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Volumn 9, Issue 10, 2014, Pages

Role of LARP6 and nonmuscle myosin in partitioning of collagen mRNAs to the ER membrane

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN ALPHA1; COLLAGEN ALPHA2; COLLAGEN TYPE 1; MESSENGER RNA; MYOSIN; NONMUSCLE MYOSIN; PROTEIN LARP6; RNA BINDING PROTEIN; UNCLASSIFIED DRUG; AUTOANTIGEN; RIBONUCLEOPROTEIN; SS-B ANTIGEN;

EID: 84907484125     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0108870     Document Type: Article
Times cited : (19)

References (90)
  • 1
    • 0347418197 scopus 로고    scopus 로고
    • Collagens, modifying enzymes and their mutations in humans, flies and worms
    • Myllyharju J, Kivirikko K.I. (2004) Collagens, modifying enzymes and their mutations in humans, flies and worms. Trends Genet 20: 33-43.
    • (2004) Trends Genet , vol.20 , pp. 33-43
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 2
    • 0031940007 scopus 로고    scopus 로고
    • Collagen biosynthesis: A mini-review cluster
    • Kivirikko KI (1998) Collagen biosynthesis: a mini-review cluster. Matrix Biol 16: 355-356.
    • (1998) Matrix Biol , vol.16 , pp. 355-356
    • Kivirikko, K.I.1
  • 3
    • 50849145156 scopus 로고    scopus 로고
    • Collagen fibrillogenesis: Fibronectin, integrins, and minor collagens as organizers and nucleators
    • Kadler KE, Hill A, Canty-Laird EG (2008) Collagen fibrillogenesis: fibronectin, integrins, and minor collagens as organizers and nucleators. Curr Opin Cell Biol 20: 495-501.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 495-501
    • Kadler, K.E.1    Hill, A.2    Canty-Laird, E.G.3
  • 4
    • 84889661563 scopus 로고    scopus 로고
    • Nonmuscle myosin II powered transport of newly formed collagen fibrils at the plasma membrane
    • Kalson NS, Starborg T, Lu Y., Mironov A, Humphries SM, et al (2013) Nonmuscle myosin II powered transport of newly formed collagen fibrils at the plasma membrane. Proc Natl Acad Sci U S A 110: E4743-4752.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. E4743-4752
    • Kalson, N.S.1    Starborg, T.2    Lu, Y.3    Mironov, A.4    Humphries, S.M.5
  • 5
    • 0031957558 scopus 로고    scopus 로고
    • Measurement of dermal collagen synthesis rate in vivo in humans
    • el-Harake W.A., Furman MA, Cook B, Nair K.S., Kukowski J., et al. (1998) Measurement of dermal collagen synthesis rate in vivo in humans. Am J Physiol 274: E586-591.
    • (1998) Am J Physiol , vol.274 , pp. E586-591
    • El-Harake, W.A.1    Furman, M.A.2    Cook, B.3    Nair, K.S.4    Kukowski, J.5
  • 6
    • 42949165563 scopus 로고    scopus 로고
    • Dietary protein intake affects albumin fractional synthesis rate in younger and older adults equally
    • Thalacker-Mercer A.E., Campbell W.W. (2008) Dietary protein intake affects albumin fractional synthesis rate in younger and older adults equally. Nutr Rev 66: 91-95.
    • (2008) Nutr Rev , vol.66 , pp. 91-95
    • Thalacker-Mercer, A.E.1    Campbell, W.W.2
  • 7
    • 54749096378 scopus 로고    scopus 로고
    • Fractional protein synthesis rates are similar when measured by intraperitoneal or intravenous flooding doses of L-[ring-2H5]phenylalanine in combination with a rapid regimen of sampling in piglets
    • Bregendahl K, Yang X, Liu L., Yen JT, Rideout TC, et al. (2008) Fractional protein synthesis rates are similar when measured by intraperitoneal or intravenous flooding doses of L-[ring-2H5]phenylalanine in combination with a rapid regimen of sampling in piglets. J Nutr 138: 1976-1981.
    • (2008) J Nutr , vol.138 , pp. 1976-1981
    • Bregendahl, K.1    Yang, X.2    Liu, L.3    Yen, J.T.4    Rideout, T.C.5
  • 8
    • 0026668322 scopus 로고
    • Protein turnover, synthesis and secretion of albumin in hepatocytes isolated from rats bearing walker 256 carcinoma
    • Villa P, Arioli P, Guaitani A. (1992) Protein turnover, synthesis and secretion of albumin in hepatocytes isolated from rats bearing Walker 256 carcinoma. In Vitro Cell Dev Biol 28A: 157-160.
    • (1992) Vitro Cell Dev Biol , vol.28 A , pp. 157-160
    • Villa, P.1    Arioli, P.2    Guaitani, A.3
  • 10
    • 0030835428 scopus 로고    scopus 로고
    • Posttranscriptional regulation of collagen alpha1(I) mRNA in hepatic stellate cells
    • Stefanovic B, Hellerbrand C, Holcik M., Briendl M, Aliebhaber S, et al (1997) Posttranscriptional regulation of collagen alpha1(I) mRNA in hepatic stellate cells. Mol Cell Biol 17: 5201-5209.
