodecamer ??? approximately 732 kDa immediately after synthesis, and was maintained ??? the oligomeric form throughout the targeting process.
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0028800171
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Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway
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Harding TM, Morano KA, Scott SV, Klionsky DJ. Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway. J Cell Biol. 131:1995;591-602.
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(1995)
J Cell Biol
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Harding, T.M.1
Morano, K.A.2
Scott, S.V.3
Klionsky, D.J.4
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47
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0029953575
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Genetic and phenotypic overlap between autophagy and the cytoplasm to vacuole protein targeting pathway
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Harding TM, Hefner-Gravink A, Thumm M, Klionsky DJ. Genetic and phenotypic overlap between autophagy and the cytoplasm to vacuole protein targeting pathway. J Biol Chem. 271:1996;17621-17624.
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(1996)
J Biol Chem
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Harding, T.M.1
Hefner-Gravink, A.2
Thumm, M.3
Klionsky, D.J.4
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48
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0029913505
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Cytoplasm to vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole
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Scott SV, Hefner-Gravink A, Morano KA, Noda T, Ohsumi Y, Klionsky DJ. Cytoplasm to vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole. Proc Natl Acad Sci USA. 93:1996;12304-12308.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 12304-12308
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Scott, S.V.1
Hefner-Gravink, A.2
Morano, K.A.3
Noda, T.4
Ohsumi, Y.5
Klionsky, D.J.6
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49
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0030852279
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Aminopeptidase I is targeted to the vacuole by a nonclassical vesicular mechanism
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of outstanding interest. The authors describe the biochemical characterization of the cytosol-to vacuole targeting pathway. The identification of amino peptidase I in ??? intermediates, cytosolic vesicles and subvacuolar vesicles supports a autophagic model for protein uptake by this pathway.
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Scott SV, Baba M, Ohsumi Y, Klionsky DJ. Aminopeptidase I is targeted to the vacuole by a nonclassical vesicular mechanism. of outstanding interest J Cell Biol. 138:1997;37-44 The authors describe the biochemical characterization of the cytosol-to vacuole targeting pathway. The identification of amino peptidase I in ??? intermediates, cytosolic vesicles and subvacuolar vesicles supports a autophagic model for protein uptake by this pathway.
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(1997)
J Cell Biol
, vol.138
, pp. 37-44
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Scott, S.V.1
Baba, M.2
Ohsumi, Y.3
Klionsky, D.J.4
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50
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0031417385
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Two distinct pathways for targeting proteins from the cytoplasm to the vacuole/lysosome
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of outstanding interest. The authors give a comparison of amino-peptidase I targeting in rich ??? and starvation conditions, demonstrating that structures ??? similar to autophagosomes form in rich media and are used for the ??? targeting of amino-peptidase I. The vesicles formed in rich media are ??? Cvt vesicles and are smaller than autophagosomes and do not appear ??? include bulk cytosol.
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Baba M, Osumi M, Scott SV, Klionsky DJ, Ohsumi Y. Two distinct pathways for targeting proteins from the cytoplasm to the vacuole/lysosome. of outstanding interest J Cell Biol. 139:1997;1687-1695 The authors give a comparison of amino-peptidase I targeting in rich ??? and starvation conditions, demonstrating that structures ??? similar to autophagosomes form in rich media and are used for the ??? targeting of amino-peptidase I. The vesicles formed in rich media are ??? Cvt vesicles and are smaller than autophagosomes and do not appear ??? include bulk cytosol.
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(1997)
J Cell Biol
, vol.139
, pp. 1687-1695
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Baba, M.1
Osumi, M.2
Scott, S.V.3
Klionsky, D.J.4
Ohsumi, Y.5
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51
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0030807624
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A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole
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of special interest. This paper describes the characterization of the vacuolar t-SNARE Vam3p Vam3p is necessary for the correct targeting of multiple ??? hydrolases. In addition, both autophagy and cytoplasm-to-vacuole ??? are disrupted in temperature-sensitive vam3 cells, suggesting that Vam3p ??? a multispecificity receptor for fusion at the vacuole membrane.
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Darsow T, Rieder SE, Emr SD. A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole. of special interest J Cell Biol. 138:1997;517-529 This paper describes the characterization of the vacuolar t-SNARE Vam3p Vam3p is necessary for the correct targeting of multiple ??? hydrolases. In addition, both autophagy and cytoplasm-to-vacuole ??? are disrupted in temperature-sensitive vam3 cells, suggesting that Vam3p ??? a multispecificity receptor for fusion at the vacuole membrane.
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(1997)
J Cell Biol
, vol.138
, pp. 517-529
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Darsow, T.1
Rieder, S.E.2
Emr, S.D.3
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52
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0030940407
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Vam2/Vps41p and Vam6/Vps39p are components of a protein complex on the vacuolar membranes and involved in the vacuolar assembly in ??? yeast Saccharomyces cerevisiae
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Nakamura N, Hirata A, Ohsumi Y, Wada Y. Vam2/Vps41p and Vam6/Vps39p are components of a protein complex on the vacuolar membranes and involved in the vacuolar assembly in ??? yeast Saccharomyces cerevisiae. J Biol Chem. 272:1997;11344-11349.
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(1997)
J Biol Chem
, vol.272
, pp. 11344-11349
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Nakamura, N.1
Hirata, A.2
Ohsumi, Y.3
Wada, Y.4
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53
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0030830765
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A novel RING finger protein complex ??? for a late step in protein transport to the yeast vacuole
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of special interest. This paper demonstrates that Vps18p function is required for ??? endocytic and autophagic protein transport to the vacuole.
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Rieder SE, Emr SD. A novel RING finger protein complex ??? for a late step in protein transport to the yeast vacuole. of special interest Mol Biol Cell. 8:1997;2307-2327 This paper demonstrates that Vps18p function is required for ??? endocytic and autophagic protein transport to the vacuole.
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(1997)
Mol Biol Cell
, vol.8
, pp. 2307-2327
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Rieder, S.E.1
Emr, S.D.2
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