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Volumn 21, Issue 3, 2011, Pages 168-176

Chaperoning osteogenesis: New protein-folding disease paradigms

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; CALNEXIN; CALRETICULIN; CHAPERONE; COLLAGEN; COLLAGEN TYPE 1; HEAT SHOCK PROTEIN 47; PROCOLLAGEN; PROCOLLAGEN LYSINE 2 OXOGLUTARATE 5 DIOXYGENASE; PROTEIN;

EID: 79952105767     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2010.11.007     Document Type: Review
Times cited : (66)

References (87)
  • 1
    • 70350244550 scopus 로고    scopus 로고
    • Genetic control of bone formation
    • Karsenty G., et al. Genetic control of bone formation. Annu. Rev. Cell Dev. Biol. 2009, 25:629-648.
    • (2009) Annu. Rev. Cell Dev. Biol. , vol.25 , pp. 629-648
    • Karsenty, G.1
  • 3
    • 69249205598 scopus 로고    scopus 로고
    • A paradigm of integrative physiology, the crosstalk between bone and energy metabolisms
    • Confavreux C.B., et al. A paradigm of integrative physiology, the crosstalk between bone and energy metabolisms. Mol. Cell Endocrinol. 2009, 310:21-29.
    • (2009) Mol. Cell Endocrinol. , vol.310 , pp. 21-29
    • Confavreux, C.B.1
  • 5
    • 72449183578 scopus 로고    scopus 로고
    • Null mutations in LEPRE1 and CRTAP cause severe recessive osteogenesis imperfecta
    • Marini J.C., et al. Null mutations in LEPRE1 and CRTAP cause severe recessive osteogenesis imperfecta. Cell Tissue Res. 2010, 339:59-70.
    • (2010) Cell Tissue Res. , vol.339 , pp. 59-70
    • Marini, J.C.1
  • 6
    • 33750207868 scopus 로고    scopus 로고
    • CRTAP is required for prolyl 3-hydroxylation and mutations cause recessive osteogenesis imperfecta
    • Morello R., et al. CRTAP is required for prolyl 3-hydroxylation and mutations cause recessive osteogenesis imperfecta. Cell 2006, 127:291-304.
    • (2006) Cell , vol.127 , pp. 291-304
    • Morello, R.1
  • 7
    • 33845866114 scopus 로고    scopus 로고
    • Deficiency of cartilage-associated protein in recessive lethal osteogenesis imperfecta
    • Barnes A.M., et al. Deficiency of cartilage-associated protein in recessive lethal osteogenesis imperfecta. N. Engl. J. Med. 2006, 355:2757-2764.
    • (2006) N. Engl. J. Med. , vol.355 , pp. 2757-2764
    • Barnes, A.M.1
  • 8
    • 33847321022 scopus 로고    scopus 로고
    • Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta
    • Cabral W.A., et al. Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta. Nat. Genet. 2007, 39:359-365.
    • (2007) Nat. Genet. , vol.39 , pp. 359-365
    • Cabral, W.A.1
  • 9
    • 74249109599 scopus 로고    scopus 로고
    • Severe osteogenesis imperfecta in cyclophilin B-deficient mice
    • Choi J.W., et al. Severe osteogenesis imperfecta in cyclophilin B-deficient mice. PLoS Genet. 2009, 5:e1000750.
    • (2009) PLoS Genet. , vol.5
    • Choi, J.W.1
  • 10
    • 70350506376 scopus 로고    scopus 로고
    • PPIB mutations cause severe osteogenesis imperfecta
    • van Dijk F.S., et al. PPIB mutations cause severe osteogenesis imperfecta. Am. J. Hum. Genet. 2009, 85:521-527.
    • (2009) Am. J. Hum. Genet. , vol.85 , pp. 521-527
    • van Dijk, F.S.1
  • 11
    • 76649130557 scopus 로고    scopus 로고
    • Lack of cyclophilin B in osteogenesis imperfecta with normal collagen folding
    • Barnes A.M., et al. Lack of cyclophilin B in osteogenesis imperfecta with normal collagen folding. N. Engl. J. Med. 2010, 362:521-528.