    • (1997) Mol Cell Biol , vol.17 , pp. 5201-5209
    • Stefanovic, B.1    Hellerbrand, C.2    Holcik, M.3    Briendl, M.4    Aliebhaber, S.5
  • 11
    • 78149298226 scopus 로고    scopus 로고
    • Mechanisms of tubulointerstitial fibrosis
    • Zeisberg M, Neilson E.G. (2010) Mechanisms of tubulointerstitial fibrosis. J Am Soc Nephrol 21: 1819-1834.
    • (2010) J Am Soc Nephrol , vol.21 , pp. 1819-1834
    • Zeisberg, M.1    Neilson, E.G.2
  • 13
    • 60649102339 scopus 로고    scopus 로고
    • Pulmonary fibrosis: Pathogenesis, etiology and regulation
    • Wilson MS, Wynn T.A. (2009) Pulmonary fibrosis: pathogenesis, etiology and regulation. Mucosal Immunol 2: 103-121.
    • (2009) Mucosal Immunol , vol.2 , pp. 103-121
    • Wilson, M.S.1    Wynn, T.A.2
  • 14
    • 73149093404 scopus 로고    scopus 로고
    • Binding of LARP6 to the conserved 5' stem-loop regulates translation of mRNAs encoding type I collagen
    • Cai L, Fritz D, Stefanovic L., Stefanovic B. (2010) Binding of LARP6 to the conserved 5' stem-loop regulates translation of mRNAs encoding type I collagen. J Mol Biol 395: 309-326.
    • (2010) J Mol Biol , vol.395 , pp. 309-326
    • Cai, L.1    Fritz, D.2    Stefanovic, L.3    Stefanovic, B.4
  • 16
    • 84886788919 scopus 로고    scopus 로고
    • Serine-threonine kinase receptor-associated protein (STRAP) regulates translation of type I collagen mRNAs
    • Vukmirovic M, Manojlovic Z, Stefanovic B. (2013) Serine-threonine kinase receptor-associated protein (STRAP) regulates translation of type I collagen mRNAs. Mol Cell Biol 33: 3893-3906.
    • (2013) Mol Cell Biol , vol.33 , pp. 3893-3906
    • Vukmirovic, M.1    Manojlovic, Z.2    Stefanovic, B.3
  • 17
    • 84878656886 scopus 로고    scopus 로고
    • Tacrolimus (FK506) prevents early stages of ethanol induced hepatic fibrosis by targeting LARP6 dependent mechanism of collagen synthesis
    • Manojlovic Z, Blackmon J, Stefanovic B. (2013) Tacrolimus (FK506) prevents early stages of ethanol induced hepatic fibrosis by targeting LARP6 dependent mechanism of collagen synthesis. PLoS One 8: e65897.
    • (2013) PLoS One , vol.8 , pp. e65897
    • Manojlovic, Z.1    Blackmon, J.2    Stefanovic, B.3
  • 18
    • 84855985830 scopus 로고    scopus 로고
    • A novel role of RNA helicase A in regulation of translation of type I collagen mRNAs
    • Manojlovic Z, Stefanovic B. (2012) A novel role of RNA helicase A in regulation of translation of type I collagen mRNAs. RNA 18: 321-334.
    • (2012) RNA , vol.18 , pp. 321-334
    • Manojlovic, Z.1    Stefanovic, B.2
  • 19
    • 80052601574 scopus 로고    scopus 로고
    • A novel role of vimentin filaments: Binding and stabilization of collagen mRNAs
    • Challa AA, Stefanovic B. (2011) A novel role of vimentin filaments: binding and stabilization of collagen mRNAs. Mol Cell Biol 31: 3773-3789.
    • (2011) Mol Cell Biol , vol.31 , pp. 3773-3789
    • Challa, A.A.1    Stefanovic, B.2
  • 22
    • 0033005168 scopus 로고    scopus 로고
    • Molecular mechanisms of nonmuscle myosin-II regulation
    • Bresnick AR (1999) Molecular mechanisms of nonmuscle myosin-II regulation. Curr Opin Cell Biol 11: 26-33.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 26-33
    • Bresnick, A.R.1
  • 23
    • 0031720373 scopus 로고    scopus 로고
    • Differential expression and functions of cortical myosin IIA and IIB isotypes during meiotic maturation, fertilization, and mitosis in mouse oocytes and embryos
    • Simerly C, Nowak G, de Lanerolle P, Schatten G. (1998) Differential expression and functions of cortical myosin IIA and IIB isotypes during meiotic maturation, fertilization, and mitosis in mouse oocytes and embryos. Mol Biol Cell 9: 2509-2525.
    • (1998) Mol Biol Cell , vol.9 , pp. 2509-2525
    • Simerly, C.1    Nowak, G.2    De Lanerolle, P.3    Schatten, G.4
  • 24
    • 0030970331 scopus 로고    scopus 로고
    • Characterization of isoform diversity among smooth muscle and nonmuscle myosin heavy chains
    • Kelley CA (1997) Characterization of isoform diversity among smooth muscle and nonmuscle myosin heavy chains. Comp Biochem Physiol B Biochem Mol Biol 117: 39-49.
