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Volumn 168, Issue 4, 2006, Pages 1299-1308

Mutant fibrinogen cleared from the endoplasmic reticulum via endoplasmic reticulum-associated protein degradation and autophagy: An explanation for liver disease

Author keywords

[No Author keywords available]

Indexed keywords

AGUADILLA; ARGININE; FIBRINOGEN; FIBRINOGEN VARIANT; MUTANT PROTEIN; POLYPEPTIDE; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 33645451010     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: 10.2353/ajpath.2006.051097     Document Type: Article
Times cited : (95)

References (58)
  • 1
    • 28344448202 scopus 로고    scopus 로고
    • Fibrinogen and fibrin structure and function
    • Mosesson MW: Fibrinogen and fibrin structure and function. J Thromb Haemost 2005, 3:1894-1904
    • (2005) J Thromb Haemost , vol.3 , pp. 1894-1904
    • Mosesson, M.W.1
  • 2
    • 17444392120 scopus 로고    scopus 로고
    • Fibrinogen and fibrin
    • Weisel JW: Fibrinogen and fibrin. Adv Protein Chem 2005, 70:247-299
    • (2005) Adv Protein Chem , vol.70 , pp. 247-299
    • Weisel, J.W.1
  • 4
    • 0029661284 scopus 로고    scopus 로고
    • The role of betagamma and alphagamma complexes in the assembly of human fibrinogen
    • Huang S, Cao Z, Chung DW, Davie EW: The role of betagamma and alphagamma complexes in the assembly of human fibrinogen. J Biol Chem 1996, 271:27942-27947
    • (1996) J Biol Chem , vol.271 , pp. 27942-27947
    • Huang, S.1    Cao, Z.2    Chung, D.W.3    Davie, E.W.4
  • 5
    • 0034964312 scopus 로고    scopus 로고
    • Fibrinogen biosynthesis: Assembly, intracellular degradation, and association with lipid synthesis and secretion
    • Redman CM, Xia H: Fibrinogen biosynthesis: assembly, intracellular degradation, and association with lipid synthesis and secretion. Ann NY Acad Sci 2001, 936:480-495
    • (2001) Ann NY Acad Sci , vol.936 , pp. 480-495
    • Redman, C.M.1    Xia, H.2
  • 6
    • 0033546716 scopus 로고    scopus 로고
    • The degradation of nascent fibrinogen chains is mediated by the ubiquitin proteasome pathway
    • Xia H, Redman CM: The degradation of nascent fibrinogen chains is mediated by the ubiquitin proteasome pathway. Biochem Biophys Res Commun 1999, 261:590-597
    • (1999) Biochem Biophys Res Commun , vol.261 , pp. 590-597
    • Xia, H.1    Redman, C.M.2
  • 9
    • 0033882702 scopus 로고    scopus 로고
    • Fibrinogen brescia: Hepatic endoplasmic reticulum storage and hypofibrinogenemia because of a gamma284 Gly→Arg mutation
    • Brennan SO, Wyatt J, Medicina D, Callea F, George PM: Fibrinogen brescia: hepatic endoplasmic reticulum storage and hypofibrinogenemia because of a gamma284 Gly→Arg mutation. Am J Pathol 2000, 157:189-196
    • (2000) Am J Pathol , vol.157 , pp. 189-196
    • Brennan, S.O.1    Wyatt, J.2    Medicina, D.3    Callea, F.4    George, P.M.5
  • 10
    • 0036707542 scopus 로고    scopus 로고
    • Novel fibrinogen gamma375 Arg→Trp mutation (fibrinogen aguadilla) causes hepatic endoplasmic reticulum storage and hypofibrinogenemia
    • Brennan SO, Maghzal G, Shneider BL, Gordon R, Magid MS, George PM: Novel fibrinogen gamma375 Arg→Trp mutation (fibrinogen aguadilla) causes hepatic endoplasmic reticulum storage and hypofibrinogenemia. Hepatology 2002, 36:652-658
    • (2002) Hepatology , vol.36 , pp. 652-658
    • Brennan, S.O.1    Maghzal, G.2    Shneider, B.L.3    Gordon, R.4    Magid, M.S.5    George, P.M.6
  • 11
    • 0025350658 scopus 로고
    • Alpha 1-antitrypsin deficiency, emphysema, and liver disease: Genetic basis and strategies for therapy
