메뉴 건너뛰기




Volumn 133, Issue 2, 1996, Pages 469-483

Intracellular interaction of collagen-specific stress protein HSP47 with newly synthesized procollagen

Author keywords

[No Author keywords available]

Indexed keywords

2,2' BIPYRIDINE; BAFILOMYCIN A1; BREFELDIN A; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 47; MONENSIN; PROCOLLAGEN; UNCLASSIFIED DRUG;

EID: 0029968576     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.133.2.469     Document Type: Article
Times cited : (196)

References (62)
  • 1
    • 0023841862 scopus 로고
    • A view of acidic intracellular compartments
    • Andersen, R.G., and L. Orci. 1988 A view of acidic intracellular compartments J. Cell Biol. 160:539-543
    • (1988) J. Cell Biol. , vol.160 , pp. 539-543
    • Andersen, R.G.1    Orci, L.2
  • 2
    • 0024462447 scopus 로고
    • A novel 58-kDa protein associates, with the Golgi apparatus and microtubules
    • Bloom, O.S , and T A. Brachear 1989. A novel 58-kDa protein associates, with the Golgi apparatus and microtubules J. Cell Biol. 264:16083-16092.
    • (1989) J. Cell Biol. , vol.264 , pp. 16083-16092
    • Bloom, O.S.1    Brachear, T.A.2
  • 3
    • 0022981315 scopus 로고
    • Purification and properties of the groES morphogenetic protein of Eschenchia Coli
    • Chandrasekhar, G.N., K Tilly, C. Woolford, R. Hendrix, and C. Georgopoulos 1986. Purification and properties of the groES morphogenetic protein of Eschenchia Coli. J Biol. Chem. 261:12414-12419.
    • (1986) J Biol. Chem. , vol.261 , pp. 12414-12419
    • Chandrasekhar, G.N.1    Tilly, K.2    Woolford, C.3    Hendrix, R.4    Georgopoulos, C.5
  • 4
    • 0027182875 scopus 로고
    • BiP binds type I procollagen proα chains with mutations in the carboxyl-terminal propeptides synthesized by cells from patients with osteogenesis imperfecta
    • Chessler, S.D , and P H. Byers. 1993. BiP binds type I procollagen proα chains with mutations in the carboxyl-terminal propeptides synthesized by cells from patients with osteogenesis imperfecta. J. Biol. Chem 268:8226-18233
    • (1993) J. Biol. Chem , vol.268 , pp. 8226-18233
    • Chessler, S.D.1    Byers, P.H.2
  • 5
    • 0027203904 scopus 로고
    • Mutations in the carboxyl-terminal propeptide of the proα1(I) chain of type I collagen result in defective chain association and produce lethal osteogenesis imperfecta
    • Chessler, S.D., G.A Wallis, and P H Byers. 1993. Mutations in the carboxyl-terminal propeptide of the proα1(I) chain of type I collagen result in defective chain association and produce lethal osteogenesis imperfecta. J. Biol Chem. 268 18218-18225.
    • (1993) J. Biol Chem. , vol.268 , pp. 18218-18225
    • Chessler, S.D.1    Wallis, G.A.2    Byers, P.H.3
  • 6
    • 0027468569 scopus 로고
    • Parallel regulation of procollagen I and colligin, a collagen-binding protein and a member of the serine protease inhibitor family
    • Clarke, E.P , N. Jam, A. Brickenden, LA. Lorimer, and B D. Sanwal 1993. Parallel regulation of procollagen I and colligin, a collagen-binding protein and a member of the serine protease inhibitor family. J. Cell Biol 121:193-199.