    • (1997) Comp Biochem Physiol B Biochem Mol Biol , vol.117 , pp. 39-49
    • Kelley, C.A.1
  • 25
    • 84860296418 scopus 로고    scopus 로고
    • In vivo studies on nonmuscle myosin II expression and function in heart development
    • Ma X, Adelstein R.S. (2012) In vivo studies on nonmuscle myosin II expression and function in heart development. Front Biosci (Landmark Ed) 17: 545-555.
    • (2012) Front Biosci (Landmark Ed) , vol.17 , pp. 545-555
    • Ma, X.1    Adelstein, R.S.2
  • 26
    • 43749119360 scopus 로고    scopus 로고
    • Regulation of the smooth muscle contractile phenotype by nonmuscle myosin
    • Ogut O, Yuen SL, Brozovich F.V. (2007) Regulation of the smooth muscle contractile phenotype by nonmuscle myosin. J Muscle Res Cell Motil 28: 409-414.
    • (2007) J Muscle Res Cell Motil , vol.28 , pp. 409-414
    • Ogut, O.1    Yuen, S.L.2    Brozovich, F.V.3
  • 30
    • 84868532127 scopus 로고    scopus 로고
    • Nonmuscle myosin II regulates migration but not contraction in rat hepatic stellate cells
    • Moore CC, Lakner AM, Yengo C.M., Schrum L.W. (2011) Nonmuscle myosin II regulates migration but not contraction in rat hepatic stellate cells. World J He-patol 3: 184-197.
    • (2011) World J He-patol , vol.3 , pp. 184-197
    • Moore, C.C.1    Lakner, A.M.2    Yengo, C.M.3    Schrum, L.W.4
  • 31
    • 78649630469 scopus 로고    scopus 로고
    • Distinct roles for non-muscle myosin II isoforms in mouse hepatic stellate cells
    • Liu Z, Van Rossen E, Timmermans JP, Geerts A, van Grunsven LA, et al. (2011) Distinct roles for non-muscle myosin II isoforms in mouse hepatic stellate cells. J Hepatol 54: 132-141.
    • (2011) J Hepatol , vol.54 , pp. 132-141
    • Liu, Z.1    Van Rossen, E.2    Timmermans, J.P.3    Geerts, A.4    Van Grunsven, L.A.5
  • 32
    • 0035197549 scopus 로고    scopus 로고
    • Wound-induced migration of rat hepatic stellate cells is modulated by endothelin-1 through rho-kinase-mediated alterations in the acto-myosin cytoskeleton
    • Tangkijvanich P, Tam SP, Yee HF Jr (2001) Wound-induced migration of rat hepatic stellate cells is modulated by endothelin-1 through rho-kinase-mediated alterations in the acto-myosin cytoskeleton. Hepatology 33: 74-80.
    • (2001) Hepatology , vol.33 , pp. 74-80
    • Tangkijvanich, P.1    Tam, S.P.2    Yee, H.F.3
  • 33
    • 77955328816 scopus 로고    scopus 로고
    • Nonmuscle myosin-dependent synthesis of type I collagen
    • Cai L, Fritz D, Stefanovic L., Stefanovic B. (2010) Nonmuscle myosin-dependent synthesis of type I collagen. J Mol Biol 401: 564-578.
    • (2010) J Mol Biol , vol.401 , pp. 564-578
    • Cai, L.1    Fritz, D.2    Stefanovic, L.3    Stefanovic, B.4
  • 34
    • 0035839613 scopus 로고    scopus 로고
    • Myosin ii light chain phosphorylation regulates membrane localization and apoptotic signaling of tumor necrosis factor receptor-1
    • Jin Y, Atkinson SJ, Marrs J.A., Gallagher P.J. (2001) Myosin ii light chain phosphorylation regulates membrane localization and apoptotic signaling of tumor necrosis factor receptor-1. J Biol Chem 276: 30342-30349.
    • (2001) J Biol Chem , vol.276 , pp. 30342-30349
    • Jin, Y.1    Atkinson, S.J.2    Marrs, J.A.3    Gallagher, P.J.4
  • 36
    • 0038054702 scopus 로고    scopus 로고
    • Variation in the extent of microsatellite instability in human cell lines with defects in different mismatch repair genes
    • Yamada NA, Castro A, Farber R.A. (2003) Variation in the extent of microsatellite instability in human cell lines with defects in different mismatch repair genes. Mutagenesis 18: 277-282.
    • (2003) Mutagenesis , vol.18 , pp. 277-282
    • Yamada, N.A.1    Castro, A.2    Farber, R.A.3
  • 37
    • 33746511526 scopus 로고    scopus 로고
    • Gene expression profile of quiescent and activated rat hepatic stellate cells implicates wnt signaling pathway in activation
    • Jiang F, Parsons CJ, Stefanovic B. (2006) Gene expression profile of quiescent and activated rat hepatic stellate cells implicates Wnt signaling pathway in activation. J Hepatol 45: 401-409.
    • (2006) J Hepatol , vol.45 , pp. 401-409
    • Jiang, F.1    Parsons, C.J.2    Stefanovic, B.3
  • 38
    • 24144468641 scopus 로고    scopus 로고
    • Direct hepatotoxic effect of KC chemokine in the liver without infiltration of neutrophils
    • Stefanovic L, Brenner DA, Stefanovic B. (2005) Direct hepatotoxic effect of KC chemokine in the liver without infiltration of neutrophils. Exp Biol Med (Maywood) 230: 573-586.