    • Crystal RG: Alpha 1-antitrypsin deficiency, emphysema, and liver disease: genetic basis and strategies for therapy. J Clin Invest 1990, 85:1343-1352
    • (1990) J Clin Invest , vol.85 , pp. 1343-1352
    • Crystal, R.G.1
  • 12
    • 0024238708 scopus 로고
    • The natural history of liver disease in alpha 1-antitrypsin deficient children
    • Sveger T: The natural history of liver disease in alpha 1-antitrypsin deficient children. Acta Paediatr Scand 1988, 77:847-851
    • (1988) Acta Paediatr Scand , vol.77 , pp. 847-851
    • Sveger, T.1
  • 13
    • 0028593988 scopus 로고
    • A lag in intracellular degradation of mutant alpha-1-antitrypsin correlates with the liver disease phentotype in homozygous PiZZ individuals
    • Wu Y, Whitman I, Molmenti E, Moore K, Hippenmeyer P, Perlmutter DH: A lag in intracellular degradation of mutant alpha-1-antitrypsin correlates with the liver disease phentotype in homozygous PiZZ individuals. Proc Natl Acad Sci USA 1994, 91:9014-9018
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9014-9018
    • Wu, Y.1    Whitman, I.2    Molmenti, E.3    Moore, K.4    Hippenmeyer, P.5    Perlmutter, D.H.6
  • 14
    • 85047684827 scopus 로고    scopus 로고
    • α1-antitrypsin polymerization and the serpinopathies: Pathobiology and the prospects for therapy
    • Lomas DA, Mahadeva R: α1-Antitrypsin polymerization and the serpinopathies: pathobiology and the prospects for therapy. J Clin Investig 2002, 110:1585-1590
    • (2002) J Clin Investig , vol.110 , pp. 1585-1590
    • Lomas, D.A.1    Mahadeva, R.2
  • 15
    • 1542466459 scopus 로고    scopus 로고
    • Alpha1-antitrypsin deficiency: Liver disease associated with retention of a mutant secretory glycoprotein in the endoplasmic reticulum
    • Edited by P Brass, N Gregersen. Totowa, NJ, Humana Press
    • Perlmutter DH: Alpha1-antitrypsin deficiency: liver disease associated with retention of a mutant secretory glycoprotein in the endoplasmic reticulum. Protein Misfolding and Disease, Principles and Protocols. Edited by P Brass, N Gregersen. Totowa, NJ, Humana Press, 2003, pp 39-56
    • (2003) Protein Misfolding and Disease, Principles and Protocols , pp. 39-56
    • Perlmutter, D.H.1
  • 16
    • 0030465416 scopus 로고    scopus 로고
    • A 30-year perspective on alpha 1-antitrypsin deficiency
    • Eriksson S: A 30-year perspective on alpha 1-antitrypsin deficiency. Chest 1996, 110:237S-242S
    • (1996) Chest , vol.110
    • Eriksson, S.1
  • 17
    • 0035976919 scopus 로고    scopus 로고
    • The proteasome participates in degradation of mutant alpha 1-antitrypsin Z in the endoplasmic reticulum of hepatoma-derived hepatocytes
    • Teckman JH, Burrows J, Hidvegi T, Schmidt B, Hale PD, Perlmutter DH: The proteasome participates in degradation of mutant alpha 1-antitrypsin Z in the endoplasmic reticulum of hepatoma-derived hepatocytes. J Biol Chem 2001, 276:44865-44872
    • (2001) J Biol Chem , vol.276 , pp. 44865-44872
    • Teckman, J.H.1    Burrows, J.2    Hidvegi, T.3    Schmidt, B.4    Hale, P.D.5    Perlmutter, D.H.6
  • 18
    • 0030447659 scopus 로고    scopus 로고
    • Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate
    • Werner ED, Brodsky JL, McCracken AA: Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate. Proc Natl Acad Sci USA 1999, 93:13797-13801
    • (1999) Proc Natl Acad Sci USA , vol.93 , pp. 13797-13801
    • Werner, E.D.1    Brodsky, J.L.2    McCracken, A.A.3
  • 19
    • 30044436220 scopus 로고    scopus 로고
    • Characterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: One for soluble A1PiZ and another for aggregates of A1PiZ
    • Kruse KB, Brodsky JL, McCracken AA: Characterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: one for soluble A1PiZ and another for aggregates of A1PiZ. Mol Biol Cell 2005, 17:203-212