    • (1993) J. Cell Biol , vol.121 , pp. 193-199
    • Clarke, E.P.1    Jam, N.2    Brickenden, A.3    Lorimer, L.A.4    Sanwal, B.D.5
  • 7
    • 0027455464 scopus 로고
    • Posttranslational folding of vesicular stomatitis virus G protein in the ER: Involvement of noncovalent and covalent complexes
    • De Silva, A . I. Braakman, and A. Helenius 1993. Posttranslational folding of vesicular stomatitis virus G protein in the ER: involvement of noncovalent and covalent complexes J Cell Biol. 120.647-655
    • (1993) J Cell Biol. , vol.120 , pp. 647-655
    • De Silva, A.1    Braakman, I.2    Helenius, A.3
  • 8
    • 0025005759 scopus 로고
    • Quality control in the endoplasmic reticulum: Folding and misfolding of vesicular stomatitis virus G protein in cells and in vitro
    • DeSilva, A.M., W.E. Balch, and A. Helenius 1990. Quality control in the endoplasmic reticulum: folding and misfolding of vesicular stomatitis virus G protein in cells and in vitro. J. Cell Biol. 111:857-866.
    • (1990) J. Cell Biol. , vol.111 , pp. 857-866
    • DeSilva, A.M.1    Balch, W.E.2    Helenius, A.3
  • 9
    • 0026677375 scopus 로고
    • Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein
    • Donaldson, J.G., D. Finazzi, and R.D. Klausner. 1992. Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein. Nature (Lond ). 360:350-352.
    • (1992) Nature (Lond ) , vol.360 , pp. 350-352
    • Donaldson, J.G.1    Finazzi, D.2    Klausner, R.D.3
  • 10
    • 0025674154 scopus 로고
    • Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action
    • Donaldson, J.G., J. Lippincott-Schwartz, G S. Bloom, T E. Kreis, and R.D. Klausner. 1990. Dissociation of a 110-kD peripheral membrane protein from the Golgi apparatus is an early event in brefeldin A action. J. Cell Biol. 111: 2295-2306.
    • (1990) J. Cell Biol. , vol.111 , pp. 2295-2306
    • Donaldson, J.G.1    Lippincott-Schwartz, J.2    Bloom, G.S.3    Kreis, T.E.4    Klausner, R.D.5
  • 12
  • 13
    • 0028076031 scopus 로고
    • Folding of VSV G protein: Sequential interaction with BiP and calnexin
    • Hammond, C., and A. Helenius. 1994a. Folding of VSV G protein: sequential interaction with BiP and calnexin. Science (Wash. DC). 266:456-458.
    • (1994) Science (Wash. DC) , vol.266 , pp. 456-458
    • Hammond, C.1    Helenius, A.2
  • 14
    • 0028339518 scopus 로고
    • Quality control in the secretory pathway: Retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus
    • Hammond, C., and A. Helenius. 1994b. Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus. J. Cell Biol 126:41-52.
    • (1994) J. Cell Biol , vol.126 , pp. 41-52
    • Hammond, C.1    Helenius, A.2
  • 15
    • 0027363512 scopus 로고
    • Inhibition of intracellular transport of newly synthesized prolactin by bafilomycin Al in a pituitary tumor cell line, GH3 cells
    • Henomatsu, N., T. Yoshimori, A Yamamoto, Y Moriyama, and Y. Tashiro. 1993 Inhibition of intracellular transport of newly synthesized prolactin by bafilomycin Al in a pituitary tumor cell line, GH3 cells. Eur. J. Cell Biol. 62. 127-139.
    • (1993) Eur. J. Cell Biol. , vol.62 , pp. 127-139
    • Henomatsu, N.1    Yoshimori, T.2    Yamamoto, A.3    Moriyama, Y.4    Tashiro, Y.5
  • 16
    • 0025821002 scopus 로고
    • HSP47: A tissue-specific, transformation-sensitive, collagen-binding heat shock protein of chicken embryo fibroblasts
    • Hirayoshi, K., H. Kudo, H. Takechi, A. Nakai, A. Iwamatsu, K.M. Yamada, and K. Nagata. 1991. HSP47: a tissue-specific, transformation-sensitive, collagen-binding heat shock protein of chicken embryo fibroblasts. Mol. Cell Biol 11:4036-4044.
