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Volumn 499, Issue , 2011, Pages 167-182

Hsp47 as a collagen-specific molecular chaperone

Author keywords

Autophagy; Collagen; Collagen related disorder; Endoplasmic reticulum; Hsp47; Molecular chaperone; Serpin H1

Indexed keywords

CHAPERONE; COLLAGEN; COLLAGEN BINDING PROTEIN; HEAT SHOCK PROTEIN 47; PROCOLLAGEN; UBIQUITIN;

EID: 79959326422     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/B978-0-12-386471-0.00009-2     Document Type: Chapter
Times cited : (108)

References (74)
  • 1
    • 38549103628 scopus 로고    scopus 로고
    • Protein quality control in the early secretory pathway
    • DOI 10.1038/sj.emboj.7601974, PII 7601974
    • T. Anelli, and R. Sitia Protein quality control in the early secretory pathway EMBO J. 27 2008 315 327 (Pubitemid 351161662)
    • (2008) EMBO Journal , vol.27 , Issue.2 , pp. 315-327
    • Anelli, T.1    Sitia, R.2
  • 2
    • 0018959643 scopus 로고
    • Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Role of disulfide bridges and peptide bond isomerization
    • DOI 10.1111/j.1432-1033.1980.tb04610.x
    • H.P. Bachinger, P. Bruckner, R. Timpl, D.J. Prockop, and J. Engel Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Role of disulfide bridges and peptide bond isomerization Eur. J. Biochem. 106 1980 619 632 (Pubitemid 10025788)
    • (1980) European Journal of Biochemistry , vol.106 , Issue.2 , pp. 619-632
    • Bachinger, H.P.1    Bruckner, P.2    Timpl, R.3
  • 3
    • 60349120776 scopus 로고    scopus 로고
    • Genetic diseases of connective tissues: Cellular and extracellular effects of ECM mutations
    • J.F. Bateman, R.P. Boot-Handford, and S.R. Lamande Genetic diseases of connective tissues: Cellular and extracellular effects of ECM mutations Nat. Rev. Genet. 10 2009 173 183
    • (2009) Nat. Rev. Genet. , vol.10 , pp. 173-183
    • Bateman, J.F.1    Boot-Handford, R.P.2    Lamande, S.R.3
  • 4
    • 0015624009 scopus 로고
    • The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen
    • R.A. Berg, and D.J. Prockop The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen Biochem. Biophys. Res. Commun. 52 1973 115 120
    • (1973) Biochem. Biophys. Res. Commun. , vol.52 , pp. 115-120
    • Berg, R.A.1    Prockop, D.J.2
  • 6
    • 20444362433 scopus 로고    scopus 로고
    • Expression of HSP47, a collagen-specific chaperone, in normal and diseased human liver
    • DOI 10.1038/labinvest.3700271
    • K.E. Brown, K.A. Broadhurst, M.M. Mathahs, E.M. Brunt, and W.N. Schmidt Expression of HSP47, a collagen-specific chaperone, in normal and diseased human liver Lab. Invest. 85 2005 789 797 (Pubitemid 40799708)
    • (2005) Laboratory Investigation , vol.85 , Issue.6 , pp. 789-797
    • Brown, K.E.1    Broadhurst, K.A.2    Mathahs, M.M.3    Brunt, E.M.4    Schmidt, W.N.5
  • 7
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • B. Bukau, J. Weissman, and A. Horwich Molecular chaperones and protein quality control Cell 125 2006 443 451
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 8
    • 0030812651 scopus 로고    scopus 로고
    • The C-propeptide domain of procollagen can be replaced with a transmembrane domain without affecting trimer formation or collagen triple helix folding during biosynthesis
    • N.J. Bulleid, J.A. Dalley, and J.F. Lees The C-propeptide domain of procollagen can be replaced with a transmembrane domain without affecting trimer formation or collagen triple helix folding during biosynthesis EMBO J. 16 1997 6694 6701 (Pubitemid 27503482)
    • (1997) EMBO Journal , vol.16 , Issue.22 , pp. 6694-6701
    • Bulleid, N.J.1    Dalley, J.A.2    Lees, J.F.3
  • 9
    • 0023403278 scopus 로고