    • (2005) Mol Biol Cell , vol.17 , pp. 203-212
    • Kruse, K.B.1    Brodsky, J.L.2    McCracken, A.A.3
  • 20
    • 0033671965 scopus 로고    scopus 로고
    • Retention of mutant alpha(1)-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response
    • Teckman JH, Perlmutter DH: Retention of mutant alpha(1)-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response. Am J Physiol Gastrointest Liver Physiol 2000, 279:G961-G974
    • (2000) Am J Physiol Gastrointest Liver Physiol , vol.279
    • Teckman, J.H.1    Perlmutter, D.H.2
  • 23
    • 0027418063 scopus 로고
    • PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chrymotryptic activity and degradation of ubiquitinated proteins
    • Heinemeyer W, Gruhler A, Mohrle V, Mahe Y, Wolf DH: PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chrymotryptic activity and degradation of ubiquitinated proteins. J Biol Chem 1993, 268:5115-5120
    • (1993) J Biol Chem , vol.268 , pp. 5115-5120
    • Heinemeyer, W.1    Gruhler, A.2    Mohrle, V.3    Mahe, Y.4    Wolf, D.H.5
  • 24
    • 0027759380 scopus 로고
    • A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome
    • Brodsky JL, Schekman R: A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome. J Cell Biol 1993, 123:1355-1363
    • (1993) J Cell Biol , vol.123 , pp. 1355-1363
    • Brodsky, J.L.1    Schekman, R.2
  • 25
    • 0035889160 scopus 로고    scopus 로고
    • The alternatively spliced alpha(E)C domain of human fibrinogen-420 is a novel ligand for leukocyte integrins alpha(M)beta(2) and alpha(X)beta(2)
    • Lishko VK, Yakubenko VP, Hertzberg KM, Grieninger G, Ugarova TP: The alternatively spliced alpha(E)C domain of human fibrinogen-420 is a novel ligand for leukocyte integrins alpha(M)beta(2) and alpha(X)beta(2). Blood 2001, 98:2448-2455
    • (2001) Blood , vol.98 , pp. 2448-2455
    • Lishko, V.K.1    Yakubenko, V.P.2    Hertzberg, K.M.3    Grieninger, G.4    Ugarova, T.P.5
  • 26
    • 0028586017 scopus 로고
    • Regulatable promoters of Saccharomyces cerevisiae: Comparison of transcriptional activity and their use for heterologous expression
    • Mumberg D, Müller R, Funk M: Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression. Nucleic Acids Res 1994, 22:5767-5768
    • (1994) Nucleic Acids Res , vol.22 , pp. 5767-5768
    • Mumberg, D.1    Müller, R.2    Funk, M.3
  • 27
    • 14744271884 scopus 로고
    • High-level expression of tetanus toxin fragment-C in Pichia-pastoris strains containing multiple tandem integrations of the gene
    • Clare JJ, Rayment FB, Ballantine SP, Sreekrishna K, Romanos MA: High-level expression of tetanus toxin fragment-C in Pichia-pastoris strains containing multiple tandem integrations of the gene. BioTechnology 1991, 9:455-460
    • (1991) BioTechnology , vol.9 , pp. 455-460
    • Clare, J.J.1    Rayment, F.B.2    Ballantine, S.P.3    Sreekrishna, K.4    Romanos, M.A.5
  • 28
    • 30044439688 scopus 로고    scopus 로고
    • Techniques and protocols: High-efficiency transformation of yeast
    • Edited by MM Dickerson. New York, Cold Spring Harbor Press
    • Adams A, Gottschling DE, Kaiser CA, Stearns T: Techniques and protocols: high-efficiency transformation of yeast. Methods in Yeast Genetics. Edited by MM Dickerson. New York, Cold Spring Harbor Press, 1997, pp 99-102
    • (1997) Methods in Yeast Genetics , pp. 99-102
    • Adams, A.1    Gottschling, D.E.2    Kaiser, C.A.3    Stearns, T.4
  • 30
    • 0027313552 scopus 로고
    • Selective protein degradation in the yeast exocytic pathway