    • (2005) Exp Biol Med (Maywood) , vol.230 , pp. 573-586
    • Stefanovic, L.1    Brenner, D.A.2    Stefanovic, B.3
  • 39
    • 0344688414 scopus 로고    scopus 로고
    • A rad53 kinase-dependent surveillance mechanism that regulates histone protein levels in S. Cerevisiae
    • Gunjan A, Verreault A. (2003) A Rad53 kinase-dependent surveillance mechanism that regulates histone protein levels in S. cerevisiae. Cell 115: 537-549.
    • (2003) Cell , vol.115 , pp. 537-549
    • Gunjan, A.1    Verreault, A.2
  • 40
    • 42949117285 scopus 로고    scopus 로고
    • Analysis of mRNA partitioning between the cytosol and endoplasmic reticulum compartments of Mammalian cells
    • Stephens SB, Dodd RD, Lerner R.S., Pyhtila BM, Nicchitta C.V. (2008) Analysis of mRNA partitioning between the cytosol and endoplasmic reticulum compartments of mammalian cells. Methods Mol Biol 419: 197-214.
    • (2008) Methods Mol Biol , vol.419 , pp. 197-214
    • Stephens, S.B.1    Dodd, R.D.2    Lerner, R.S.3    Pyhtila, B.M.4    Nicchitta, C.V.5
  • 41
    • 84934434313 scopus 로고    scopus 로고
    • Fractionation of subcellular membrane vesicles of epithelial and nonepithelial cells by OptiPrep density gradient ultracentrifugation
    • Li X, Donowitz M. (2008) Fractionation of subcellular membrane vesicles of epithelial and nonepithelial cells by OptiPrep density gradient ultracentrifugation. Methods Mol Biol 440: 97-110.
    • (2008) Methods Mol Biol , vol.440 , pp. 97-110
    • Li, X.1    Donowitz, M.2
  • 43
    • 84878941023 scopus 로고    scopus 로고
    • Signal recognition particle: An essential protein-targeting machine
    • Akopian D, Shen K, Zhang X., Shan S.O. (2013) Signal recognition particle: an essential protein-targeting machine. Annu Rev Biochem 82: 693-721.
    • (2013) Annu Rev Biochem , vol.82 , pp. 693-721
    • Akopian, D.1    Shen, K.2    Zhang, X.3    Shan, S.O.4
  • 44
    • 32044449159 scopus 로고    scopus 로고
    • Pathways for compartmentalizing protein synthesis in eukaryotic cells: The template-partitioning model
    • Nicchitta CV, Lerner RS, Stephens S.B., Dodd RD, Pyhtila B. (2005) Pathways for compartmentalizing protein synthesis in eukaryotic cells: the template-partitioning model. Biochem Cell Biol 83: 687-695.
    • (2005) Biochem Cell Biol , vol.83 , pp. 687-695
    • Nicchitta, C.V.1    Lerner, R.S.2    Stephens, S.B.3    Dodd, R.D.4    Pyhtila, B.5
  • 45
    • 0036702296 scopus 로고    scopus 로고
    • A platform for compartmentalized protein synthesis: Protein translation and translocation in the ER
    • Nicchitta CV (2002) A platform for compartmentalized protein synthesis: protein translation and translocation in the ER. Curr Opin Cell Biol 14: 412-416.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 412-416
    • Nicchitta, C.V.1
  • 46
    • 84880604441 scopus 로고    scopus 로고
    • Take the (RN)A-train: Localization of mRNA to the endoplasmic reticulum
    • Hermesh O, Jansen R.P. (2013) Take the (RN)A-train: localization of mRNA to the endoplasmic reticulum. Biochim Biophys Acta 1833: 2519-2525.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 2519-2525
    • Hermesh, O.1    Jansen, R.P.2
  • 47
    • 84884760322 scopus 로고    scopus 로고
    • Translation- and SRP-independent mRNA targeting to the endoplasmic reticulum in the yeast saccharomyces cerevisiae
    • Kraut-Cohen J., Afanasieva E, Haim-Vilmovsky L, Slobodin B., Yosef I, et al. (2013) Translation- and SRP-independent mRNA targeting to the endoplasmic reticulum in the yeast Saccharomyces cerevisiae. Mol Biol Cell 24: 3069-3084.
    • (2013) Mol Biol Cell , vol.24 , pp. 3069-3084
    • Kraut-Cohen, J.1    Afanasieva, E.2    Haim-Vilmovsky, L.3    Slobodin, B.4    Yosef, I.5
  • 48
    • 84861534927 scopus 로고    scopus 로고
    • P180 promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulum
    • Cui XA, Zhang H, Palazzo A.F. (2012) p180 promotes the ribosome-independent localization of a subset of mRNA to the endoplasmic reticulum. PLoS Biol 10: e1001336.
    • (2012) PLoS Biol , vol.10 , pp. e1001336
    • Cui, X.A.1    Zhang, H.2    Palazzo, A.F.3
  • 49
    • 40449115740 scopus 로고    scopus 로고
    • Signal sequence- and translation-independent mRNA localization to the endoplasmic reticulum
    • Pyhtila B, Zheng T, Lager P.J., Keene JD, Reedy MC, et al. (2008) Signal sequence- and translation-independent mRNA localization to the endoplasmic reticulum. Rna 14: 445-453.
