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Volumn 62, Issue 3, 2000, Pages 642-654

Vacuolar system-associated protein-60: A protein characterized from bovine granulosa and luteal cells that is associated with intracellular vesicles and related to human 80K-H and murine β-glucosidase II

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; COMPLEMENTARY DNA; MEMBRANE PROTEIN; POLYCLONAL ANTIBODY; RECOMBINANT PROTEIN;

EID: 0242692851     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod62.3.642     Document Type: Article
Times cited : (23)

References (57)
  • 1
    • 0002679569 scopus 로고
    • Oocyte-granulosa cell interactions
    • Adashi EY, Leung PCK (eds.), New York: Raven Press
    • Salustri A, Hascall VC, Camaioni A, Yanagishita M. Oocyte-granulosa cell interactions. In: Adashi EY, Leung PCK (eds.), The Ovary. New York: Raven Press; 1993; 209-225.
    • (1993) The Ovary , pp. 209-225
    • Salustri, A.1    Hascall, V.C.2    Camaioni, A.3    Yanagishita, M.4
  • 2
    • 0002466714 scopus 로고
    • The mammalian ovum
    • Knobil E, Neill JD (eds.), New York: Raven Press
    • Wassarman PM, Albertini DF. The mammalian ovum. In: Knobil E, Neill JD (eds.), The Physiology of Reproduction. New York: Raven Press; 1994: 79-122.
    • (1994) The Physiology of Reproduction , pp. 79-122
    • Wassarman, P.M.1    Albertini, D.F.2
  • 3
    • 0029999222 scopus 로고    scopus 로고
    • Mammalian oocyte growth and development in vitro
    • Eppig JJ. Mammalian oocyte growth and development in vitro. Mol Reprod Dev 1996; 44:260-273.
    • (1996) Mol Reprod Dev , vol.44 , pp. 260-273
    • Eppig, J.J.1
  • 4
    • 0025790484 scopus 로고
    • Qualitative and quantitative changes in protein synthesis of bovine follicular cells during the preovulatory period
    • Rabahi F, Monniaux D, Pisselet C, Chupin D, Durand P. Qualitative and quantitative changes in protein synthesis of bovine follicular cells during the preovulatory period. Mol Reprod Dev 1991; 30:265-274.
    • (1991) Mol Reprod Dev , vol.30 , pp. 265-274
    • Rabahi, F.1    Monniaux, D.2    Pisselet, C.3    Chupin, D.4    Durand, P.5
  • 5
    • 0024709671 scopus 로고
    • Isolation of cDNAs encoding a substrate for protein kinase C: Nucleotide sequence and chromosomal mapping of the gene for a human 80K protein
    • Sakai K, Hirai M, Minoshima S, Kudoh J, Fukuyama R, Shimizu N. Isolation of cDNAs encoding a substrate for protein kinase C: nucleotide sequence and chromosomal mapping of the gene for a human 80K protein. Genomics 1989; 5:309-315.
    • (1989) Genomics , vol.5 , pp. 309-315
    • Sakai, K.1    Hirai, M.2    Minoshima, S.3    Kudoh, J.4    Fukuyama, R.5    Shimizu, N.6
  • 6
    • 0025708382 scopus 로고
    • Purification of two distinct proteins of approximate M, 80 000 from human epithelial cells and identification as proper substrates for protein kinase C
    • Hirai M, Shimizu N. Purification of two distinct proteins of approximate M, 80 000 from human epithelial cells and identification as proper substrates for protein kinase C. Biochem J 1990; 270:583-589.
    • (1990) Biochem J , vol.270 , pp. 583-589
    • Hirai, M.1    Shimizu, N.2
  • 7
    • 0030915788 scopus 로고    scopus 로고
    • Identification of the CD45-associated 116-kDa and 80-kDa proteins as the α- and β-subunits of α-glucosidase II
    • Arendt CW, Ostergaard HL. Identification of the CD45-associated 116-kDa and 80-kDa proteins as the α- and β-subunits of α-glucosidase II. J Biol Chem 1997; 272:13117-13125.