    • McCracken AA, Kruse KB: Selective protein degradation in the yeast exocytic pathway. Mol Biol Cell 1993, 4:729-736
    • (1993) Mol Biol Cell , vol.4 , pp. 729-736
    • McCracken, A.A.1    Kruse, K.B.2
  • 31
    • 0032558972 scopus 로고    scopus 로고
    • Mutations in the cytosolic DnaJ homologue, YDJ1, delay and compromise the efficient translation of heterologous proteins in yeast
    • Brodsky JL, Lawrence JG, Caplan AJ: Mutations in the cytosolic DnaJ homologue, YDJ1, delay and compromise the efficient translation of heterologous proteins in yeast. Biochemistry 1998, 37:18045-18055
    • (1998) Biochemistry , vol.37 , pp. 18045-18055
    • Brodsky, J.L.1    Lawrence, J.G.2    Caplan, A.J.3
  • 32
    • 0030845363 scopus 로고    scopus 로고
    • Electrospray ionisation analysis of human fibrinogen
    • Brennan SO: Electrospray ionisation analysis of human fibrinogen. Thromb Haemost 1997, 78:1055-1058
    • (1997) Thromb Haemost , vol.78 , pp. 1055-1058
    • Brennan, S.O.1
  • 33
    • 0034108939 scopus 로고    scopus 로고
    • Isolation of ERp29, a novel endoplasmic reticulum protein, from rat enamel cells: Evidence for a unique role in secretory-protein synthesis
    • Hubbard MJ, Mchugh NJ, Carne DL: Isolation of ERp29, a novel endoplasmic reticulum protein, from rat enamel cells: evidence for a unique role in secretory-protein synthesis. Eur J Biochem 2000, 267:1945-1956
    • (2000) Eur J Biochem , vol.267 , pp. 1945-1956
    • Hubbard, M.J.1    Mchugh, N.J.2    Carne, D.L.3
  • 35
    • 24044535062 scopus 로고    scopus 로고
    • Grp78, Grp94 and Grp170 interact with alpha-1-antitrypsin mutants that are retained in the endoplasmic reticulum
    • Schmidt BZ, Perlmutter DH: Grp78, Grp94 and Grp170 interact with alpha-1-antitrypsin mutants that are retained in the endoplasmic reticulum. Am J Physiol Gastrointest Liver Physiol 2005, 289:G444-G455
    • (2005) Am J Physiol Gastrointest Liver Physiol , vol.289
    • Schmidt, B.Z.1    Perlmutter, D.H.2
  • 36
    • 0025924634 scopus 로고
    • Glycosylation and structure of the yeast MF alpha 1 alpha-factor precursor is important for efficient transport through the secretory pathway
    • Caplan S, Green R, Rocco J, Kurjan J: Glycosylation and structure of the yeast MF alpha 1 alpha-factor precursor is important for efficient transport through the secretory pathway. J Bacteriol 1991, 173:627-635
    • (1991) J Bacteriol , vol.173 , pp. 627-635
    • Caplan, S.1    Green, R.2    Rocco, J.3    Kurjan, J.4
  • 37
    • 0027246187 scopus 로고
    • Processing of the carboxyl 15-amino acid extension in the alpha-chain of fibrinogen
    • Farrell DH, Huang S, Davie EW: Processing of the carboxyl 15-amino acid extension in the alpha-chain of fibrinogen. J Biol Chem 1993, 268:10351-10355
    • (1993) J Biol Chem , vol.268 , pp. 10351-10355
    • Farrell, D.H.1    Huang, S.2    Davie, E.W.3
  • 38
    • 0028881825 scopus 로고
    • Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (A alpha 20 Val → Asp)
    • Brennan SO, Hammonds B, George PM: Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (A alpha 20 Val → Asp). J Clin Invest 1995, 96:2854-2858
    • (1995) J Clin Invest , vol.96 , pp. 2854-2858
    • Brennan, S.O.1    Hammonds, B.2    George, P.M.3
  • 39
    • 27244462836 scopus 로고    scopus 로고
    • Differential degradation of the three fibrinogen chains by proteasomes: Involvement of Sec61p and cytosolic Hsp70
    • Xia H, Redman CM: Differential degradation of the three fibrinogen chains by proteasomes: involvement of Sec61p and cytosolic Hsp70. Arch Biochem Biophys 2001, 390:137-145
    • (2001) Arch Biochem Biophys , vol.390 , pp. 137-145
    • Xia, H.1    Redman, C.M.2