    • (1991) Mol. Cell Biol , vol.11 , pp. 4036-4044
    • Hirayoshi, K.1    Kudo, H.2    Takechi, H.3    Nakai, A.4    Iwamatsu, A.5    Yamada, K.M.6    Nagata, K.7
  • 17
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • Hurtley, S M., and A. Helenius. 1989 Protein oligomerization in the endoplasmic reticulum. Annu Rev. Cell Biol. 5:277-307.
    • (1989) Annu Rev. Cell Biol. , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 18
    • 0024400060 scopus 로고
    • Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP)
    • Hurtley, S.M., D.G. Bole, H. Hoover-Liny, A Helenius, and C.S. Copeland 1989. Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). J. Cell Biol. 108.2117-2126.
    • (1989) J. Cell Biol. , vol.108 , pp. 2117-2126
    • Hurtley, S.M.1    Bole, D.G.2    Hoover-Liny, H.3    Helenius, A.4    Copeland, C.S.5
  • 19
    • 0027538121 scopus 로고
    • Retrieval of transmembrane proteins to the endoplasmic reticulum
    • Jackson, M.R , T. Nilsson, and P.A. Peterson. 1993. Retrieval of transmembrane proteins to the endoplasmic reticulum. J. Cell Biol. 121:317-333.
    • (1993) J. Cell Biol. , vol.121 , pp. 317-333
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 20
    • 0028172259 scopus 로고
    • Inhibition of procollagen I degradation by colligin: A collagen-binding serpin
    • Jam, N , A. Brickenden, E.H Ball, and B.D. Sanwal. 1994. Inhibition of procollagen I degradation by colligin: a collagen-binding serpin. Arch Biochem Biophys. 314.23-30
    • (1994) Arch Biochem Biophys. , vol.314 , pp. 23-30
    • Jam, N.1    Brickenden, A.2    Ball, E.H.3    Sanwal, B.D.4
  • 21
    • 0028321960 scopus 로고
    • Preferential localization of heat shock protein 47 in dilated endoplasmic reticulum of chick chondrocytes
    • Kambe, K., A Yamamoto, T. Yoshimori, K. Hirayoshi, R. Ogawa, and Y. Tashiro. 1994. Preferential localization of heat shock protein 47 in dilated endoplasmic reticulum of chick chondrocytes. J Histochem. Cytochem. 42:833-841.
    • (1994) J Histochem. Cytochem. , vol.42 , pp. 833-841
    • Kambe, K.1    Yamamoto, A.2    Yoshimori, T.3    Hirayoshi, K.4    Ogawa, R.5    Tashiro, Y.6
  • 22
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner, R.D., J.G Donaldson, and J. Lippincott-Schwartz. 1992. Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116:1071-1080.
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 23
    • 0023644751 scopus 로고
    • Interchain disulfide bond formation in type I and II procollagen
    • Koivu, J., and R. Myllyla. 1987 Interchain disulfide bond formation in type I and II procollagen. J Biol. Chem 262:6159-6164
    • (1987) J Biol. Chem , vol.262 , pp. 6159-6164
    • Koivu, J.1    Myllyla, R.2
  • 24
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R., and S. Kornfeld. 1985. Assembly of asparagine-linked oligosaccharides. Ann Rev. Biochem. 54:631-664.
    • (1985) Ann Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 25
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi, Y., M. Segal, K. Normington, M.-J. Gething, and J. Sambrook. 1988. The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature (Lond.). 332:462-464.
    • (1988) Nature (Lond.) , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.-J.4    Sambrook, J.5
  • 26
    • 0025919701 scopus 로고
    • PtK1 cells contain a nondiffusible, dominant factor that makes the Golgi apparatus resistant to brefeldin A
    • Ktistakis, N.T., M.G. Roth, and G.S. Bloom. 1991. PtK1 cells contain a nondiffusible, dominant factor that makes the Golgi apparatus resistant to brefeldin A. J Cell Biol. 113.1009-1023.