    • (1997) J Biol Chem , vol.272 , pp. 13117-13125
    • Arendt, C.W.1    Ostergaard, H.L.2
  • 8
    • 0001263746 scopus 로고    scopus 로고
    • Molecular identity and cellular distribution of advanced glycation endproduct receptors: Relationship of p60 to OST-48 and p90 to 80K-H membrane proteins
    • Li YM, Mitsuhashi T, Wojciechowicz D, Shimizu N, Li J, Stitt A, He CJ, Banerjee D, Vlassara H. Molecular identity and cellular distribution of advanced glycation endproduct receptors: relationship of p60 to OST-48 and p90 to 80K-H membrane proteins. Proc Natl Acad Sci USA 1996; 93:11047-11052.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11047-11052
    • Li, Y.M.1    Mitsuhashi, T.2    Wojciechowicz, D.3    Shimizu, N.4    Li, J.5    Stitt, A.6    He, C.J.7    Banerjee, D.8    Vlassara, H.9
  • 9
    • 0000816317 scopus 로고    scopus 로고
    • Identification of p90, a prominent tyrosine-phosphorylated protein in fibroblast growth factor-stimulated cells, as 80K-H
    • Goh KC, Lim YP, Ong SH, Siak CB, Cao X, Tan YH, Guy GR. Identification of p90, a prominent tyrosine-phosphorylated protein in fibroblast growth factor-stimulated cells, as 80K-H. J Biol Chem 1996; 271:5832-5838.
    • (1996) J Biol Chem , vol.271 , pp. 5832-5838
    • Goh, K.C.1    Lim, Y.P.2    Ong, S.H.3    Siak, C.B.4    Cao, X.5    Tan, Y.H.6    Guy, G.R.7
  • 10
    • 1842372689 scopus 로고    scopus 로고
    • Signal transduction pathway of human libroblast growth factor receptor 3
    • Kanai M, Göke M, Tsunekawa S, Podolsky DK. Signal transduction pathway of human libroblast growth factor receptor 3. J Biol Chem 1997; 272:6621-6628.
    • (1997) J Biol Chem , vol.272 , pp. 6621-6628
    • Kanai, M.1    Göke, M.2    Tsunekawa, S.3    Podolsky, D.K.4
  • 11
    • 0029910144 scopus 로고    scopus 로고
    • Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly hound noncatalytic HDEL-containing subunit
    • Trombetta ES, Simons JF, Helenius A. Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly hound noncatalytic HDEL-containing subunit. J Biol Chem 1996; 44:27509-27516.
    • (1996) J Biol Chem , vol.44 , pp. 27509-27516
    • Trombetta, E.S.1    Simons, J.F.2    Helenius, A.3
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 1979; 76:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 14
    • 0022260239 scopus 로고
    • Proteins transferred to nitrocellulose for use as immunogens
    • Knudsen KA. Proteins transferred to nitrocellulose for use as immunogens. Anal Biochem 1985; 147:285-288.
    • (1985) Anal Biochem , vol.147 , pp. 285-288
    • Knudsen, K.A.1
  • 16
    • 0023277545 scopus 로고    scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 1997; 162:156-159.
    • (1997) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 17
    • 0028114351 scopus 로고
    • Structure of the bovine follicle-stimulating hormone receptor complementary DNA and expression in bovine tissues
    • Houde A, Lambert A, Saumande J, Silversides DW, Lussier JG. Structure of the bovine follicle-stimulating hormone receptor complementary DNA and expression in bovine tissues. Mol Reprod Dev 1994; 39:127-135.
    • (1994) Mol Reprod Dev , vol.39 , pp. 127-135
    • Houde, A.1    Lambert, A.2    Saumande, J.3    Silversides, D.W.4    Lussier, J.G.5
  • 20
    • 0027105007 scopus 로고
    • A knowledge base for predicting protein localization sites in eukaryotic cells
    • Nakai K, Kanehisa M. A knowledge base for predicting protein localization sites in eukaryotic cells. Genomics 1992; 14:897-911.