    • (2010) N. Engl. J. Med. , vol.362 , pp. 521-528
    • Barnes, A.M.1
  • 12
    • 77950381244 scopus 로고    scopus 로고
    • Mutations in the gene encoding the RER protein FKBP65 cause autosomal-recessive osteogenesis imperfecta
    • Alanay Y., et al. Mutations in the gene encoding the RER protein FKBP65 cause autosomal-recessive osteogenesis imperfecta. Am. J. Hum. Genet. 2010, 86:551-559.
    • (2010) Am. J. Hum. Genet. , vol.86 , pp. 551-559
    • Alanay, Y.1
  • 13
    • 68249130696 scopus 로고    scopus 로고
    • A missense mutation in the SERPINH1 gene in Dachshunds with osteogenesis imperfecta
    • Drogemuller C., et al. A missense mutation in the SERPINH1 gene in Dachshunds with osteogenesis imperfecta. PLoS Genet. 2009, 5:e1000579.
    • (2009) PLoS Genet. , vol.5
    • Drogemuller, C.1
  • 14
    • 77949262259 scopus 로고    scopus 로고
    • Homozygosity for a missense mutation in SERPINH1, which encodes the collagen chaperone protein HSP47, results in severe recessive osteogenesis imperfecta
    • Christiansen H.E., et al. Homozygosity for a missense mutation in SERPINH1, which encodes the collagen chaperone protein HSP47, results in severe recessive osteogenesis imperfecta. Am. J. Hum. Genet. 2010, 86:389-398.
    • (2010) Am. J. Hum. Genet. , vol.86 , pp. 389-398
    • Christiansen, H.E.1
  • 15
    • 77955567275 scopus 로고    scopus 로고
    • FKBP10 and Bruck syndrome: phenotypic heterogeneity or call for reclassification?
    • Erratum 571
    • Shaheen R., et al. FKBP10 and Bruck syndrome: phenotypic heterogeneity or call for reclassification?. Am. J. Hum. Genet. 2010, 87:306-307. Erratum 571.
    • (2010) Am. J. Hum. Genet. , vol.87 , pp. 306-307
    • Shaheen, R.1
  • 16
    • 79951842354 scopus 로고    scopus 로고
    • Mutations in FKBP10 cause recessive osteogenesis imperfecta and type 1 bruck syndrome. J. Bone. Miner Res., In press., doi:10.1002/jbmr.250
    • Kelley, B.P. et al. (2010) Mutations in FKBP10 cause recessive osteogenesis imperfecta and type 1 bruck syndrome. J. Bone. Miner Res., In press. doi:10.1002/jbmr.250.
    • (2010)
    • Kelley, B.P.1
  • 17
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl F.U., Hayer-Hartl M. Converging concepts of protein folding in vitro and in vivo. Nat. Struct. Mol. Biol. 2009, 16:574-581.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 18
    • 39149143645 scopus 로고    scopus 로고
    • Chaperone machines in action
    • Saibil H.R. Chaperone machines in action. Curr. Opin. Struct. Biol. 2008, 18:35-42.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 35-42
    • Saibil, H.R.1
  • 19
    • 69849093197 scopus 로고    scopus 로고
    • The endoplasmic reticulum: crossroads for newly synthesized polypeptide chains
    • Cali T., et al. The endoplasmic reticulum: crossroads for newly synthesized polypeptide chains. Prog. Mol. Biol. Transl. Sci. 2008, 83:135-179.
    • (2008) Prog. Mol. Biol. Transl. Sci. , vol.83 , pp. 135-179
    • Cali, T.1
  • 20
    • 33744956370 scopus 로고    scopus 로고
    • Specific recognition of the collagen triple helix by chaperone HSP47. II. The HSP47-binding structural motif in collagens and related proteins
    • Koide T., et al. Specific recognition of the collagen triple helix by chaperone HSP47. II. The HSP47-binding structural motif in collagens and related proteins. J. Biol. Chem. 2006, 281:11177-11185.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11177-11185
    • Koide, T.1
  • 21
    • 33645639418 scopus 로고    scopus 로고
    • Specific recognition of the collagen triple helix by chaperone HSP47: minimal structural requirement and spatial molecular orientation
    • Koide T., et al. Specific recognition of the collagen triple helix by chaperone HSP47: minimal structural requirement and spatial molecular orientation. J. Biol. Chem. 2006, 281:3432-3438.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3432-3438
    • Koide, T.1
  • 22
    • 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
    • Ishida Y., et al. Type I collagen in Hsp47-null cells is aggregated in endoplasmic reticulum and deficient in N-propeptide processing and fibrillogenesis. Mol. Biol. Cell 2006, 17:2346-2355.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2346-2355
    • Ishida, Y.1
  • 23
    • 66349112572 scopus 로고    scopus 로고
    • Autophagic elimination of misfolded procollagen aggregates in the endoplasmic reticulum as a means of cell protection
    • Ishida Y., et al. Autophagic elimination of misfolded procollagen aggregates in the endoplasmic reticulum as a means of cell protection. Mol. Biol. Cell 2009, 20:2744-2754.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2744-2754
    • Ishida, Y.1
  • 24
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C.B. Principles that govern the folding of protein chains. Science 1973, 181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 25
    • 77951977004 scopus 로고    scopus 로고
    • Protein kinetic stability
    • Sanchez-Ruiz J.M. Protein kinetic stability. Biophys. Chem. 2010, 148:1-15.