    • (1991) J Cell Biol. , vol.113 , pp. 1009-1023
    • Ktistakis, N.T.1    Roth, M.G.2    Bloom, G.S.3
  • 27
    • 0021354691 scopus 로고
    • Cell surface-associated proteins which bind native type IV collagen or gelatin
    • Kurkmen, M., A. Taylor, J.I. Garrels, and B.L Hogan. 1984. Cell surface-associated proteins which bind native type IV collagen or gelatin J. Biol. Chem. 259:5915-5922.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5915-5922
    • Kurkmen, M.1    Taylor, A.2    Garrels, J.I.3    Hogan, B.L.4
  • 28
    • 0025187298 scopus 로고
    • A human homologue of the yeast HDEL receptor
    • Lewis, M J., and H.R.B. Pelham. 1990. A human homologue of the yeast HDEL receptor Nature (Lond ). 348:162-163
    • (1990) Nature (Lond ) , vol.348 , pp. 162-163
    • Lewis, M.J.1    Pelham, H.R.B.2
  • 29
    • 0026604647 scopus 로고
    • Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum
    • Lewis, M.J., and H.R.B Pelham. 1992. Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum. Cell 68:353-364.
    • (1992) Cell , vol.68 , pp. 353-364
    • Lewis, M.J.1    Pelham, H.R.B.2
  • 30
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • Liberek, K , J. Marszalek, D. Ang, C. Georgopoulos, and M. Zylicz 1991. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl Acad. Sci USA. 88:2874-2878.
    • (1991) Proc. Natl Acad. Sci USA , vol.88 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 31
    • 0025232841 scopus 로고
    • Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway
    • Lippincott-Schwartz, J., J.G. Donaldson, A. Schweizer, E G Berger, H.-P. Hauri, L.C. Yuan, and R.D. Klausner. 1990. Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway. Cell. 60:821-836.
    • (1990) Cell , vol.60 , pp. 821-836
    • Lippincott-Schwartz, J.1    Donaldson, J.G.2    Schweizer, A.3    Berger, E.G.4    Hauri, H.-P.5    Yuan, L.C.6    Klausner, R.D.7
  • 32
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: Evidence for membrane cycling from Golgi ER
    • Lippincott-Schwartz, J., L C Yuan, J.S. Bonifacino, and R.D. Klausner 1989. Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi ER. Cell. 56:801-813
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 33
    • 0028113925 scopus 로고
    • Coexpression of the collagen-binding stress protein HSP47 gene and the α1(I) and α1(III) collagen genes in carbon tetrachloride-induced rat liver fibrosis
    • Masuda, H., M. Fukumoto, K. Hirayoshi, and K Nagata. 1994. Coexpression of the collagen-binding stress protein HSP47 gene and the α1(I) and α1(III) collagen genes in carbon tetrachloride-induced rat liver fibrosis. J Clin. Invest 94:2481-2488.
    • (1994) J Clin. Invest , vol.94 , pp. 2481-2488
    • Masuda, H.1    Fukumoto, M.2    Hirayoshi, K.3    Nagata, K.4
  • 34
    • 0026808864 scopus 로고
    • The endoplasmic reticulum stress protein grp94. in addition to BiP, associates with unassembled immunoglobulin chains
    • Melnick, J., S Aviel, and Y. Argon. 1992. The endoplasmic reticulum stress protein grp94. in addition to BiP, associates with unassembled immunoglobulin chains. J Biol Chem. 267:21303-21306.
    • (1992) J Biol Chem. , vol.267 , pp. 21303-21306
    • Melnick, J.1    Aviel, S.2    Argon, Y.3
  • 35
    • 0028170231 scopus 로고
    • Sequential interaction of the chaperones BiP and grp94 with immunoglobulin chains in the endoplasmic reticulum
    • Melnick, J., J.L Dul, and Y Argon. 1994. Sequential interaction of the chaperones BiP and grp94 with immunoglobulin chains in the endoplasmic reticulum. Nature (Lond.). 370:373-375.