    • (1992) Genomics , vol.14 , pp. 897-911
    • Nakai, K.1    Kanehisa, M.2
  • 21
    • 0023967439 scopus 로고
    • Rapid, reversible staining of Northern blots prior to hybridization
    • Herrin DL, Schmidt GW. Rapid, reversible staining of Northern blots prior to hybridization. Biotechniques 1988; 6:196-200.
    • (1988) Biotechniques , vol.6 , pp. 196-200
    • Herrin, D.L.1    Schmidt, G.W.2
  • 22
    • 0021770769 scopus 로고
    • The use of heparin as a simple cost-effective means of controlling background in nucleic acid hybridization procedures
    • Singh L, Jones KW. The use of heparin as a simple cost-effective means of controlling background in nucleic acid hybridization procedures. Nucleic Acids Res 1984; 12:5627-5638.
    • (1984) Nucleic Acids Res , vol.12 , pp. 5627-5638
    • Singh, L.1    Jones, K.W.2
  • 24
    • 2142659145 scopus 로고
    • Isolation of nuclei by sucrose gradient centrifugation
    • Ausubet FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K (eds.), New York: John Wiley & Sons, Inc.; section 4.10.6
    • Greenberg ME, Bender TP. Isolation of nuclei by sucrose gradient centrifugation. In: Ausubet FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K (eds.), Current Protocols in Molecular Biology. New York: John Wiley & Sons, Inc.; 1994: section 4.10.6.
    • (1994) Current Protocols in Molecular Biology
    • Greenberg, M.E.1    Bender, T.P.2
  • 25
    • 0006121218 scopus 로고
    • Endoglycosidase and glycoamidase release of N-linked oligosaccharides
    • Ausubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K (eds.), New York: John Wiley & Sons, Inc.; section 17.13.1
    • Freeze HH. Endoglycosidase and glycoamidase release of N-linked oligosaccharides. In: Ausubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K (eds.), Current Protocols in Molecular Biology. New York: John Wiley & Sons, Inc.; 1994: section 17.13.1.
    • (1994) Current Protocols in Molecular Biology
    • Freeze, H.H.1
  • 26
    • 0026725764 scopus 로고
    • The dephosphorylation of insulin and epidermal growth factor receptors. Role of endosome-associated phosphotyrosine phosphatase(s)
    • Faure R, Baquiran G, Bergcron JJ, Posner BI. The dephosphorylation of insulin and epidermal growth factor receptors. Role of endosome-associated phosphotyrosine phosphatase(s). J Biol Chem 1992; 267: 11215-11221.
    • (1992) J Biol Chem , vol.267 , pp. 11215-11221
    • Faure, R.1    Baquiran, G.2    Bergcron, J.J.3    Posner, B.I.4
  • 27
    • 0021894454 scopus 로고
    • Uptake of insulin and other ligands into receptor-rich endocytic components of target cells: The endosomal apparatus
    • Bergeron JJM, Cruz J, Khan MN, Posner BI. Uptake of insulin and other ligands into receptor-rich endocytic components of target cells: the endosomal apparatus. Annu Rev Physiol 1985; 47:383-403.
    • (1985) Annu Rev Physiol , vol.47 , pp. 383-403
    • Bergeron, J.J.M.1    Cruz, J.2    Khan, M.N.3    Posner, B.I.4
  • 29
    • 0033305427 scopus 로고    scopus 로고
    • High expression of bovine α glutathione S-transferase (GSTA1, GSTA2) subunits is mainly associated with steroidogenically active cells and regulated by gonadotropins in bovine ovarian follicles
    • Rabahi F, Brûlé S, Sirois J, Beckers J-F, Silversides DW, Lussier JG. High expression of bovine α glutathione S-transferase (GSTA1, GSTA2) subunits is mainly associated with steroidogenically active cells and regulated by gonadotropins in bovine ovarian follicles. Endocrinology 1999; 140:3507-3517.