    • (2008) Rna , vol.14 , pp. 445-453
    • Pyhtila, B.1    Zheng, T.2    Lager, P.J.3    Keene, J.D.4    Reedy, M.C.5
  • 50
    • 33845597429 scopus 로고    scopus 로고
    • RNA-mediated sequestration of the RNA helicase eIF4A by pateamine A inhibits translation initiation
    • Bordeleau ME, Cencic R, Lindqvist L., Oberer M, Northcote P, et al (2006) RNA-mediated sequestration of the RNA helicase eIF4A by Pateamine A inhibits translation initiation. Chem Biol 13: 1287-1295.
    • (2006) Chem Biol , vol.13 , pp. 1287-1295
    • Bordeleau, M.E.1    Cencic, R.2    Lindqvist, L.3    Oberer, M.4    Northcote, P.5
  • 51
    • 69949118279 scopus 로고    scopus 로고
    • Inhibition of nonsense-mediated mRNA decay by the natural product pateamine A through eukaryotic initiation factor 4AIII
    • Dang Y, Low WK, Xu J, Gehring N.H., Dietz HC, et al. (2009) Inhibition of nonsense-mediated mRNA decay by the natural product pateamine A through eukaryotic initiation factor 4AIII. J Biol Chem 284: 23613-23621.
    • (2009) J Biol Chem , vol.284 , pp. 23613-23621
    • Dang, Y.1    Low, W.K.2    Xu, J.3    Gehring, N.H.4    Dietz, H.C.5
  • 52
    • 0041832111 scopus 로고    scopus 로고
    • Partitioning and translation of mRNAs encoding soluble proteins on membrane-bound ribosomes
    • Lerner RS, Seiser RM, Zheng T, Lager P.J., Reedy MC, et al. (2003) Partitioning and translation of mRNAs encoding soluble proteins on membrane-bound ribosomes. Rna 9: 1123-1137.
    • (2003) Rna , vol.9 , pp. 1123-1137
    • Lerner, R.S.1    Seiser, R.M.2    Zheng, T.3    Lager, P.J.4    Reedy, M.C.5
  • 53
    • 28644450485 scopus 로고    scopus 로고
    • Stable ribosome binding to the endoplasmic reticulum enables compartment-specific regulation of mRNA translation
    • Stephens SB, Dodd RD, Brewer J.W., Lager PJ, Keene JD, et al. (2005) Stable ribosome binding to the endoplasmic reticulum enables compartment-specific regulation of mRNA translation. Mol Biol Cell 16: 5819-5831.
    • (2005) Mol Biol Cell , vol.16 , pp. 5819-5831
    • Stephens, S.B.1    Dodd, R.D.2    Brewer, J.W.3    Lager, P.J.4    Keene, J.D.5
  • 54
    • 47049089675 scopus 로고    scopus 로고
    • Defective C-propeptides of the proalpha2(I) chain of type I procollagen impede molecular assembly and result in osteogenesis imperfecta
    • Pace JM, Wiese M, Drenguis A.S., Kuznetsova N., Leikin S, et al. (2008) Defective C-propeptides of the proalpha2(I) chain of type I procollagen impede molecular assembly and result in osteogenesis imperfecta. J Biol Chem 283: 16061-16067.
    • (2008) J Biol Chem , vol.283 , pp. 16061-16067
    • Pace, J.M.1    Wiese, M.2    Drenguis, A.S.3    Kuznetsova, N.4    Leikin, S.5
  • 55
    • 0029892471 scopus 로고    scopus 로고
    • Mutation in the carboxy-terminal propeptide of the pro alpha 1(I) chain of type I collagen in a child with severe osteogenesis imperfecta (OI type III): Possible implications for protein folding
    • Oliver JE, Thompson EM, Pope F.M., Nicholls A.C. (1996) Mutation in the carboxy-terminal propeptide of the Pro alpha 1(I) chain of type I collagen in a child with severe osteogenesis imperfecta (OI type III): possible implications for protein folding. Hum Mutat 7: 318-326.
    • (1996) Hum Mutat , vol.7 , pp. 318-326
    • Oliver, J.E.1    Thompson, E.M.2    Pope, F.M.3    Nicholls, A.C.4
  • 56
    • 0028338656 scopus 로고
    • Production of overmodified type I procollagen in a case of osteogenesis imperfecta
    • Tajima S, Takehana M, Azuma N. (1994) Production of overmodified type I procollagen in a case of osteogenesis imperfecta. J Dermatol 21: 219-222.
    • (1994) J Dermatol , vol.21 , pp. 219-222
    • Tajima, S.1    Takehana, M.2    Azuma, N.3
  • 57
    • 0028902639 scopus 로고
    • Endoplasmic reticulum-mediated quality control of type I collagen production by cells from osteogenesis imperfecta patients with mutations in the pro alpha 1 (I) chain carboxyl-terminal propeptide which impair subunit assembly
    • Lamande SR, Chessler SD, Golub S.B., Byers PH, Chan D, et al. (1995) Endoplasmic reticulum-mediated quality control of type I collagen production by cells from osteogenesis imperfecta patients with mutations in the pro alpha 1 (I) chain carboxyl-terminal propeptide which impair subunit assembly. J Biol Chem 270: 8642-8649.