  • 40
    • 0037769904 scopus 로고    scopus 로고
    • Stress tolerance of misfolded carboxypeptidase Y requires maintenance of protein trafficking and degradative pathways
    • Spear ED, Ng DT: Stress tolerance of misfolded carboxypeptidase Y requires maintenance of protein trafficking and degradative pathways. Mol Biol Cell 2003, 14:2756-2767
    • (2003) Mol Biol Cell , vol.14 , pp. 2756-2767
    • Spear, E.D.1    Ng, D.T.2
  • 41
    • 0029829005 scopus 로고    scopus 로고
    • A pathway for targeting soluble misfolded proteins to the yeast vacuole
    • Hong E, Davidson AR, Kaiser CA: A pathway for targeting soluble misfolded proteins to the yeast vacuole. J Cell Biol 1996, 135:623-633
    • (1996) J Cell Biol , vol.135 , pp. 623-633
    • Hong, E.1    Davidson, A.R.2    Kaiser, C.A.3
  • 42
    • 0032511128 scopus 로고    scopus 로고
    • Different degradation pathways for heterologous glycoproteins in yeast
    • Holkeri H, Makarow M: Different degradation pathways for heterologous glycoproteins in yeast. FEBS Lett 1998, 429:162-166
    • (1998) FEBS Lett , vol.429 , pp. 162-166
    • Holkeri, H.1    Makarow, M.2
  • 43
    • 0038785977 scopus 로고    scopus 로고
    • Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae
    • Jorgensen MU, Emr SD, Winther JR: Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae. Eur J Biochem 1999, 260:461-469
    • (1999) Eur J Biochem , vol.260 , pp. 461-469
    • Jorgensen, M.U.1    Emr, S.D.2    Winther, J.R.3
  • 44
    • 2442582580 scopus 로고    scopus 로고
    • Degradation of mutated bovine pancreatic trypsin inhibitor (BPTI) in the yeast vacuole suggests post-endoplasmic reticulum protein quality control
    • Coughlan CM, Walker JL, Cochran JC, Wittrup KD, Brodsky JL: Degradation of mutated bovine pancreatic trypsin inhibitor (BPTI) in the yeast vacuole suggests post-endoplasmic reticulum protein quality control. J Biol Chem 2004, 279:15289-15297
    • (2004) J Biol Chem , vol.279 , pp. 15289-15297
    • Coughlan, C.M.1    Walker, J.L.2    Cochran, J.C.3    Wittrup, K.D.4    Brodsky, J.L.5
  • 45
    • 0036843023 scopus 로고    scopus 로고
    • Secretory pathway quality control operating in Golgi, plasmalemmal, and endosomal systems
    • Arvan P, Zhao X, Ramos-Castaneda J, Chang A: Secretory pathway quality control operating in Golgi, plasmalemmal, and endosomal systems. Traffic 2002, 3:771-780
    • (2002) Traffic , vol.3 , pp. 771-780
    • Arvan, P.1    Zhao, X.2    Ramos-Castaneda, J.3    Chang, A.4
  • 46
    • 0020338057 scopus 로고
    • PEP4 gene function is required for expression of several vacuolar hydrolases in Saccharomyces cerevisiae
    • Jones EW, Zubenko GS, Parker RR: PEP4 gene function is required for expression of several vacuolar hydrolases in Saccharomyces cerevisiae. Genetics 102:665-677, 1982
    • (1982) Genetics , vol.102 , pp. 665-677
    • Jones, E.W.1    Zubenko, G.S.2    Parker, R.R.3
  • 47
    • 0026755363 scopus 로고
    • The mechanism of Z alpha 1-antitrypsin accumulation in the liver
    • Lomas DA, Evans DL, Finch JT, Carrell RW: The mechanism of Z alpha 1-antitrypsin accumulation in the liver. Nature 1992, 357:605-607
    • (1992) Nature , vol.357 , pp. 605-607
    • Lomas, D.A.1    Evans, D.L.2    Finch, J.T.3    Carrell, R.W.4
  • 49
    • 0035809160 scopus 로고    scopus 로고
    • Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae
    • Kihara A, Noda T, Ishihara N, Ohsumi Y: Two distinct Vps34 phosphatidylinositol 3-kinase complexes function in autophagy and carboxypeptidase Y sorting in Saccharomyces cerevisiae. J Cell Biol 2001, 152:519-530
    • (2001) J Cell Biol , vol.152 , pp. 519-530