    • (1999) Endocrinology , vol.140 , pp. 3507-3517
    • Rabahi, F.1    Brûlé, S.2    Sirois, J.3    Beckers, J.-F.4    Silversides, D.W.5    Lussier, J.G.6
  • 30
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of a protein. J Mol Biol 1982; 157:105-132.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 31
    • 0023665902 scopus 로고
    • An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs
    • Kozak M. An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res 1987; 15:8125-8148.
    • (1987) Nucleic Acids Res , vol.15 , pp. 8125-8148
    • Kozak, M.1
  • 32
    • 0023928974 scopus 로고
    • Transcending the impenetrable: How proteins come to terms with membranes
    • Heijne GV. Transcending the impenetrable: how proteins come to terms with membranes. Biochim Biophys Acta 1988; 947:307-333.
    • (1988) Biochim Biophys Acta , vol.947 , pp. 307-333
    • Heijne, G.V.1
  • 33
    • 0030836789 scopus 로고    scopus 로고
    • Expression of a cDNA encoding the glucose trimming enzyme glucosidase II in CHO cells and molecular characterization of the enzyme deficiency in a mutant mouse lymphoma cell line
    • Flura T, Brada D, Ziak M, Roth J. Expression of a cDNA encoding the glucose trimming enzyme glucosidase II in CHO cells and molecular characterization of the enzyme deficiency in a mutant mouse lymphoma cell line. Glycobiology 1997; 7:617-624.
    • (1997) Glycobiology , vol.7 , pp. 617-624
    • Flura, T.1    Brada, D.2    Ziak, M.3    Roth, J.4
  • 34
    • 0030771750 scopus 로고    scopus 로고
    • Affinity purification and characterization of glucosidase II from pig liver
    • Hentges A, Bause E. Affinity purification and characterization of glucosidase II from pig liver. J Biol Chem 1997; 378:1031-1038.
    • (1997) J Biol Chem , vol.378 , pp. 1031-1038
    • Hentges, A.1    Bause, E.2
  • 35
    • 0021245984 scopus 로고
    • Isolation of a homogeneous glucosidase II from pig kidney microsomes
    • Brada D, Dubach UC. Isolation of a homogeneous glucosidase II from pig kidney microsomes. Eur J Biochem 1984; 141:149-156.
    • (1984) Eur J Biochem , vol.141 , pp. 149-156
    • Brada, D.1    Dubach, U.C.2
  • 36
    • 0032982719 scopus 로고    scopus 로고
    • Alternative splicing of transcripts encoding the α- and β-subunits of mouse glucosidase II in T lymphocytes
    • Arendt CW, Dawicki W, Ostergaard HL. Alternative splicing of transcripts encoding the α- and β-subunits of mouse glucosidase II in T lymphocytes. Glycobiology 1999; 9:277-283.
    • (1999) Glycobiology , vol.9 , pp. 277-283
    • Arendt, C.W.1    Dawicki, W.2    Ostergaard, H.L.3
  • 37
    • 0024396312 scopus 로고
    • Crystal structures of the helix-loop-helix calcium-binding proteins
    • Strynadka NCJ, James MNG. Crystal structures of the helix-loop-helix calcium-binding proteins. Annu Rev Biochem 1989; 58:951-998.
    • (1989) Annu Rev Biochem , vol.58 , pp. 951-998
    • Strynadka, N.C.J.1    James, M.N.G.2
  • 38
    • 0026771336 scopus 로고
    • Evolution of EF-hand calcium-modulated proteins. II. Domains of several subfamilies have diverse evolutionary histories
    • Nakayama S, Moncrief ND, Kretsinger RH. Evolution of EF-hand calcium-modulated proteins. II. Domains of several subfamilies have diverse evolutionary histories. J Mol Evol 1992; 34:416-448.
    • (1992) J Mol Evol , vol.34 , pp. 416-448
    • Nakayama, S.1    Moncrief, N.D.2    Kretsinger, R.H.3
  • 39
    • 0025978546 scopus 로고
    • Intracellular calcium-binding proteins: More sites than insights
    • Heizmann CW, Hunziker W. Intracellular calcium-binding proteins: more sites than insights. Trends Biochem Sci 1991; 16:98-103.