    • (1995) J Biol Chem , vol.270 , pp. 8642-8649
    • Lamande, S.R.1    Chessler, S.D.2    Golub, S.B.3    Byers, P.H.4    Chan, D.5
  • 58
    • 33845653958 scopus 로고    scopus 로고
    • Isoelectric points and post-translational modifications of connexin26 and connexin32
    • Locke D, Koreen IV, Harris A.L. (2006) Isoelectric points and post-translational modifications of connexin26 and connexin32. FASEB J 20: 1221-1223.
    • (2006) FASEB J , vol.20 , pp. 1221-1223
    • Locke, D.1    Koreen, I.V.2    Harris, A.L.3
  • 59
    • 0023178378 scopus 로고
    • A structural mutation of the collagen alpha 1(I)CB7 peptide in lethal perinatal osteogenesis imperfecta
    • Bateman JF, Mascara T, Chan D., Cole W.G. (1987) A structural mutation of the collagen alpha 1(I)CB7 peptide in lethal perinatal osteogenesis imperfecta. J Biol Chem 262: 4445-4451.
    • (1987) J Biol Chem , vol.262 , pp. 4445-4451
    • Bateman, J.F.1    Mascara, T.2    Chan, D.3    Cole, W.G.4
  • 60
    • 33750932583 scopus 로고    scopus 로고
    • Fibrosis, not cell size, delineates beta-myosin heavy chain reexpression during cardiac hypertrophy and normal aging in vivo
    • Pandya K, Kim HS, Smithies O. (2006) Fibrosis, not cell size, delineates beta-myosin heavy chain reexpression during cardiac hypertrophy and normal aging in vivo. Proc Natl Acad Sci U S A 103: 16864-16869.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 16864-16869
    • Pandya, K.1    Kim, H.S.2    Smithies, O.3
  • 61
    • 0037392942 scopus 로고    scopus 로고
    • The specificities of protein kinase inhibitors: An update
    • Bain J, McLauchlan H, Elliott M., Cohen P. (2003) The specificities of protein kinase inhibitors: an update. Biochem J 371: 199-204.
    • (2003) Biochem J , vol.371 , pp. 199-204
    • Bain, J.1    McLauchlan, H.2    Elliott, M.3    Cohen, P.4
  • 62
    • 0026409760 scopus 로고
    • Myosin light chain kinase inhibitors ML-7 and ML-9 inhibit mouse lung carcinoma cell attachment to the fibronectin substratum
    • Isemura M, Mita T, Satoh K., Narumi K, Motomiya M. (1991) Myosin light chain kinase inhibitors ML-7 and ML-9 inhibit mouse lung carcinoma cell attachment to the fibronectin substratum. Cell Biol Int Rep 15: 965-972.
    • (1991) Cell Biol Int Rep , vol.15 , pp. 965-972
    • Isemura, M.1    Mita, T.2    Satoh, K.3    Narumi, K.4    Motomiya, M.5
  • 65
    • 0033613967 scopus 로고    scopus 로고
    • Identification and characterization of golgin-84, a novel golgi integral membrane protein with a cytoplasmic coiled-coil domain
    • Bascom RA, Srinivasan S, Nussbaum R.L. (1999) Identification and characterization of golgin-84, a novel Golgi integral membrane protein with a cytoplasmic coiled-coil domain. J Biol Chem 274: 2953-2962.
    • (1999) J Biol Chem , vol.274 , pp. 2953-2962
    • Bascom, R.A.1    Srinivasan, S.2    Nussbaum, R.L.3
  • 66
    • 0141751697 scopus 로고    scopus 로고
    • Ca2+ sensitivity of smooth muscle and nonmuscle myosin II: Modulated by G proteins, kinases, and myosin phosphatase
    • Somlyo AP, Somlyo A.V. (2003) Ca2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase. Physiol Rev 83: 1325-1358.
    • (2003) Physiol Rev , vol.83 , pp. 1325-1358
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 67
    • 33745505877 scopus 로고    scopus 로고
    • Myosin light chain kinase plays a role in the regulation of epithelial cell survival
    • Connell LE, Helfman D.M. (2006) Myosin light chain kinase plays a role in the regulation of epithelial cell survival. J Cell Sci 119: 2269-2281.
    • (2006) J Cell Sci , vol.119 , pp. 2269-2281
    • Connell, L.E.1    Helfman, D.M.2
  • 68
    • 34548303687 scopus 로고    scopus 로고
    • Myosin light chain kinase-independent inhibition by ML-9 of murine TRPC6 channels expressed in HEK293 cells
    • Shi J, Takahashi S, Jin X.H., Li YQ, Ito Y, et al. (2007) Myosin light chain kinase-independent inhibition by ML-9 of murine TRPC6 channels expressed in HEK293 cells. Br J Pharmacol 152: 122-131.