    • (1994) Nature (Lond.) , vol.370 , pp. 373-375
    • Melnick, J.1    Dul, J.L.2    Argon, Y.3
  • 36
    • 0023652396 scopus 로고
    • A c-termmal signal prevents secretion of luminal ER proteins
    • Munro, S., and H.R.B. Pelham, 1987. A c-termmal signal prevents secretion of luminal ER proteins. Cell. 48:899-907.
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.B.2
  • 37
    • 0023918107 scopus 로고
    • Biosynthesis of a novel transformation-sensitive heat-shock protein that binds to collagen
    • Nagata, K., K. Hirayoshi, M. Obara, S. Saga, and K.M Yamada 1988. Biosynthesis of a novel transformation-sensitive heat-shock protein that binds to collagen. J. Biol. Chem. 263:8344-8349.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8344-8349
    • Nagata, K.1    Hirayoshi, K.2    Obara, M.3    Saga, S.4    Yamada, K.M.5
  • 38
    • 0000407117 scopus 로고
    • Interaction of IISP47 with newly synthesized procollagen. and regulation of HSP expression
    • B Maresca and S. Lindoquist, editors. Springer-Verlag. New York
    • Nagata, K., A. Nakai, N. Hosokawa, H. Kudo, H. Takechi, M. Satoh, and K. Hirayoshi. 1991. Interaction of IISP47 with newly synthesized procollagen. and regulation of HSP expression. In Heat Shock. B Maresca and S. Lindoquist, editors. Springer-Verlag. New York 105-110
    • (1991) Heat Shock , pp. 105-110
    • Nagata, K.1    Nakai, A.2    Hosokawa, N.3    Kudo, H.4    Takechi, H.5    Satoh, M.6    Hirayoshi, K.7
  • 39
    • 0022548519 scopus 로고
    • A major collagen-binding protein of chick embryo fibroblasts is a novel heat shock protein
    • Nagata, K., S Saga, and K.M. Yamada 1986 A major collagen-binding protein of chick embryo fibroblasts is a novel heat shock protein. J. Cell BioL 103: 223-229.
    • (1986) J. Cell BioL , vol.103 , pp. 223-229
    • Nagata, K.1    Saga, S.2    Yamada, K.M.3
  • 40
    • 0027310172 scopus 로고
    • Proliferative activation of quiescent rat-1A cells by ΔFosB
    • Nakabeppu, Y., S. Oda, and M. Sekiguchi, 1993. Proliferative activation of quiescent rat-1A cells by ΔFosB. Mol Cell Biol 13:4157-4166.
    • (1993) Mol Cell Biol , vol.13 , pp. 4157-4166
    • Nakabeppu, Y.1    Oda, S.2    Sekiguchi, M.3
  • 41
    • 0025707233 scopus 로고
    • Transformation of BALB/3T3 cells by simian virus 40 causes a decreased synthesis of a collagen-binding heat-shock protein (hsp74)
    • Nakai, A , K Hirayoshi, and K. Nagata. 1990 Transformation of BALB/3T3 cells by simian virus 40 causes a decreased synthesis of a collagen-binding heat-shock protein (hsp74). J Biol Chem. 265.992-999.
    • (1990) J Biol Chem. , vol.265 , pp. 992-999
    • Nakai, A.1    Hirayoshi, K.2    Nagata, K.3
  • 42
    • 0026772964 scopus 로고
    • Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum
    • Nakai, A., M. Satoh, K. Hirayoshi, and K. Nagata. 1992. Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum. J. Cell Biol. 117:903-914.
    • (1992) J. Cell Biol. , vol.117 , pp. 903-914
    • Nakai, A.1    Satoh, M.2    Hirayoshi, K.3    Nagata, K.4
  • 43
    • 0027988156 scopus 로고
    • Interactions between collagen-binding stress protein HSP47 and collagen
    • Natsume, T., T. Koide, S Yokota, K. Hirayoshi, and K Nagata. 1994. Interactions between collagen-binding stress protein HSP47 and collagen. J Biol Chem. 269:31224-31228.