    • (1991) Trends Biochem Sci , vol.16 , pp. 98-103
    • Heizmann, C.W.1    Hunziker, W.2
  • 40
    • 0027439695 scopus 로고
    • 2+-binding protein with multiple EF-hand motifs and a carboxyl-terminal HDEL sequence
    • 2+-binding protein with multiple EF-hand motifs and a carboxyl-terminal HDEL sequence. J Biol Chem 1993; 268:699-705.
    • (1993) J Biol Chem , vol.268 , pp. 699-705
    • Ozawa, M.1    Muramatsu, T.2
  • 41
    • 0028339802 scopus 로고
    • The endoplasmic reticulum calcium-binding protein of 55 kDa is a novel EF-hand protein retained in the endoplasmic reticulum by a carboxyl-terminal His-Asp-Glu-Leu motif
    • Weis K, Griffiths G, Lamond Al. The endoplasmic reticulum calcium-binding protein of 55 kDa is a novel EF-hand protein retained in the endoplasmic reticulum by a carboxyl-terminal His-Asp-Glu-Leu motif. J Biol Chem 1994; 269:19142-19150.
    • (1994) J Biol Chem , vol.269 , pp. 19142-19150
    • Weis, K.1    Griffiths, G.2    Lamond, Al.3
  • 42
    • 0026355413 scopus 로고
    • Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations
    • Hunter T. Sefton BM (eds.), San Diego: Academic Press Inc.
    • Pearson RB, Kemp BE. Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations. In: Hunter T. Sefton BM (eds.), Methods in Enzymology, Part A, Vol. 200. San Diego: Academic Press Inc.; 1991: 62-81.
    • (1991) Methods in Enzymology , vol.200 , Issue.PART A , pp. 62-81
    • Pearson, R.B.1    Kemp, B.E.2
  • 43
    • 0025757377 scopus 로고
    • The COOH terminus of several liver carboxylesterases targets these enzymes to the lumen of the endoplasmic reticulum
    • Robbi M, Beaufay H. The COOH terminus of several liver carboxylesterases targets these enzymes to the lumen of the endoplasmic reticulum. J Biol Chem 1991; 266:20498-20503.
    • (1991) J Biol Chem , vol.266 , pp. 20498-20503
    • Robbi, M.1    Beaufay, H.2
  • 44
    • 0030450784 scopus 로고    scopus 로고
    • The dynamic organisation of the secretory pathway
    • Pelham HRB. The dynamic organisation of the secretory pathway. Cell Struct Funct 1996; 21:413-419.
    • (1996) Cell Struct Funct , vol.21 , pp. 413-419
    • Pelham, H.R.B.1
  • 45
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro S, Pelham HRB. A C-terminal signal prevents secretion of luminal ER proteins. Cell 1987; 48:899-907.
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.B.2
  • 46
    • 0027439583 scopus 로고
    • Molecular cloning, characterization, subcellular localization and dynamics of p23, the mammalian KDEL receptor
    • Tang BL, Wong SH, Qi XL, Low SH, Hong W. Molecular cloning, characterization, subcellular localization and dynamics of p23, the mammalian KDEL receptor. J Cell Biol 1993; 120:325-338.
    • (1993) J Cell Biol , vol.120 , pp. 325-338
    • Tang, B.L.1    Wong, S.H.2    Qi, X.L.3    Low, S.H.4    Hong, W.5
  • 47
    • 0025045118 scopus 로고
    • Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal
    • Yoshimori T, Semba T, Takemoto H, Akagi S, Yamamoto A, Tashiro Y. Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal. J Biol Chem 1990; 265:15984-15990.
    • (1990) J Biol Chem , vol.265 , pp. 15984-15990
    • Yoshimori, T.1    Semba, T.2    Takemoto, H.3    Akagi, S.4    Yamamoto, A.5    Tashiro, Y.6
  • 48
    • 0026689538 scopus 로고
    • Heavy chain binding protein (BiP/GRP78) and endoplasmin are exported from the endoplasmic reticulum in rat exocrine pancreatic cells, similar to protein disulfide-isomerase
    • Takemoto H, Yoshimori T, Yamamoto A, Miyata Y, Yahara I, Inoue K, Tashiro Y. Heavy chain binding protein (BiP/GRP78) and endoplasmin are exported from the endoplasmic reticulum in rat exocrine pancreatic cells, similar to protein disulfide-isomerase. Arch Biochem Biophys 1992; 296:129-136.