    • Differentiation defective mutants of skeletal myoblasts altered in a gelatin-binding glycoprotein
    • G.A. Cates, D. Nandan, A.M. Brickenden, and B.D. Sanwal Differentiation defective mutants of skeletal myoblasts altered in a gelatin-binding glycoprotein Biochem. Cell Biol. 65 1987 767 775
    • (1987) Biochem. Cell Biol. , vol.65 , pp. 767-775
    • Cates, G.A.1    Nandan, D.2    Brickenden, A.M.3    Sanwal, B.D.4
  • 11
    • 0023815508 scopus 로고
    • Cleavage of type I and type II procollagens by type I/II procollagen N-proteinase. Correlation of kinetic constants with the predicted conformations of procollagen substrates
    • K.E. Dombrowski, and D.J. Prockop Cleavage of type I and type II procollagens by type I/II procollagen N-proteinase. Correlation of kinetic constants with the predicted conformations of procollagen substrates J. Biol. Chem. 263 1988 16545 16552 (Pubitemid 18268831)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.32 , pp. 16545-16552
    • Dombrowski, K.E.1    Prockop, D.J.2
  • 13
    • 0025904728 scopus 로고
    • The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper
    • J. Engel, and D.J. Prockop The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper Annu. Rev. Biophys. Biophys. Chem. 20 1991 137 152
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 137-152
    • Engel, J.1    Prockop, D.J.2
  • 14
    • 0033600789 scopus 로고    scopus 로고
    • Proteasomal degradation of unassembled mutant type I collagen pro-alpha1(I) chains
    • J. Fitzgerald, S.R. Lamande, and J.F. Bateman Proteasomal degradation of unassembled mutant type I collagen pro-alpha1(I) chains J. Biol. Chem. 274 1999 27392 27398
    • (1999) J. Biol. Chem. , vol.274 , pp. 27392-27398
    • Fitzgerald, J.1    Lamande, S.R.2    Bateman, J.F.3
  • 15
    • 58149398233 scopus 로고    scopus 로고
    • Atg4B(C74A) hampers autophagosome closure: A useful protein for inhibiting autophagy
    • N. Fujita, T. Noda, and T. Yoshimori Atg4B(C74A) hampers autophagosome closure: A useful protein for inhibiting autophagy Autophagy 5 2009 88 89
    • (2009) Autophagy , vol.5 , pp. 88-89
    • Fujita, N.1    Noda, T.2    Yoshimori, T.3
  • 17
    • 2442451197 scopus 로고    scopus 로고
    • Intracellular trafficking and degradation of unassociated proα2 chains of collagen type I
    • DOI 10.1016/j.yexcr.2004.01.029, PII S0014482704000655
    • M.G. Gotkin, C.R. Ripley, S.R. Lamande, J.F. Bateman, and R.S. Bienkowski Intracellular trafficking and degradation of unassociated proalpha2 chains of collagen type I Exp. Cell Res. 296 2004 307 316 (Pubitemid 38624651)
    • (2004) Experimental Cell Research , vol.296 , Issue.2 , pp. 307-316
    • Gotkin, M.G.1    Ripley, C.R.2    Lamande, S.R.3    Bateman, J.F.4    Bienkowski, R.S.5
  • 18
    • 0034649591 scopus 로고    scopus 로고
    • Protein-specific chaperones: The role of hsp47 begins to gel
    • DOI 10.1016/S0960-9822(00)00850-2
    • L.M. Hendershot, and N.J. Bulleid Protein-specific chaperones: The role of hsp47 begins to gel Curr. Biol. 10 2000 R912 R915 (Pubitemid 32062651)
    • (2000) Current Biology , vol.10 , Issue.24
    • Hendershot, L.M.1    Bulleid, N.J.2
  • 20
    • 0025821002 scopus 로고
    • HSP47: A tissue-specific, transformation-sensitive, collagen-binding heat shock protein of chicken embryo fibroblasts
    • K. Hirayoshi, H. Kudo, H. Takechi, A. Nakai, A. Iwamatsu, K.M. Yamada, and K. Nagata HSP47: A tissue-specific, transformation-sensitive, collagen-binding heat shock protein of chicken embryo fibroblasts Mol. Cell. Biol. 11 1991 4036 4044 (Pubitemid 21895793)
    • (1991) Molecular and Cellular Biology , vol.11 , Issue.8 , 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
