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Volumn 12, Issue 5, 1997, Pages 404-416

Review: α1-Antitrypsin deficiency associated liver disease

Author keywords

endoplasmic reticulum degradation; liver disease

Indexed keywords

ALPHA 1 ANTITRYPSIN DEFICIENCY; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; GENETIC DISORDER; HUMAN; LIVER CELL CARCINOMA; LIVER CIRRHOSIS; LIVER DISEASE; LIVER INJURY; LIVER TRANSPLANTATION; PATHOGENESIS; PRIORITY JOURNAL; REVIEW; SITE DIRECTED MUTAGENESIS;

EID: 0030922043     PISSN: 08159319     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1440-1746.1997.tb00451.x     Document Type: Review
Times cited : (42)

References (99)
  • 1
    • 0027741886 scopus 로고
    • Liver disease in α1-antitrypsin deficiency
    • Ockner RK, Boyer J, eds. Philadelphia: WB Saunders
    • Perlmutter DH. Liver disease in α1-antitrypsin deficiency. In: Ockner RK, Boyer J, eds. Progress in Liver Disease, vol. IX. Philadelphia: WB Saunders, 1993; 139-65.
    • (1993) Progress in Liver Disease , vol.9 , pp. 139-165
    • Perlmutter, D.H.1
  • 2
    • 0002177969 scopus 로고
    • Alpha-1-antitrypsin deficiency
    • Scriver CR, Beaudet AL, Sly WS, Valle D, eds. New York: McGraw-Hill Inc.
    • Wilson E, Cox D. Alpha-1-antitrypsin deficiency. In: Scriver CR, Beaudet AL, Sly WS, Valle D, eds. The Metabolic Basis of Inherited Disease. New York: McGraw-Hill Inc., 1989; 2409-37.
    • (1989) The Metabolic Basis of Inherited Disease , pp. 2409-2437
    • Wilson, E.1    Cox, D.2
  • 4
    • 0017163949 scopus 로고
    • 1-antitrypsin PiZ
    • 1-antitrypsin PiZ. FEBS Lett. 1976; 65: 195-7.
    • (1976) FEBS Lett. , vol.65 , pp. 195-197
    • Jeppsson, J.-O.1
  • 5
    • 0017736773 scopus 로고
    • Alpha-1-antitrypsin: Sequence of the Z variant tryptic peptide
    • Owen MC, Carrell RW. Alpha-1-antitrypsin: Sequence of the Z variant tryptic peptide. FEBS Lett. 1976; 79: 247-9.
    • (1976) FEBS Lett. , vol.79 , pp. 247-249
    • Owen, M.C.1    Carrell, R.W.2
  • 7
    • 0020576225 scopus 로고
    • Alpha-1-antitrypsin deficiency detection by analysis of mutation of the gene
    • Kidd VJ, Wallace RB, Itakura K, Woo SLC. Alpha-1-antitrypsin deficiency detection by analysis of mutation of the gene. Nature 1983; 304: 230-4.
    • (1983) Nature , vol.304 , pp. 230-234
    • Kidd, V.J.1    Wallace, R.B.2    Itakura, K.3    Woo, S.L.C.4
  • 11
    • 0023664505 scopus 로고
    • 1-antitrypsin does not prevent its synthesis and secretion
    • 1-antitrypsin does not prevent its synthesis and secretion. FEBS Lett. 1987; 216: 79-82.
    • (1987) FEBS Lett. , vol.216 , pp. 79-82
    • Foreman, R.C.1
  • 13
    • 0345691691 scopus 로고
    • Molecular basis for defective secretion of variants having altered potential for salt bridge formation between amino acids 240 and 342
    • McCracken AA, Druse KB, Brown JL. Molecular basis for defective secretion of variants having altered potential for salt bridge formation between amino acids 240 and 342. Mol. Cell Biol. 1989; 9: 1408-14.
    • (1989) Mol. Cell Biol. , vol.9 , pp. 1408-1414
    • McCracken, A.A.1    Druse, K.B.2    Brown, J.L.3
  • 15
    • 0025341287 scopus 로고
    • 1-antitrypsin from Xenopus oocytes
    • 1-antitrypsin from Xenopus oocytes. FEBS Lett. 1990; 268:21-3.
    • (1990) FEBS Lett. , vol.268 , pp. 21-23
    • Wu, Y.1    Foreman, R.C.2
  • 17
    • 0022852281 scopus 로고