    • (1994) J Biol Chem. , vol.269 , pp. 31224-31228
    • Natsume, T.1    Koide, T.2    Yokota, S.3    Hirayoshi, K.4    Nagata, K.5
  • 44
    • 0024314706 scopus 로고
    • Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum
    • Nilsson, T., M.R Jackcon, and P.A. Peterson 1989 Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum. Cell 58:707-718
    • (1989) Cell , vol.58 , pp. 707-718
    • Nilsson, T.1    Jackcon, M.R.2    Peterson, P.A.3
  • 46
    • 0026635559 scopus 로고
    • Monensin and brefeldin a differentially affect the phosphorylation and sulfation of secretory proteins
    • Rosa, P., S Mantovani, R, Rosboch, and W.B Huttner. 1992. Monensin and brefeldin A differentially affect the phosphorylation and sulfation of secretory proteins. J. Biol. Chem. 267:12227-12232.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12227-12232
    • Rosa, P.1    Mantovani, S.2    Rosboch, R.3    Huttner, W.B.4
  • 47
    • 0017277545 scopus 로고
    • Termination of procollagen chain synthesis by puromycin
    • Rosenbloom, J., R. Endo, and M. Harsch. 1976. Termination of procollagen chain synthesis by puromycin. J. Biol Chem. 251:2070-2076.
    • (1976) J. Biol Chem. , vol.251 , pp. 2070-2076
    • Rosenbloom, J.1    Endo, R.2    Harsch, M.3
  • 48
    • 0023373787 scopus 로고
    • pH-dependent function, purification, and intracellular location of a major collagen-binding glycoprotein
    • Saga, S., K. Nagata, W.-T. Chen, and K.M. Yamada. 1987. pH-dependent function, purification, and intracellular location of a major collagen-binding glycoprotein. J. Cell Biol. 105:517-527.
    • (1987) J. Cell Biol. , vol.105 , pp. 517-527
    • Saga, S.1    Nagata, K.2    Chen, W.-T.3    Yamada, K.M.4
  • 50
    • 0026052099 scopus 로고
    • Distribution of the intermediate elements operating in ER to Golgi transport
    • Saraste, J., and K. Svensson 1991 Distribution of the intermediate elements operating in ER to Golgi transport. J Cell Sci. 100:415-430.
    • (1991) J Cell Sci. , vol.100 , pp. 415-430
    • Saraste, J.1    Svensson, K.2
  • 51
    • 0028031170 scopus 로고
    • Hsp47 and the translation-translocation machinery cooperate in the production of α1(I) chains of type I procollagen
    • Sauk, J.J , T. Smith, K. Norris, and L. Ferreira 1994 Hsp47 and the translation-translocation machinery cooperate in the production of α1(I) chains of type I procollagen J Biol. Chem 269:3941-3946.
    • (1994) J Biol. Chem , vol.269 , pp. 3941-3946
    • Sauk, J.J.1    Smith, T.2    Norris, K.3    Ferreira, L.4
  • 52
    • 0023733211 scopus 로고
    • Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulovesicular compartment at the cis-side of the Golsi apparatus
    • Schweizer, A., J.A. Fransen, T. Bachi, L. Ginsel, and H.-P. Haun. 1988. Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulovesicular compartment at the cis-side of the Golsi apparatus. J Cell Biol. 107:1643-1653.
    • (1988) J Cell Biol. , vol.107 , pp. 1643-1653
    • Schweizer, A.1    Fransen, J.A.2    Bachi, T.3    Ginsel, L.4    Haun, H.-P.5
  • 53
    • 0025610518 scopus 로고
    • Identification of an intermediate compartment involved in protein transport from endoplasmic reticulum to Golgi apparatus
    • Schweizer, A., J A.M Fransen, K Matter, T.E. Kreis, L. Ginsel, and H.-P. Hauri. 1990. Identification of an intermediate compartment involved in protein transport from endoplasmic reticulum to Golgi apparatus. Eur. J. Cell Biol. 53.185-196.