    • (2010) Biophys. Chem. , vol.148 , pp. 1-15
    • Sanchez-Ruiz, J.M.1
  • 26
    • 34447095724 scopus 로고    scopus 로고
    • Molecular gymnastics: serpin structure, folding and misfolding
    • Whisstock J.C., Bottomley S.P. Molecular gymnastics: serpin structure, folding and misfolding. Curr. Opin. Struct. Biol. 2006, 16:761-768.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 761-768
    • Whisstock, J.C.1    Bottomley, S.P.2
  • 28
    • 60349128086 scopus 로고    scopus 로고
    • Prion protein misfolding and disease
    • Moore R.A., et al. Prion protein misfolding and disease. Curr. Opin. Struct. Biol. 2009, 19:14-22.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 14-22
    • Moore, R.A.1
  • 29
    • 0032558779 scopus 로고    scopus 로고
    • Unfolded conformations of alpha-lytic protease are more stable than its native state
    • Sohl J.L., et al. Unfolded conformations of alpha-lytic protease are more stable than its native state. Nature 1998, 395:817-819.
    • (1998) Nature , vol.395 , pp. 817-819
    • Sohl, J.L.1
  • 30
    • 4644285228 scopus 로고    scopus 로고
    • Protein folding in the cell: reshaping the folding funnel
    • Clark P.L. Protein folding in the cell: reshaping the folding funnel. Trends Biochem. Sci. 2004, 29:527-534.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 527-534
    • Clark, P.L.1
  • 31
    • 42449151176 scopus 로고    scopus 로고
    • Protein folding and misfolding: mechanism and principles
    • Englander S.W., et al. Protein folding and misfolding: mechanism and principles. Q. Rev. Biophys. 2007, 40:287-326.
    • (2007) Q. Rev. Biophys. , vol.40 , pp. 287-326
    • Englander, S.W.1
  • 32
    • 48249134448 scopus 로고    scopus 로고
    • The protein folding problem
    • Dill K.A., et al. The protein folding problem. Annu. Rev. Biophys. 2008, 37:289-316.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 289-316
    • Dill, K.A.1
  • 33
    • 17844373840 scopus 로고    scopus 로고
    • Procollagen trafficking, processing and fibrillogenesis
    • Canty E.G., Kadler K.E. Procollagen trafficking, processing and fibrillogenesis. J. Cell Sci. 2005, 118:1341-1353.
    • (2005) J. Cell Sci. , vol.118 , pp. 1341-1353
    • Canty, E.G.1    Kadler, K.E.2
  • 34
    • 33744928420 scopus 로고    scopus 로고
    • Collagen biosynthesis
    • Springer-Verlag
    • Koide, T. and Nagata, K. (2005) Collagen biosynthesis. In Collagen, pp. 85-114, Springer-Verlag.
    • (2005) In Collagen , pp. 85-114
    • Koide, T.1    Nagata, K.2
  • 35
    • 25444463441 scopus 로고    scopus 로고
    • Structure, stability and folding of the collagen triple helix. In Collagen, Springer-Verlag
    • Engel, J. and Bachinger, H.P. (2005) Structure, stability and folding of the collagen triple helix. In Collagen, pp. 7-33, Springer-Verlag.