  • 21
    • 75649114551 scopus 로고    scopus 로고
    • Mechanism and components of endoplasmic reticulum-associated degradation
    • J. Hoseki, R. Ushioda, and K. Nagata Mechanism and components of endoplasmic reticulum-associated degradation J. Biochem. 147 2010 19 25
    • (2010) J. Biochem. , vol.147 , pp. 19-25
    • Hoseki, J.1    Ushioda, R.2    Nagata, K.3
  • 22
    • 0023110803 scopus 로고
    • 2+ -binding glycoprotein. Evidence for the localisation of colligin in the endoplasmic reticulum
    • DOI 10.1111/j.1432-1033.1987.tb10736.x
    • 2+ -binding glycoprotein. Evidence for the localisation of colligin in the endoplasmic reticulum Eur. J. Biochem. 163 1987 57 65 (Pubitemid 17015425)
    • (1987) European Journal of Biochemistry , vol.163 , Issue.1 , pp. 57-65
    • Hughes, R.C.1    Taylor, A.2    Sage, H.3    Hogan, B.L.M.4
  • 24
    • 73449083755 scopus 로고    scopus 로고
    • Autophagy eliminates a specific species of misfolded procollagen and plays a protective role in cell survival against ER stress
    • Y. Ishida, and K. Nagata Autophagy eliminates a specific species of misfolded procollagen and plays a protective role in cell survival against ER stress Autophagy 5 2009 1217 1219
    • (2009) Autophagy , vol.5 , pp. 1217-1219
    • Ishida, Y.1    Nagata, K.2
  • 25
    • 33745747824 scopus 로고    scopus 로고
    • Type I collagen in Hsp47-null cells is aggregated in endoplasmic reticulum and deficient in N-propeptide processing and fibrillogenesis
    • DOI 10.1091/mbc.E05-11-1065
    • Y. Ishida, H. Kubota, A. Yamamoto, A. Kitamura, H.P. Bachinger, and K. Nagata Type I collagen in Hsp47-null cells is aggregated in endoplasmic reticulum and deficient in N-propeptide processing and fibrillogenesis Mol. Biol. Cell 17 2006 2346 2355 (Pubitemid 44011749)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.5 , pp. 2346-2355
    • Ishida, Y.1    Kubota, H.2    Yamamoto, A.3    Kitamura, A.4    Bachinger, H.P.5    Nagata, K.6
  • 28
    • 0033521011 scopus 로고    scopus 로고
    • Substrate recognition of collagen-specific molecular chaperone HSP47: Structural requirements and binding regulation
    • T. Koide, S. Asada, and K. Nagata Substrate recognition of collagen-specific molecular chaperone HSP47. Structural requirements and binding regulation J. Biol. Chem. 274 1999 34523 34526 (Pubitemid 129509484)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.49 , pp. 34523-34526
    • Koide, T.1    Asada, S.2    Nagata, K.3
  • 29
    • 0034623246 scopus 로고    scopus 로고
    • Conformational requirements of collagenous peptides for recognition by the chaperone protein HSP47
    • T. Koide, A. Aso, T. Yorihuzi, and K. Nagata Conformational requirements of collagenous peptides for recognition by the chaperone protein HSP47 J. Biol. Chem. 275 2000 27957 27963
    • (2000) J. Biol. Chem. , vol.275 , pp. 27957-27963
    • Koide, T.1    Aso, A.2    Yorihuzi, T.3    Nagata, K.4
  • 30
    • 0037155282 scopus 로고    scopus 로고
    • Xaa-Arg-Gly triplets in the collagen triple helix are dominant binding sites for the molecular chaperone HSP47
    • DOI 10.1074/jbc.M106497200
    • T. Koide, Y. Takahara, S. Asada, and K. Nagata Xaa-Arg-Gly triplets in the collagen triple helix are dominant binding sites for the molecular chaperone HSP47 J. Biol. Chem. 277 2002 6178 6182 (Pubitemid 34968407)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.8 , pp. 6178-6182
    • Koide, T.1    Takahara, Y.2    Asada, S.3    Nagata, K.4
  • 34
    • 34247398719 scopus 로고    scopus 로고
    • Constitutive autophagy: Vital role in clearance of unfavorable proteins in neurons
    • DOI 10.1038/sj.cdd.4402120, PII 4402120