    • (1990) Eur. J. Cell Biol. , vol.53 , pp. 185-196
    • Schweizer, A.1    Fransen, J.A.M.2    Matter, K.3    Kreis, T.E.4    Ginsel, L.5    Hauri, H.-P.6
  • 54
    • 0025362445 scopus 로고
    • ERD2, yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway
    • Semenza, J.C , K.G. Hardwick, N Dean, and H.R.B. Pelham. 1990 ERD2, yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway. Cell 61.1349-1357.
    • (1990) Cell , vol.61 , pp. 1349-1357
    • Semenza, J.C.1    Hardwick, K.G.2    Dean, N.3    Pelham, H.R.B.4
  • 55
    • 0026608252 scopus 로고
    • Molecular cloning of a mouse 47-kda heat shock protein (HSP47). a collagen-binding stress protein, and its expression during the differentiation of F9 teratocarcinoma cells
    • Takechi, H., K. Hirayoshi, H. Kudo, S. Saga, and K. Nagata. 1992 Molecular cloning of a mouse 47-kda heat shock protein (HSP47). a collagen-binding stress protein, and its expression during the differentiation of F9 teratocarcinoma cells. Eur J. Biochem. 206:323-329
    • (1992) Eur J. Biochem. , vol.206 , pp. 323-329
    • Takechi, H.1    Hirayoshi, K.2    Kudo, H.3    Saga, S.4    Nagata, K.5
  • 56
    • 0027439583 scopus 로고
    • Molecular cloning, characterization, subcellular localization and dynamics of p23, the mammalian KDEL receptor
    • Tang, B.L., S.H. Wong, X.L Qi. S.H Low, and W Hong 1993. Molecular cloning, characterization, subcellular localization and dynamics of p23, the mammalian KDEL receptor. J. Cell Biol 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
  • 57
    • 0027724473 scopus 로고
    • Hydrolysis of bound GTP by ARF protein triggers uncoattng of Golgi-derived COP-coated vesicles
    • Tamgawa, G., L Orci, M Amherdt, M. Ravazzola, J.B. Helms, and J .E. Rothman, 1993. Hydrolysis of bound GTP by ARF protein triggers uncoattng of Golgi-derived COP-coated vesicles. J. Cell Biol 123:1365-1371.
    • (1993) J. Cell Biol , vol.123 , pp. 1365-1371
    • Tamgawa, G.1    Orci, L.2    Amherdt, M.3    Ravazzola, M.4    Helms, J.B.5    Rothman, J.E.6
  • 58
    • 0020635123 scopus 로고
    • Perturbation of vesicular traffic with the carboxylic ionophore monensin
    • Tartakoff, A.M. 1983. Perturbation of vesicular traffic with the carboxylic ionophore monensin. Cell. 32:1026-1028.
    • (1983) Cell , vol.32 , pp. 1026-1028
    • Tartakoff, A.M.1
  • 59
    • 0018393233 scopus 로고
    • Monovalent tonophores inhibit secretion of procollagen and fibronectin from cultured human fibroblasts
    • Uchida, N., H. Smilowitz, and M L Tanzer. 1979 Monovalent tonophores inhibit secretion of procollagen and fibronectin from cultured human fibroblasts Proc Natl. Acad. Sci. USA. 76:1868-1872.
    • (1979) Proc Natl. Acad. Sci. USA , vol.76 , pp. 1868-1872
    • Uchida, N.1    Smilowitz, H.2    Tanzer, M.L.3
  • 61
    • 0027513285 scopus 로고
    • pH-dependent binding of KDEL to its receptor in vitro
    • Wilson, D.W., M.J Lewis, and H R.B. Pelham. 1993. pH-dependent binding of KDEL to its receptor in vitro. J. Biol Chem. 268:7465-7468.
    • (1993) J. Biol Chem. , vol.268 , pp. 7465-7468
    • Wilson, D.W.1    Lewis, M.J.2    Pelham, H.R.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.