    • (2005) , pp. 7-33
    • Engel, J.1    Bachinger, H.P.2
  • 36
    • 0037022329 scopus 로고    scopus 로고
    • Type I collagen is thermally unstable at body temperature
    • Leikina E., et al. Type I collagen is thermally unstable at body temperature. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:1314-1318.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1314-1318
    • Leikina, E.1
  • 37
    • 41749116397 scopus 로고    scopus 로고
    • Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm
    • Makareeva E., Leikin S. Procollagen triple helix assembly: an unconventional chaperone-assisted folding paradigm. PLoS One 2007, 2:e1029.
    • (2007) PLoS One , vol.2
    • Makareeva, E.1    Leikin, S.2
  • 38
    • 41949119604 scopus 로고    scopus 로고
    • Structural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta
    • Makareeva E., et al. Structural heterogeneity of type I collagen triple helix and its role in osteogenesis imperfecta. J. Biol. Chem. 2008, 283:4787-4798.
    • (2008) J. Biol. Chem. , vol.283 , pp. 4787-4798
    • Makareeva, E.1
  • 39
    • 33646593224 scopus 로고    scopus 로고
    • Molecular mechanism of alpha 1(I)-osteogenesis imperfecta/Ehlers-Danlos syndrome: unfolding of an N-anchor domain at the N-terminal end of the type I collagen triple helix
    • Makareeva E., et al. Molecular mechanism of alpha 1(I)-osteogenesis imperfecta/Ehlers-Danlos syndrome: unfolding of an N-anchor domain at the N-terminal end of the type I collagen triple helix. J. Biol. Chem. 2006, 281:6463-6470.
    • (2006) J. Biol. Chem. , vol.281 , pp. 6463-6470
    • Makareeva, E.1
  • 40
    • 50649120554 scopus 로고    scopus 로고
    • Prolyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets
    • Myllyharju J. Prolyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets. Ann. Med. 2008, 40:402-417.
    • (2008) Ann. Med. , vol.40 , pp. 402-417
    • Myllyharju, J.1
  • 42
    • 0742304951 scopus 로고    scopus 로고
    • HSP47 as a collagen-specific molecular chaperone: function and expression in normal mouse development
    • Nagata K. HSP47 as a collagen-specific molecular chaperone: function and expression in normal mouse development. Semin. Cell Dev. Biol. 2003, 14:275-282.
    • (2003) Semin. Cell Dev. Biol. , vol.14 , pp. 275-282
    • Nagata, K.1
  • 43
    • 0034683570 scopus 로고    scopus 로고
    • Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis
    • Nagai N., et al. Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis. J. Cell Biol. 2000, 150:1499-1506.
    • (2000) J. Cell Biol. , vol.150 , pp. 1499-1506
    • Nagai, N.1
  • 44
    • 57649134970 scopus 로고    scopus 로고
    • The rough endoplasmic reticulum-resident FK506-binding protein FKBP65 is a molecular chaperone that interacts with collagens
    • Ishikawa Y., et al. The rough endoplasmic reticulum-resident FK506-binding protein FKBP65 is a molecular chaperone that interacts with collagens. J. Biol. Chem. 2008, 283:31584-31590.
    • (2008) J. Biol. Chem. , vol.283 , pp. 31584-31590
    • Ishikawa, Y.1
  • 45
    • 0028220202 scopus 로고
    • Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta
    • Raghunath M., et al. Delayed triple helix formation of mutant collagen from patients with osteogenesis imperfecta. J. Mol. Biol. 1994, 236:940-949.
    • (1994) J. Mol. Biol. , vol.236 , pp. 940-949
    • Raghunath, M.1
  • 46
    • 71449127603 scopus 로고    scopus 로고
    • Missense mutations that cause Bruck syndrome affect enzymatic activity, folding, and oligomerization of lysyl hydroxylase 2
    • Hyry M., et al. Missense mutations that cause Bruck syndrome affect enzymatic activity, folding, and oligomerization of lysyl hydroxylase 2. J. Biol. Chem. 2009, 284:30917-30924.