    • M. Komatsu, T. Ueno, S. Waguri, Y. Uchiyama, E. Kominami, and K. Tanaka Constitutive autophagy: Vital role in clearance of unfavorable proteins in neurons Cell Death Differ. 14 2007 887 894 (Pubitemid 46629828)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.5 , pp. 887-894
    • Komatsu, M.1    Ueno, T.2    Waguri, S.3    Uchiyama, Y.4    Kominami, E.5    Tanaka, K.6
  • 37
    • 0021354691 scopus 로고
    • Cell surface-associated proteins which bind native type IV collagen or gelatin
    • M. Kurkinen, A. Taylor, J.I. Garrels, and B.L. Hogan Cell surface-associated proteins which bind native type IV collagen or gelatin J. Biol. Chem. 259 1984 5915 5922 (Pubitemid 14142736)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.9 , pp. 5915-5922
    • Kurkinen, M.1    Taylor, A.2    Garrels, J.I.3    Hogan, B.L.M.4
  • 38
    • 0033208952 scopus 로고    scopus 로고
    • Procollagen folding and assembly: The role of endoplasmic reticulum enzymes and molecular chaperones
    • DOI 10.1006/scdb.1999.0317, PII S1084952199903178
    • S.R. Lamande, and J.F. Bateman Procollagen folding and assembly: The role of endoplasmic reticulum enzymes and molecular chaperones Semin. Cell Dev. Biol. 10 1999 455 464 (Pubitemid 129513233)
    • (1999) Seminars in Cell and Developmental Biology , vol.10 , Issue.5 , pp. 455-464
    • Lamande, S.R.1    Bateman, J.F.2
  • 41
    • 41749116397 scopus 로고    scopus 로고
    • Procollagen triple helix assembly: An unconventional chaperone-assisted folding paradigm
    • E. Makareeva, and S. Leikin Procollagen triple helix assembly: An unconventional chaperone-assisted folding paradigm PLoS ONE 2 2007 e1029
    • (2007) PLoS ONE , vol.2 , pp. 1029
    • Makareeva, E.1    Leikin, S.2
  • 42
  • 43
    • 12344322951 scopus 로고    scopus 로고
    • Accumulation of type IV collagen in dilated ER leads to apoptosis in Hsp47-knockout mouse embryos via induction of CHOP
    • DOI 10.1242/jcs.01514
    • T. Marutani, A. Yamamoto, N. Nagai, H. Kubota, and K. Nagata Accumulation of type IV collagen in dilated ER leads to apoptosis in Hsp47-knockout mouse embryos via induction of CHOP J. Cell Sci. 117 2004 5913 5922 (Pubitemid 40123957)
    • (2004) Journal of Cell Science , vol.117 , Issue.24 , pp. 5913-5922
    • Muratani, T.1    Yamamoto, A.2    Nagai, N.3    Kubota, H.4    Nagata, K.5
  • 44
    • 0028113925 scopus 로고
    • Coexpression of the collagen-binding stress protein HSP47 gene and the alpha 1(I) and alpha 1(III) collagen genes in carbon tetrachloride-induced rat liver fibrosis
    • H. Masuda, M. Fukumoto, K. Hirayoshi, and K. Nagata Coexpression of the collagen-binding stress protein HSP47 gene and the alpha 1(I) and alpha 1(III) collagen genes in carbon tetrachloride-induced rat liver fibrosis J. Clin. Invest. 94 1994 2481 2488
    • (1994) J. Clin. Invest. , vol.94 , pp. 2481-2488
    • Masuda, H.1    Fukumoto, M.2    Hirayoshi, K.3    Nagata, K.4
  • 45
    • 4644234938 scopus 로고    scopus 로고
    • Insufficient folding of type IV collagen and formation of abnormal basement membrane-like structure in embryoid bodies derived from Hsp47-null embryonic stem cells
    • DOI 10.1091/mbc.E04-01-0050
    • Y. Matsuoka, H. Kubota, E. Adachi, N. Nagai, T. Marutani, N. Hosokawa, and K. Nagata Insufficient folding of type IV collagen and formation of abnormal basement membrane-like structure in embryoid bodies derived from Hsp47-null embryonic stem cells Mol. Biol. Cell 15 2004 4467 4475 (Pubitemid 39299096)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.10 , pp. 4467-4475
    • Matsuoka, Y.1    Kubota, H.2    Adachi, E.3    Nagai, N.4    Marutani, T.5    Hosokawa, N.6    Nagata, K.7
  • 46
  • 47