    • (2007) Br J Pharmacol , vol.152 , pp. 122-131
    • Shi, J.1    Takahashi, S.2    Jin, X.H.3    Li, Y.Q.4    Ito, Y.5
  • 69
    • 0033600789 scopus 로고    scopus 로고
    • Proteasomal degradation of unassembled mutant type I collagen pro- alpha1(I) chains
    • Fitzgerald J, Lamande SR, Bateman J.F. (1999) Proteasomal degradation of unassembled mutant type I collagen pro- alpha1(I) chains. J Biol Chem 274: 27392-27398.
    • (1999) J Biol Chem , vol.274 , pp. 27392-27398
    • Fitzgerald, J.1    Lamande, S.R.2    Bateman, J.F.3
  • 70
    • 0033208952 scopus 로고    scopus 로고
    • Procollagen folding and assembly: The role of endoplasmic reticulum enzymes and molecular chaperones
    • Lamande SR, BatemanJF (1999) Procollagen folding and assembly: the role of endoplasmic reticulum enzymes and molecular chaperones. Semin Cell Dev Biol 10: 455-464.
    • (1999) Semin Cell Dev Biol , vol.10 , pp. 455-464
    • Lamande, S.R.1    Bateman, J.F.2
  • 71
    • 0038676258 scopus 로고    scopus 로고
    • Regulation of wound healing by growth factors and cytokines
    • Werner S, Grose R. (2003) Regulation of wound healing by growth factors and cytokines. Physiol Rev 83: 835-870.
    • (2003) Physiol Rev , vol.83 , pp. 835-870
    • Werner, S.1    Grose, R.2
  • 72
    • 77957263381 scopus 로고    scopus 로고
    • Fibrosis in hypertensive heart disease: Molecular pathways and cardioprotective strategies
    • Shahbaz AU, Sun Y, Bhattacharya S.K., Ahokas RA, Gerling IC, et al. (2010) Fibrosis in hypertensive heart disease: molecular pathways and cardioprotective strategies. J Hypertens 28 Suppl 1: S25-32.
    • (2010) J Hypertens 28 Suppl , vol.1 , pp. S25-32
    • Shahbaz, A.U.1    Sun, Y.2    Bhattacharya, S.K.3    Ahokas, R.A.4    Gerling, I.C.5
  • 74
    • 33746813256 scopus 로고    scopus 로고
    • Total absence of the alpha2(I) chain of collagen type I causes a rare form of ehlers-danlos syndrome with hypermobility and propensity to cardiac valvular problems
    • Malfait F, Symoens S, Coucke P., Nunes L, De Almeida S, et al. (2006) Total absence of the alpha2(I) chain of collagen type I causes a rare form of Ehlers-Danlos syndrome with hypermobility and propensity to cardiac valvular problems. J Med Genet 43: e36.
    • (2006) J Med Genet , vol.43 , pp. e36
    • Malfait, F.1    Symoens, S.2    Coucke, P.3    Nunes, L.4    De Almeida, S.5
  • 75
    • 0022760257 scopus 로고
    • Clinical features of homozygous alpha 2(I) collagen deficient osteogenesis imperfecta
    • Pope FM, Nicolls AC, Osse G, Lee K.W. (1986) Clinical features of homozygous alpha 2(I) collagen deficient osteogenesis imperfecta. J Med Genet 23: 377.
    • (1986) J Med Genet , vol.23 , pp. 377
    • Pope, F.M.1    Nicolls, A.C.2    Osse, G.3    Lee, K.W.4
  • 76
    • 0035984335 scopus 로고    scopus 로고
    • The role of the alpha2 chain in the stabilization of the collagen type I heterotrimer: A study of the type I homotrimer in oim mouse tissues
    • Miles CA, Sims TJ, Camacho N.P., Bailey A.J. (2002) The role of the alpha2 chain in the stabilization of the collagen type I heterotrimer: a study of the type I homotrimer in oim mouse tissues. J Mol Biol 321: 797-805.
    • (2002) J Mol Biol , vol.321 , pp. 797-805
    • Miles, C.A.1    Sims, T.J.2    Camacho, N.P.3    Bailey, A.J.4
  • 78
    • 25444502378 scopus 로고    scopus 로고
    • Collagen triple-helix formation in all-trans chains proceeds by a nucleation/growth mechanism with a purely entropic barrier
    • Bachmann A, Kiefhaber T, Boudko S., Engel J, Bachinger H.P. (2005) Collagen triple-helix formation in all-trans chains proceeds by a nucleation/growth mechanism with a purely entropic barrier. Proc Natl Acad Sci USA 102: 13897-13902.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13897-13902
    • Bachmann, A.1    Kiefhaber, T.2    Boudko, S.3    Engel, J.4    Bachinger, H.P.5
  • 79
    • 0036290657 scopus 로고    scopus 로고
    • Nucleation and propagation of the collagen triple helix in single-chain and trimerized peptides: Transition from third to first order kinetics
    • Boudko S, Frank S, Kammerer R.A., Stetefeld J., Schulthess T, et al. (2002) Nucleation and propagation of the collagen triple helix in single-chain and trimerized peptides: transition from third to first order kinetics. J Mol Biol 317: 459-470.
    • (2002) J Mol Biol , vol.317 , pp. 459-470
    • Boudko, S.1    Frank, S.2    Kammerer, R.A.3    Stetefeld, J.4    Schulthess, T.5
  • 80
    • 0033521011 scopus 로고    scopus 로고
    • Substrate recognition of collagen-specific molecular chaperone HSP47. Structural requirements and binding regulation
    • Koide T, Asada S, Nagata K. (1999) Substrate recognition of collagen-specific molecular chaperone HSP47. Structural requirements and binding regulation. J Biol Chem 274: 34523-34526.