    • (2009) J. Biol. Chem. , vol.284 , pp. 30917-30924
    • Hyry, M.1
  • 47
    • 2542497037 scopus 로고    scopus 로고
    • Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes
    • Vranka J.A., et al. Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes. J. Biol. Chem. 2004, 279:23615-23621.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23615-23621
    • Vranka, J.A.1
  • 48
    • 67650522903 scopus 로고    scopus 로고
    • Biochemical characterization of the prolyl 3-hydroxylase 1.cartilage-associated protein.cyclophilin B complex
    • Ishikawa Y., et al. Biochemical characterization of the prolyl 3-hydroxylase 1.cartilage-associated protein.cyclophilin B complex. J. Biol. Chem. 2009, 284:17641-17647.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17641-17647
    • Ishikawa, Y.1
  • 49
    • 77949442552 scopus 로고    scopus 로고
    • Prolyl 3-hydroxylase 1 and CRTAP are mutually stabilizing in the endoplasmic reticulum collagen prolyl 3-hydroxylation complex
    • Chang W., et al. Prolyl 3-hydroxylase 1 and CRTAP are mutually stabilizing in the endoplasmic reticulum collagen prolyl 3-hydroxylation complex. Hum. Mol. Genet. 2010, 19:223-234.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 223-234
    • Chang, W.1
  • 50
    • 55949095578 scopus 로고    scopus 로고
    • Effect of the -Gly-3(S)-hydroxyprolyl-4(R)-hydroxyprolyl- tripeptide unit on the stability of collagen model peptides
    • Mizuno K., et al. Effect of the -Gly-3(S)-hydroxyprolyl-4(R)-hydroxyprolyl- tripeptide unit on the stability of collagen model peptides. FEBS J. 2008, 275:5830-5840.
    • (2008) FEBS J. , vol.275 , pp. 5830-5840
    • Mizuno, K.1
  • 51
    • 77449136859 scopus 로고    scopus 로고
    • Location of 3-hydroxyproline residues in collagen types I, II, III, and V/XI implies a role in fibril supramolecular assembly
    • Weis M.A., et al. Location of 3-hydroxyproline residues in collagen types I, II, III, and V/XI implies a role in fibril supramolecular assembly. J. Biol. Chem. 2010, 285:2580-2590.
    • (2010) J. Biol. Chem. , vol.285 , pp. 2580-2590
    • Weis, M.A.1
  • 52
    • 0029132706 scopus 로고
    • Hsp47 and cyclophilin B traverse the endoplasmic reticulum with procollagen into pre-Golgi intermediate vesicles. A role for Hsp47 and cyclophilin B in the export of procollagen from the endoplasmic reticulum
    • Smith T., et al. Hsp47 and cyclophilin B traverse the endoplasmic reticulum with procollagen into pre-Golgi intermediate vesicles. A role for Hsp47 and cyclophilin B in the export of procollagen from the endoplasmic reticulum. J. Biol. Chem. 1995, 270:18323-18328.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18323-18328
    • Smith, T.1
  • 53
    • 0025968746 scopus 로고
    • Cyclosporin A slows collagen triple-helix formation in vivo: indirect evidence for a physiologic role of peptidyl-prolyl cis-trans-isomerase
    • Steinmann B., et al. Cyclosporin A slows collagen triple-helix formation in vivo: indirect evidence for a physiologic role of peptidyl-prolyl cis-trans-isomerase. J. Biol. Chem. 1991, 266:1299-1303.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1299-1303
    • Steinmann, B.1
  • 54
    • 84855635498 scopus 로고    scopus 로고
    • Mutations in PPIB, which encodes a prolyl cis-trans isomerase (cyclophilin B), in recessive forms of osteogenesis imperfecta (OI). In Program and Abstracts of the 59th Annual Meeting of the American Society of Human Genetics, Honolulu, October 20-24
    • Schwarze, U. et al. (2009) Mutations in PPIB, which encodes a prolyl cis-trans isomerase (cyclophilin B), in recessive forms of osteogenesis imperfecta (OI). In Program and Abstracts of the 59th Annual Meeting of the American Society of Human Genetics, Honolulu, October 20-24 http://www.ashg.org/2009meeting/pdf/platforms_4up.pdf.
    • (2009)
    • Schwarze, U.1
  • 55
    • 77952632630 scopus 로고    scopus 로고
    • Osteogenesis imperfecta, normal collagen folding, and lack of cyclophilin B
    • Barnes A.M., et al. Osteogenesis imperfecta, normal collagen folding, and lack of cyclophilin B. N. Engl. J. Med. 2010, 362:1941-1942.
    • (2010) N. Engl. J. Med. , vol.362 , pp. 1941-1942
    • Barnes, A.M.1
  • 56
    • 40149105885 scopus 로고    scopus 로고
    • ER stress-mediated apoptosis in a new mouse model of osteogenesis imperfecta
    • Lisse T.S., et al. ER stress-mediated apoptosis in a new mouse model of osteogenesis imperfecta. PLoS Genet. 2008, 4:e7.