    • 1-Antitrypsin: Molecular pathology, leukocytes and tissue damage
    • 1-Antitrypsin: Molecular pathology, leukocytes and tissue damage. J. Clin. Invest. 1986; 77: 1427-31.
    • (1986) J. Clin. Invest. , vol.77 , pp. 1427-1431
    • Carrell, R.W.1
  • 21
    • 0028053044 scopus 로고
    • 1-antitrypsin transgenic mice: Histopathological and DNA ploidy studies
    • 1-antitrypsin transgenic mice: Histopathological and DNA ploidy studies. Hepatology 1994; 19: 389-97.
    • (1994) Hepatology , vol.19 , pp. 389-397
    • Geller, S.A.1    Nichols, W.S.2    Kim, S.S.3
  • 25
    • 0029788023 scopus 로고    scopus 로고
    • 1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity
    • 1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity. J. Biol. Chem. 1996; 271: 22 791-5.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22791-22795
    • Qu, D.1    Teckman, T.H.2    Omura, S.3    Perlmutter, D.H.4
  • 28
    • 0014530551 scopus 로고
    • Cirrhosis associated with alpha-1-antitrypsin deficiency: A previously unrecognized inherited disorder
    • Sharp HL, Bridges RA, Krivit W, Freier EF. Cirrhosis associated with alpha-1-antitrypsin deficiency: A previously unrecognized inherited disorder. J. Lab. Clin. Med. 1969; 73: 934-9.
    • (1969) J. Lab. Clin. Med. , vol.73 , pp. 934-939
    • Sharp, H.L.1    Bridges, R.A.2    Krivit, W.3    Freier, E.F.4
  • 30
    • 0017099344 scopus 로고
    • 1-antitrypsin deficiency detected by screening of 200 000 infants
    • 1-antitrypsin deficiency detected by screening of 200 000 infants. N. Engl. J. Med. 1976; 294: 1216-21.
    • (1976) N. Engl. J. Med. , vol.294 , pp. 1216-1221
    • Sveger, T.1
  • 32
    • 0021809753 scopus 로고
    • 1-antitrypsin deficiency identified by a PiZ-specific monoclonal antibody
    • 1-antitrypsin deficiency identified by a PiZ-specific monoclonal antibody. Scand. J. Gastroenterol. 1985; 20: 835-42.
    • (1985) Scand. J. Gastroenterol. , vol.20 , pp. 835-842
    • Carlson, J.1    Eriksson, S.2
  • 33
    • 0020517872 scopus 로고
    • Alpha-1-antitrypsin MZ phenotype and cryptogenic chronic liver disease in adults
    • Vecchio FM, Fabiano A, Orsini G, Ragusa D, Massi G. Alpha-1-antitrypsin MZ phenotype and cryptogenic chronic liver disease in adults. Digestion 1983; 27: 100-4.
    • (1983) Digestion , vol.27 , pp. 100-104
    • Vecchio, F.M.1    Fabiano, A.2    Orsini, G.3    Ragusa, D.4    Massi, G.5
  • 35
    • 0028021952 scopus 로고
    • Formation and intracellular localization of hepatitis C virus envelope glycoprotein complexes expressed by recombinant vaccinia and sindbis viruses
    • Dubuisson J, Hsu HH, Cheung RC, Greenberg HB, Russell DG, Rice CM. Formation and intracellular localization of hepatitis C virus envelope glycoprotein complexes expressed by recombinant vaccinia and sindbis viruses. J. Virol. 1994; 68: 6147-60.
    • (1994) J. Virol. , vol.68 , pp. 6147-6160
    • Dubuisson, J.1    Hsu, H.H.2    Cheung, R.C.3    Greenberg, H.B.4    Russell, D.G.5    Rice, C.M.6
  • 36
    • 0030030042 scopus 로고    scopus 로고
    • Hepatitis C virus glycoprotein folding: Disulfide bond formation and association with calnexin
    • Dubussion J, Rice CM. Hepatitis C virus glycoprotein folding: Disulfide bond formation and association with calnexin. J. Virol. 1996; 70: 778-86.
    • (1996) J. Virol. , vol.70 , pp. 778-786
    • Dubussion, J.1    Rice, C.M.2
  • 40
    • 8244231847 scopus 로고