    • (1999) J Biol Chem , vol.274 , pp. 34523-34526
    • Koide, T.1    Asada, S.2    Nagata, K.3
  • 81
    • 33646286416 scopus 로고    scopus 로고
    • Hsp47: A collagen-specific molecular chaperone
    • Nagata K (1996) Hsp47: a collagen-specific molecular chaperone. Trends Biochem Sci 21: 22-26.
    • (1996) Trends Biochem Sci , vol.21 , pp. 22-26
    • Nagata, K.1
  • 82
    • 84860135774 scopus 로고    scopus 로고
    • Regulation of polysome assembly on the endoplasmic reticulum by a coiled-coil protein, p180
    • Ueno T, Kaneko K, Sata T., Hattori S, Ogawa-Goto K (2012) Regulation of polysome assembly on the endoplasmic reticulum by a coiled-coil protein, p180. Nucleic Acids Res 40: 3006-3017.
    • (2012) Nucleic Acids Res , vol.40 , pp. 3006-3017
    • Ueno, T.1    Kaneko, K.2    Sata, T.3    Hattori, S.4    Ogawa-Goto, K.5
  • 83
    • 72149085437 scopus 로고    scopus 로고
    • Expansion of the trans-golgi network following activated collagen secretion is supported by a coiled-coil microtubule-bundling protein, p180, on the ER
    • Ueno T, Kaneko K, Katano H., Sato Y, Mazitschek R, et al (2010) Expansion of the trans-Golgi network following activated collagen secretion is supported by a coiled-coil microtubule-bundling protein, p180, on the ER. Exp Cell Res 316: 329-340.
    • (2010) Exp Cell Res , vol.316 , pp. 329-340
    • Ueno, T.1    Kaneko, K.2    Katano, H.3    Sato, Y.4    Mazitschek, R.5
  • 84
    • 84885645857 scopus 로고    scopus 로고
    • Identification of a region within the placental alkaline phosphatase mRNA that mediates p180-dependent targeting to the endoplasmic reticulum
    • Cui XA, Zhang Y, Hong S.J., Palazzo A.F. (2013) Identification of a region within the placental alkaline phosphatase mRNA that mediates p180-dependent targeting to the endoplasmic reticulum. J Biol Chem 288: 29633-29641.
    • (2013) J Biol Chem , vol.288 , pp. 29633-29641
    • Cui, X.A.1    Zhang, Y.2    Hong, S.J.3    Palazzo, A.F.4
  • 85
    • 0842347405 scopus 로고    scopus 로고
    • TRAM2 protein interacts with endoplasmic reticulum ca2+ pump serca2b and is necessary for collagen type I synthesis
    • Stefanovic B, Stefanovic L, Schnabl B., Bataller R, Brenner D.A. (2004) TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and is necessary for collagen type I synthesis. Mol Cell Biol 24: 1758-1768.
    • (2004) Mol Cell Biol , vol.24 , pp. 1758-1768
    • Stefanovic, B.1    Stefanovic, L.2    Schnabl, B.3    Bataller, R.4    Brenner, D.A.5
  • 86
    • 0037328573 scopus 로고    scopus 로고
    • Myosin motors and not actin comets are mediators of the actin-based golgi-to-endoplasmic reticulum protein transport
    • Duran JM, Valderrama F, Castel S., Magdalena J, Tomas M, et al (2003) Myosin motors and not actin comets are mediators of the actin-based Golgi-to-endoplasmic reticulum protein transport. Mol Biol Cell 14: 445-459.
    • (2003) Mol Biol Cell , vol.14 , pp. 445-459
    • Duran, J.M.1    Valderrama, F.2    Castel, S.3    Magdalena, J.4    Tomas, M.5
  • 87
    • 39449101285 scopus 로고    scopus 로고
    • Nonmuscle myosin II moves in new directions
    • Conti MA, Adelstein R.S. (2008) Nonmuscle myosin II moves in new directions. J Cell Sci 121: 11-18.
    • (2008) J Cell Sci , vol.121 , pp. 11-18
    • Conti, M.A.1    Adelstein, R.S.2
  • 88
    • 1542314212 scopus 로고    scopus 로고
    • Nonmuscle myosin IIb is involved in the guidance of fibroblast migration
    • Lo CM, Buxton DB, Chua G.C., Dembo M., Adelstein RS, et al. (2004) Nonmuscle myosin IIb is involved in the guidance of fibroblast migration. Mol Biol Cell 15: 982-989.
    • (2004) Mol Biol Cell , vol.15 , pp. 982-989
    • Lo, C.M.1    Buxton, D.B.2    Chua, G.C.3    Dembo, M.4    Adelstein, R.S.5
  • 89
    • 0030604542 scopus 로고    scopus 로고
    • TGFbeta signaling: Receptors, transducers, and mad proteins
    • Massague J (1996) TGFbeta signaling: receptors, transducers, and Mad proteins. Cell 85: 947-950.
    • (1996) Cell , vol.85 , pp. 947-950
    • Massague, J.1


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