    • (2008) PLoS Genet. , vol.4
    • Lisse, T.S.1
  • 57
    • 36549047084 scopus 로고    scopus 로고
    • Selective retention and degradation of molecules with a single mutant alpha1(I) chain in the Brtl IV mouse model of OI
    • Forlino A., et al. Selective retention and degradation of molecules with a single mutant alpha1(I) chain in the Brtl IV mouse model of OI. Matrix Biol. 2007, 26:604-614.
    • (2007) Matrix Biol. , vol.26 , pp. 604-614
    • Forlino, A.1
  • 58
    • 36248949141 scopus 로고    scopus 로고
    • The endoplasmic reticulum and the unfolded protein response
    • Malhotra J.D., Kaufman R.J. The endoplasmic reticulum and the unfolded protein response. Semin. Cell Dev. Biol. 2007, 18:716-731.
    • (2007) Semin. Cell Dev. Biol. , vol.18 , pp. 716-731
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 59
    • 77953153048 scopus 로고    scopus 로고
    • Regulation of basal cellular physiology by the homeostatic unfolded protein response
    • Rutkowski D.T., Hegde R.S. Regulation of basal cellular physiology by the homeostatic unfolded protein response. J. Cell Biol. 2010, 189:783-794.
    • (2010) J. Cell Biol. , vol.189 , pp. 783-794
    • Rutkowski, D.T.1    Hegde, R.S.2
  • 60
    • 0027182875 scopus 로고
    • BiP binds type I procollagen pro alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta
    • Chessler S.D., Byers P.H. BiP binds type I procollagen pro alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta. J. Biol. Chem. 1993, 268:18226-18233.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18226-18233
    • Chessler, S.D.1    Byers, P.H.2
  • 61
    • 34250337398 scopus 로고    scopus 로고
    • Differential expression of both extracellular and intracellular proteins is involved in the lethal or nonlethal phenotypic variation of BrtlIV, a murine model for osteogenesis imperfecta
    • Forlino A., et al. Differential expression of both extracellular and intracellular proteins is involved in the lethal or nonlethal phenotypic variation of BrtlIV, a murine model for osteogenesis imperfecta. Proteomics 2007, 7:1877-1891.
    • (2007) Proteomics , vol.7 , pp. 1877-1891
    • Forlino, A.1
  • 62
    • 67649246879 scopus 로고    scopus 로고
    • 1-Antitrypsin deficiency, chronic obstructive pulmonary disease and the serpinopathies
    • 1-Antitrypsin deficiency, chronic obstructive pulmonary disease and the serpinopathies. Clin. Sci. (Lond.) 2009, 116:837-850.
    • (2009) Clin. Sci. (Lond.) , vol.116 , pp. 837-850
    • Ekeowa, U.I.1
  • 63
    • 2442451197 scopus 로고    scopus 로고
    • Intracellular trafficking and degradation of unassociated proalpha2 chains of collagen type I
    • Gotkin M.G., et al. Intracellular trafficking and degradation of unassociated proalpha2 chains of collagen type I. Exp. Cell Res. 2004, 296:307-316.
    • (2004) Exp. Cell Res. , vol.296 , pp. 307-316
    • Gotkin, M.G.1
  • 64
    • 34247121035 scopus 로고    scopus 로고
    • Stress to endoplasmic reticulum of mouse osteoblasts induces apoptosis and transcriptional activation for bone remodeling
    • Hamamura K., Yokota H. Stress to endoplasmic reticulum of mouse osteoblasts induces apoptosis and transcriptional activation for bone remodeling. FEBS Lett. 2007, 581:1769-1774.
    • (2007) FEBS Lett. , vol.581 , pp. 1769-1774
    • Hamamura, K.1    Yokota, H.2
  • 65
    • 70349652275 scopus 로고    scopus 로고
    • Signalling mediated by the endoplasmic reticulum stress transducer OASIS is involved in bone formation
    • Murakami T., et al. Signalling mediated by the endoplasmic reticulum stress transducer OASIS is involved in bone formation. Nat. Cell Biol. 2009, 11:1205-1211.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1205-1211
    • Murakami, T.1
  • 66
    • 60349120776 scopus 로고    scopus 로고
    • Genetic diseases of connective tissues: cellular and extracellular effects of ECM mutations
    • Bateman J.F., et al. Genetic diseases of connective tissues: cellular and extracellular effects of ECM mutations. Nat. Rev. Genet. 2009, 10:173-183.