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • DOI 10.1038/nature06639, PII NATURE06639
    • N. Mizushima, B. Levine, A.M. Cuervo, and D.J. Klionsky Autophagy fights disease through cellular self-digestion Nature 451 2008 1069 1075 (Pubitemid 351317450)
    • (2008) Nature , vol.451 , Issue.7182 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 48
    • 0034683570 scopus 로고    scopus 로고
    • Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis
    • N. Nagai, M. Hosokawa, S. Itohara, E. Adachi, T. Matsushita, N. Hosokawa, and K. Nagata Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis J. Cell Biol. 150 2000 1499 1506
    • (2000) J. Cell Biol. , vol.150 , pp. 1499-1506
    • Nagai, N.1    Hosokawa, M.2    Itohara, S.3    Adachi, E.4    Matsushita, T.5    Hosokawa, N.6    Nagata, K.7
  • 49
    • 33646286416 scopus 로고    scopus 로고
    • Hsp47: A collagen-specific molecular chaperone
    • K. Nagata Hsp47: A collagen-specific molecular chaperone Trends Biochem. Sci. 21 1996 22 26
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 22-26
    • Nagata, K.1
  • 50
    • 0031940622 scopus 로고    scopus 로고
    • Expression and function of heat shock protein 47: A collagen-specific molecular chaperone in the endoplasmic reticulum
    • DOI 10.1016/S0945-053X(98)90011-7
    • K. Nagata Expression and function of heat shock protein 47: A collagen-specific molecular chaperone in the endoplasmic reticulum Matrix Biol. 16 1998 379 386 (Pubitemid 28069864)
    • (1998) Matrix Biology , vol.16 , Issue.7 , pp. 379-386
    • Nagata, K.1
  • 51
    • 0742304951 scopus 로고    scopus 로고
    • HSP47 as a collagen-specific molecular chaperone: Function and expression in normal mouse development
    • DOI 10.1016/j.semcdb.2003.09.020
    • K. Nagata HSP47 as a collagen-specific molecular chaperone: Function and expression in normal mouse development Semin. Cell Dev. Biol. 14 2003 275 282 (Pubitemid 38160952)
    • (2003) Seminars in Cell and Developmental Biology , vol.14 , Issue.5 , pp. 275-282
    • Nagata, K.1
  • 52
    • 0037243908 scopus 로고    scopus 로고
    • Therapeutic strategy for fibrotic diseases by regulating the expression of collagen-specific molecular chaperone HSP47
    • DOI 10.1254/fpj.121.4
    • K. Nagata Therapeutic strategy for fibrotic diseases by regulating the expression of collagen-specific molecular chaperone HSP47 Nippon Yakurigaku Zasshi 121 2003 4 14 (Pubitemid 36119588)
    • (2003) Folia Pharmacologica Japonica , vol.121 , Issue.1 , pp. 4-14
    • Nagata, K.1
  • 53
    • 0022910050 scopus 로고
    • Phosphorylation and transformation sensitivity of a major collagen-binding protein of fibroblasts
    • K. Nagata, and K.M. Yamada Phosphorylation and transformation sensitivity of a major collagen-binding protein of fibroblasts J. Biol. Chem. 261 1986 7531 7536 (Pubitemid 17224762)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.16 , pp. 7531-7536
    • Nagata, K.1    Yamada, K.M.2
  • 54
    • 0022548519 scopus 로고
    • A major collagen-binding protein of chick embryo fibroblasts is a novel heat shock protein
    • K. Nagata, S. Saga, and K.M. Yamada A major collagen-binding protein of chick embryo fibroblasts is a novel heat shock protein J. Cell Biol. 103 1986 223 229 (Pubitemid 16067006)
    • (1986) Journal of Cell Biology , vol.103 , Issue.1 , pp. 223-229
    • Nagata, K.1    Saga, S.2    Yamada, K.M.3
  • 55
    • 27644527952 scopus 로고    scopus 로고
    • Gene expression in human keloids is altered from dermal to chondrocytic and osteogenic lineage
    • DOI 10.1111/j.1365-2443.2005.00902.x
    • M. Naitoh, H. Kubota, M. Ikeda, T. Tanaka, H. Shirane, S. Suzuki, and K. Nagata Gene expression in human keloids is altered from dermal to chondrocytic and osteogenic lineage Genes Cells 10 2005 1081 1091 (Pubitemid 41556076)