    • Kihara, A.1    Noda, T.2    Ishihara, N.3    Ohsumi, Y.4
  • 50
    • 0037135980 scopus 로고    scopus 로고
    • Novel PtdIns(3)P-binding protein Etf1 functions as an effector of the Vps34 Ptdlns 3-kinase in autophagy
    • Wurmser AE, Emr SD: Novel PtdIns(3)P-binding protein Etf1 functions as an effector of the Vps34 Ptdlns 3-kinase in autophagy. J Cell Biol 2002, 158:761-772
    • (2002) J Cell Biol , vol.158 , pp. 761-772
    • Wurmser, A.E.1    Emr, S.D.2
  • 51
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston JA, Ward CL, Kopito RR: Aggresomes: a cellular response to misfolded proteins. J Cell Biol 1998, 143:1883-1898
    • (1998) J Cell Biol , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 52
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito RR: Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 2000, 10:524-530
    • (2000) Trends Cell Biol , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 53
    • 0036303981 scopus 로고    scopus 로고
    • Hassles with taking out the garbage: Aggravating aggresomes
    • Garcia-Mata R, Gao YS, Sztul E: Hassles with taking out the garbage: aggravating aggresomes. Traffic 2002, 3:388-396
    • (2002) Traffic , vol.3 , pp. 388-396
    • Garcia-Mata, R.1    Gao, Y.S.2    Sztul, E.3
  • 54
    • 0029859978 scopus 로고    scopus 로고
    • Molecular pathogenesis of liver disease in alpha1-antitrypsin deficiency
    • Teckman JH, Qu D, Perlmutter DH: Molecular pathogenesis of liver disease in alpha1-antitrypsin deficiency. Hepatology 1996, 24:1504-1516
    • (1996) Hepatology , vol.24 , pp. 1504-1516
    • Teckman, J.H.1    Qu, D.2    Perlmutter, D.H.3
  • 55
    • 19444363520 scopus 로고    scopus 로고
    • Protein retention in the endoplasmic reticulum, blockade of programmed cell death and autophagy selectively occur in spinal cord motoneurons after glutamate receptor-mediated injury
    • Tarabal O, Caldero J, Casas C, Oppenheim RW, Esquerda JE: Protein retention in the endoplasmic reticulum, blockade of programmed cell death and autophagy selectively occur in spinal cord motoneurons after glutamate receptor-mediated injury. Mol Cell Neurosci 2005, 29:283-298
    • (2005) Mol Cell Neurosci , vol.29 , pp. 283-298
    • Tarabal, O.1    Caldero, J.2    Casas, C.3    Oppenheim, R.W.4    Esquerda, J.E.5
  • 56
    • 2942718944 scopus 로고    scopus 로고
    • Reversal of mutant myocilin non-secretion and cell killing: Implications for glaucoma
    • Liu Y, Vollrath D: Reversal of mutant myocilin non-secretion and cell killing: implications for glaucoma. Hum Mol Genet 2004, 13:1193-1204
    • (2004) Hum Mol Genet , vol.13 , pp. 1193-1204
    • Liu, Y.1    Vollrath, D.2
  • 57
    • 20444459545 scopus 로고    scopus 로고
    • Autophagy is a prosurvival mechanism in cells expressing an autosomal dominant familial neurohypophyseal diabetes insipidus mutant vasopressin transgene
    • Castino R, Davies J, Beaucourt S, Isidoro C, Murphy D: Autophagy is a prosurvival mechanism in cells expressing an autosomal dominant familial neurohypophyseal diabetes insipidus mutant vasopressin transgene. FASEB J 2005, 19:1021-1023
    • (2005) FASEB J , vol.19 , pp. 1021-1023
    • Castino, R.1    Davies, J.2    Beaucourt, S.3    Isidoro, C.4    Murphy, D.5
  • 58
    • 22344450345 scopus 로고    scopus 로고
    • Use of yeast as a model system to investigate protein conformational diseases
    • Coughlan CM, Brodsky JL: Use of yeast as a model system to investigate protein conformational diseases. Mol Biotechnol 2005, 30:171-180
    • (2005) Mol Biotechnol , vol.30 , pp. 171-180
    • Coughlan, C.M.1    Brodsky, J.L.2


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