    • (2009) Nat. Rev. Genet. , vol.10 , pp. 173-183
    • Bateman, J.F.1
  • 67
    • 33645156429 scopus 로고    scopus 로고
    • From acute ER stress to physiological roles of the Unfolded Protein Response
    • Wu J., Kaufman R.J. From acute ER stress to physiological roles of the Unfolded Protein Response. Cell Death Differ. 2006, 13:374-384.
    • (2006) Cell Death Differ. , vol.13 , pp. 374-384
    • Wu, J.1    Kaufman, R.J.2
  • 68
    • 1942501149 scopus 로고    scopus 로고
    • Osteogenesis imperfecta
    • Rauch F., Glorieux F.H. Osteogenesis imperfecta. Lancet 2004, 363:1377-1385.
    • (2004) Lancet , vol.363 , pp. 1377-1385
    • Rauch, F.1    Glorieux, F.H.2
  • 69
    • 56749095463 scopus 로고    scopus 로고
    • Cellular mechanism of decreased bone in Brtl mouse model of OI: imbalance of decreased osteoblast function and increased osteoclasts and their precursors
    • Uveges T.E., et al. Cellular mechanism of decreased bone in Brtl mouse model of OI: imbalance of decreased osteoblast function and increased osteoclasts and their precursors. J. Bone Miner Res. 2008, 23:1983-1994.
    • (2008) J. Bone Miner Res. , vol.23 , pp. 1983-1994
    • Uveges, T.E.1
  • 70
    • 0036091476 scopus 로고    scopus 로고
    • The PERK eukaryotic initiation factor 2α kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas
    • Zhang P., et al. The PERK eukaryotic initiation factor 2α kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas. Mol. Cell Biol. 2002, 22:3864-3874.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 3864-3874
    • Zhang, P.1
  • 71
    • 77951844173 scopus 로고    scopus 로고
    • Osteopotentia regulates osteoblast maturation, bone formation, and skeletal integrity in mice
    • Sohaskey M.L., et al. Osteopotentia regulates osteoblast maturation, bone formation, and skeletal integrity in mice. J. Cell Biol. 2010, 189:511-525.
    • (2010) J. Cell Biol. , vol.189 , pp. 511-525
    • Sohaskey, M.L.1
  • 72
    • 77955084141 scopus 로고    scopus 로고
    • Identification of a frameshift mutation in Osterix in a patient with recessive osteogenesis imperfecta
    • Lapunzina P., et al. Identification of a frameshift mutation in Osterix in a patient with recessive osteogenesis imperfecta. Am. J. Hum. Genet. 2010, 87:110-114.
    • (2010) Am. J. Hum. Genet. , vol.87 , pp. 110-114
    • Lapunzina, P.1
  • 73
    • 56349162283 scopus 로고    scopus 로고
    • Lrp5 controls bone formation by inhibiting serotonin synthesis in the duodenum
    • Yadav V.K., et al. Lrp5 controls bone formation by inhibiting serotonin synthesis in the duodenum. Cell 2008, 135:825-837.
    • (2008) Cell , vol.135 , pp. 825-837
    • Yadav, V.K.1
  • 74
    • 79952107856 scopus 로고    scopus 로고
    • SOST and DKK: antagonists of LRP family signaling as targets for treating bone disease
    • article ID 460120 (9 pages)
    • Mason J.J., Williams B.O. SOST and DKK: antagonists of LRP family signaling as targets for treating bone disease. J. Osteoporos. 2010, article ID 460120 (9 pages).
    • (2010) J. Osteoporos.
    • Mason, J.J.1    Williams, B.O.2
  • 75
    • 33847227672 scopus 로고    scopus 로고
    • Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans
    • Marini J.C., et al. Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans. Hum. Mutat. 2007, 28:209-221.