    • (2005) Genes to Cells , vol.10 , Issue.11 , pp. 1081-1091
    • Naitoh, M.1    Kubota, H.2    Ikeda, M.3    Tanaka, T.4    Shirane, H.5    Suzuki, S.6    Nagata, K.7
  • 56
    • 0026772964 scopus 로고
    • Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum
    • A. Nakai, M. Satoh, K. Hirayoshi, and K. Nagata Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum J. Cell Biol. 117 1992 903 914
    • (1992) J. Cell Biol. , vol.117 , pp. 903-914
    • Nakai, A.1    Satoh, M.2    Hirayoshi, K.3    Nagata, K.4
  • 57
    • 0027988156 scopus 로고
    • Interactions between collagen-binding stress protein HSP47 and collagen. Analysis of kinetic parameters by surface plasmon resonance biosensor
    • T. Natsume, T. Koide, S. Yokota, K. Hirayoshi, and K. Nagata Interactions between collagen-binding stress protein HSP47 and collagen. Analysis of kinetic parameters by surface plasmon resonance biosensor J. Biol. Chem. 269 1994 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
  • 58
    • 33750143889 scopus 로고    scopus 로고
    • The molecular chaperone HSP47 rapidly senses gravitational changes in myoblasts
    • DOI 10.1111/j.1365-2443.2006.01021.x
    • A. Oguro, T. Sakurai, Y. Fujita, S. Lee, H. Kubota, K. Nagata, and Y. Atomi The molecular chaperone HSP47 rapidly senses gravitational changes in myoblasts Genes Cells 11 2006 1253 1265 (Pubitemid 44594297)
    • (2006) Genes to Cells , vol.11 , Issue.11 , pp. 1253-1265
    • Oguro, A.1    Sakurai, T.2    Fujita, Y.3    Lee, S.4    Kubota, H.5    Nagata, K.6    Atomi, Y.7
  • 60
    • 38549101559 scopus 로고    scopus 로고
    • The role of serpins in the surveillance of the secretory pathway
    • DOI 10.1007/s00018-007-7157-0
    • H. Ragg The role of serpins in the surveillance of the secretory pathway Cell. Mol. Life Sci. 64 2007 2763 2770 (Pubitemid 351152258)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.21 , pp. 2763-2770
    • Ragg, H.1
  • 61
    • 0030798768 scopus 로고    scopus 로고
    • Collagen-binding heat shock protein (HSP) 47 expression in anti- thymocyte serum (ATS)-induced glomerulonephritis
    • DOI 10.1002/(SICI)1096-9896(199709)183:1<24::AID-PATH1106>3.0.CO;2- B
    • M.S. Razzaque, and T. Taguchi Collagen-binding heat shock protein (HSP) 47 expression in anti-thymocyte serum (ATS)-induced glomerulonephritis J. Pathol. 183 1997 24 29 (Pubitemid 27368522)
    • (1997) Journal of Pathology , vol.183 , Issue.1 , pp. 24-29
    • Razzaque, M.S.1    Taguchi, T.2
  • 62
    • 0031731125 scopus 로고    scopus 로고
    • Coexpression of collagens and collagen-binding heat shock protein 47 in human diabetic nephropathy and IgA nephropathy
    • M.S. Razzaque, A. Kumatori, T. Harada, and T. Taguchi Coexpression of collagens and collagen-binding heat shock protein 47 in human diabetic nephropathy and IgA nephropathy Nephron 80 1998 434 443 (Pubitemid 28554691)
    • (1998) Nephron , vol.80 , Issue.4 , pp. 434-443
    • Razzaque, M.S.1    Kumatori, A.2    Harada, T.3    Taguchi, T.4
  • 63
    • 78649346692 scopus 로고    scopus 로고
    • The heat shock response: Life on the verge of death
    • K. Richter, M. Haslbeck, and J. Buchner The heat shock response: Life on the verge of death Mol. Cell 40 2010 253 266
    • (2010) Mol. Cell , vol.40 , pp. 253-266
    • Richter, K.1    Haslbeck, M.2    Buchner, J.3
  • 64
    • 0023373787 scopus 로고
    • PH-dependent function, purification, and intracellular location of a major collagen-binding glycoprotein