    • (1992) Arch Biochem Biophys , vol.296 , pp. 129-136
    • Takemoto, H.1    Yoshimori, T.2    Yamamoto, A.3    Miyata, Y.4    Yahara, I.5    Inoue, K.6    Tashiro, Y.7
  • 49
    • 0028915798 scopus 로고
    • Proline-rich sequences that bind to Src homology 3 domains with individual specificities
    • Alexandropoulos K, Cheng GH, Baltimore D. Proline-rich sequences that bind to Src homology 3 domains with individual specificities. Proc Natl Acad Sci USA 1995; 92:3110-3114.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3110-3114
    • Alexandropoulos, K.1    Cheng, G.H.2    Baltimore, D.3
  • 52
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calncxin in glycoprotein folding and quality control
    • Hammond C, Braakman I, Helenius A. Role of N-linked oligosaccharide recognition, glucose trimming, and calncxin in glycoprotein folding and quality control. Proc Natl Acad Sci USA 1994; 91:913-917.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 53
    • 0023441662 scopus 로고
    • Purification and characterization of glucosidase II involved in N-linked glycoprotein processing in bovine mammary gland
    • Saxena S, Shailubhai K, Dong-Yu B, Vijay IK. Purification and characterization of glucosidase II involved in N-linked glycoprotein processing in bovine mammary gland. Biochem J 1987; 247:563-570.
    • (1987) Biochem J , vol.247 , pp. 563-570
    • Saxena, S.1    Shailubhai, K.2    Dong-Yu, B.3    Vijay, I.K.4
  • 54
    • 0020354870 scopus 로고
    • Purification and characterization of glucosidase II, and endoplasmic reticulum hydrolase involved in glycoprotein biosynthesis
    • Burns DM, Touster O. Purification and characterization of glucosidase II, and endoplasmic reticulum hydrolase involved in glycoprotein biosynthesis. J Biol Chem 1982; 257:9991-10000.
    • (1982) J Biol Chem , vol.257 , pp. 9991-10000
    • Burns, D.M.1    Touster, O.2
  • 55
    • 0023654298 scopus 로고
    • Glucosidase II, a protein of the endoplasmic reticulum with high mannose oligosaccharide chains and a rapid turnover
    • Strous GJ, Van Kerkhof P, Brok R, Roth J, Brada D. Glucosidase II, a protein of the endoplasmic reticulum with high mannose oligosaccharide chains and a rapid turnover. J Biol Chem 1987; 262:3620-3625.
    • (1987) J Biol Chem , vol.262 , pp. 3620-3625
    • Strous, G.J.1    Van Kerkhof, P.2    Brok, R.3    Roth, J.4    Brada, D.5
  • 56
    • 0022467150 scopus 로고
    • Immunolocalization of the oligosaccharide trimming enzyme glucosidase II
    • Lucocq JM, Brada D, Roth J. Immunolocalization of the oligosaccharide trimming enzyme glucosidase II. J Cell Biol 1986; 102:2137-2146.
    • (1986) J Cell Biol , vol.102 , pp. 2137-2146
    • Lucocq, J.M.1    Brada, D.2    Roth, J.3
  • 57
    • 0025174608 scopus 로고
    • Cell type-specific post-Golgi apparatus localization of a "resident" endoplasmic reticulum glycoprotein, glucosidase II
    • Brada D, Kerjaschki D, Roth J. Cell type-specific post-Golgi apparatus localization of a "resident" endoplasmic reticulum glycoprotein, glucosidase II. J Cell Biol 1990; 110:309-318.
    • (1990) J Cell Biol , vol.110 , pp. 309-318
    • Brada, D.1    Kerjaschki, D.2    Roth, J.3


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