    • (2007) Hum. Mutat. , vol.28 , pp. 209-221
    • Marini, J.C.1
  • 76
    • 21444439013 scopus 로고    scopus 로고
    • Mutations near amino end of alpha1(I) collagen cause combined osteogenesis imperfecta/Ehlers-Danlos syndrome by interference with N-propeptide processing
    • Cabral W.A., et al. Mutations near amino end of alpha1(I) collagen cause combined osteogenesis imperfecta/Ehlers-Danlos syndrome by interference with N-propeptide processing. J. Biol. Chem. 2005, 280:19259-19269.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19259-19269
    • Cabral, W.A.1
  • 77
    • 73349112261 scopus 로고    scopus 로고
    • Targeted induction of endoplasmic reticulum stress induces cartilage pathology
    • Rajpar M.H., et al. Targeted induction of endoplasmic reticulum stress induces cartilage pathology. PLoS Genet. 2009, 5:e1000691.
    • (2009) PLoS Genet. , vol.5
    • Rajpar, M.H.1
  • 78
    • 0010098815 scopus 로고    scopus 로고
    • Abnormal compartmentalization of cartilage matrix components in mice lacking collagen X: implications for function
    • Kwan K.M., et al. Abnormal compartmentalization of cartilage matrix components in mice lacking collagen X: implications for function. J. Cell Biol. 1997, 136:459-471.
    • (1997) J. Cell Biol. , vol.136 , pp. 459-471
    • Kwan, K.M.1
  • 79
    • 72449160579 scopus 로고    scopus 로고
    • The unfolded protein response and its relevance to connective tissue diseases
    • Boot-Handford R.P., Briggs M.D. The unfolded protein response and its relevance to connective tissue diseases. Cell Tissue Res. 2010, 339:197-211.
    • (2010) Cell Tissue Res. , vol.339 , pp. 197-211
    • Boot-Handford, R.P.1    Briggs, M.D.2
  • 80
    • 77954354827 scopus 로고    scopus 로고
    • In vivo cellular adaptation to ER stress: survival strategies with double-edged consequences
    • Tsang K.Y., et al. In vivo cellular adaptation to ER stress: survival strategies with double-edged consequences. J. Cell Sci. 2010, 123:2145-2154.
    • (2010) J. Cell Sci. , vol.123 , pp. 2145-2154
    • Tsang, K.Y.1
  • 81
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • Hotamisligil G.S. Endoplasmic reticulum stress and the inflammatory basis of metabolic disease. Cell 2010, 140:900-917.
    • (2010) Cell , vol.140 , pp. 900-917
    • Hotamisligil, G.S.1
  • 82
    • 33846548110 scopus 로고    scopus 로고
    • ER stress and diseases
    • Yoshida H. ER stress and diseases. FEBS J. 2007, 274:630-658.
    • (2007) FEBS J. , vol.274 , pp. 630-658
    • Yoshida, H.1
  • 83
    • 0033551199 scopus 로고    scopus 로고
    • α-Lytic protease precursor: characterization of a structured folding intermediate
    • Anderson D.E., et al. α-Lytic protease precursor: characterization of a structured folding intermediate. Biochemistry 1999, 38:4728-4735.
    • (1999) Biochemistry , vol.38 , pp. 4728-4735
    • Anderson, D.E.1
  • 84
    • 57049117303 scopus 로고    scopus 로고
    • The intramolecular chaperone-mediated protein folding
    • Chen Y.J., Inouye M. The intramolecular chaperone-mediated protein folding. Curr. Opin. Struct. Biol. 2008, 18:765-770.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 765-770
    • Chen, Y.J.1    Inouye, M.2
  • 85
    • 77954597127 scopus 로고    scopus 로고
    • An autophagy-enhancing drug promotes degradation of mutant alpha1-antitrypsin Z and reduces hepatic fibrosis
    • Hidvegi T., et al. An autophagy-enhancing drug promotes degradation of mutant alpha1-antitrypsin Z and reduces hepatic fibrosis. Science 2010, 329:229-232.
    • (2010) Science , vol.329 , pp. 229-232
    • Hidvegi, T.1
  • 86
    • 59349111783 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and autophagy as targets for cancer therapy
    • Schonthal A.H. Endoplasmic reticulum stress and autophagy as targets for cancer therapy. Cancer Lett. 2009, 275:163-169.
    • (2009) Cancer Lett. , vol.275 , pp. 163-169
    • Schonthal, A.H.1
  • 87
    • 0023657312 scopus 로고
    • The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen
    • Bachinger H.P. The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagen. J. Biol. Chem. 1987, 262:17144-17148.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17144-17148
    • Bachinger, H.P.1


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