    • S. Saga, K. Nagata, W.T. Chen, and K.M. Yamada pH-dependent function, purification, and intracellular location of a major collagen-binding glycoprotein J. Cell Biol. 105 1987 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
  • 66
    • 0029968576 scopus 로고    scopus 로고
    • Intracellular interaction of collagen-specific stress protein HSP47 with newly synthesized procollagen
    • DOI 10.1083/jcb.133.2.469
    • M. Satoh, K. Hirayoshi, S. Yokota, N. Hosokawa, and K. Nagata Intracellular interaction of collagen-specific stress protein HSP47 with newly synthesized procollagen J. Cell Biol. 133 1996 469 483 (Pubitemid 26132541)
    • (1996) Journal of Cell Biology , vol.133 , Issue.2 , pp. 469-483
    • Satoh, M.1    Hirayoshi, K.2    Yokota, S.-I.3    Hosokawa, N.4    Nagata, K.5
  • 68
    • 0031818036 scopus 로고    scopus 로고
    • Antisense oligonucleotides against collagen-binding stress protein HSP47 suppress collagen accumulation in experimental glomerulonephritis
    • M. Sunamoto, K. Kuze, H. Tsuji, N. Ohishi, K. Yagi, K. Nagata, T. Kita, and T. Doi Antisense oligonucleotides against collagen-binding stress protein HSP47 suppress collagen accumulation in experimental glomerulonephritis Lab. Invest. 78 1998 967 972 (Pubitemid 28378211)
    • (1998) Laboratory Investigation , vol.78 , Issue.8 , pp. 967-972
    • Sunamoto, M.1    Kuze, K.2    Tsuji, H.3    Ohishi, N.4    Yagi, K.5    Nagata, K.6    Kita, T.7    Doi, T.8
  • 69
    • 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
    • H. Takechi, K. Hirayoshi, A. Nakai, H. Kudo, S. Saga, and K. Nagata 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 1992 323 329
    • (1992) Eur. J. Biochem. , vol.206 , pp. 323-329
    • Takechi, H.1    Hirayoshi, K.2    Nakai, A.3    Kudo, H.4    Saga, S.5    Nagata, K.6
  • 70
    • 0034657132 scopus 로고    scopus 로고
    • Hsp47: A molecular chaperone that interacts with and stabilizes correctly-folded procollagen
    • M. Tasab, M.R. Batten, and N.J. Bulleid Hsp47: A molecular chaperone that interacts with and stabilizes correctly-folded procollagen EMBO J. 19 2000 2204 2211 (Pubitemid 30259001)
    • (2000) EMBO Journal , vol.19 , Issue.10 , pp. 2204-2211
    • Tasab, M.1    Batten, M.R.2    Bulleid, N.J.3
  • 71
    • 0037144491 scopus 로고    scopus 로고
    • Sequence-specific recognition of collagen triple helices by the collagen-specific molecular chaperone HSP47
    • M. Tasab, L. Jenkinson, and N.J. Bulleid Sequence-specific recognition of collagen triple helices by the collagen-specific molecular chaperone HSP47 J. Biol. Chem. 277 2002 35007 35012
    • (2002) J. Biol. Chem. , vol.277 , pp. 35007-35012
    • Tasab, M.1    Jenkinson, L.2    Bulleid, N.J.3
  • 72
    • 0034254604 scopus 로고    scopus 로고
    • Structure-function studies on Hsp47: pH-dependent inhibition of collagen fibril formation in vitro
    • C.A. Thomson, and V.S. Ananthanarayanan Structurefunction studies on hsp47: pH-dependent inhibition of collagen fibril formation in vitro Biochem. J. 349 Pt 3 2000 877 883 (Pubitemid 30609421)
    • (2000) Biochemical Journal , vol.349 , Issue.3 , pp. 877-883
    • Thomson, C.A.1    Ananthanarayanan, V.S.2
  • 73
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulum-associated degradation
    • S.S. Vembar, and J.L. Brodsky One step at a time: Endoplasmic reticulum-associated degradation Nat. Rev. Mol. Cell Biol. 9 2008 944 957
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 74
    • 33846548110 scopus 로고    scopus 로고
    • ER stress and diseases
    • DOI 10.1111/j.1742-4658.2007.05639.x
    • H. Yoshida ER stress and diseases FEBS J. 274 2007 630 658 (Pubitemid 46150855)
    • (2007) FEBS Journal , vol.274 , Issue.3 , pp. 630-658
    • Yoshida, H.1


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