    • Hepatitis and cholestasis in infancy: Intra-hepatic disorders
    • Mowat AP ed. London: Butterworths
    • Mowat AP. Hepatitis and cholestasis in infancy: Intra-hepatic disorders. In: Mowat AP ed. Liver Disorder in Childhood. London: Butterworths, 1992; 43-58.
    • (1992) Liver Disorder in Childhood , pp. 43-58
    • Mowat, A.P.1
  • 41
    • 0020596835 scopus 로고
    • Alpha-1-antitrypsin liver disease: Differential diagnosis of PAS-positive diastase-resistant globules in liver cells
    • Qizibash A, Yong-Pong O. Alpha-1-antitrypsin liver disease: Differential diagnosis of PAS-positive diastase-resistant globules in liver cells. Am. J. Clin. Pathol. 1983; 79: 697-702.
    • (1983) Am. J. Clin. Pathol. , vol.79 , pp. 697-702
    • Qizibash, A.1    Yong-Pong, O.2
  • 42
    • 0028031801 scopus 로고
    • Liver transplantation for end-stage liver disease associated with alpha-1-antitrypsin deficiency in children: Pretransplant natural history, timing and results of transplantation
    • Filipponi F, Soubrane O, Labrousse F et al. Liver transplantation for end-stage liver disease associated with alpha-1-antitrypsin deficiency in children: Pretransplant natural history, timing and results of transplantation. J. Hepatol. 1994; 20: 72-8.
    • (1994) J. Hepatol. , vol.20 , pp. 72-78
    • Filipponi, F.1    Soubrane, O.2    Labrousse, F.3
  • 43
    • 0028658386 scopus 로고
    • Liver transplantation for neonatal hepatitis as compared to the other two leading indications for liver transplantation in children
    • Casavilla FA, Reyes J, Tzakis A et al. Liver transplantation for neonatal hepatitis as compared to the other two leading indications for liver transplantation in children. J. Hepatol. 1994; 21: 1035-9.
    • (1994) J. Hepatol. , vol.21 , pp. 1035-1039
    • Casavilla, F.A.1    Reyes, J.2    Tzakis, A.3
  • 46
    • 0028825747 scopus 로고
    • Gene therapy for cystic fibrosis: Challenges and future directions
    • Wilson JM. Gene therapy for cystic fibrosis: Challenges and future directions. J. Clin. Invest. 1995; 96: 2547-54.
    • (1995) J. Clin. Invest. , vol.96 , pp. 2547-2554
    • Wilson, J.M.1
  • 47
    • 0030563195 scopus 로고    scopus 로고
    • Molecular medicine: Adenoviruses as gene-delivery vehicles
    • Wilson JM. Molecular medicine: Adenoviruses as gene-delivery vehicles. N. Engl. J. Med. 1996; 335: 1185-7.
    • (1996) N. Engl. J. Med. , vol.335 , pp. 1185-1187
    • Wilson, J.M.1
  • 48
    • 0029996147 scopus 로고    scopus 로고
    • In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector
    • Naldini L, Blomer U, Gallay P et al. In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector. Science 1996; 272: 263-7.
    • (1996) Science , vol.272 , pp. 263-267
    • Naldini, L.1    Blomer, U.2    Gallay, P.3
  • 49
    • 0028170231 scopus 로고
    • Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
    • Melnick J, Dul JL, Argon Y. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature 1994; 370: 373-5.
    • (1994) Nature , vol.370 , pp. 373-375
    • Melnick, J.1    Dul, J.L.2    Argon, Y.3
  • 50
    • 0028186873 scopus 로고
    • Antisense catalytic RNAs as therapeutic agents
    • Castanotto D, Rossi JJ, Sarver N. Antisense catalytic RNAs as therapeutic agents. Adv. Pharmacol. 1994; 25: 289-317.
    • (1994) Adv. Pharmacol. , vol.25 , pp. 289-317
    • Castanotto, D.1    Rossi, J.J.2    Sarver, N.3
  • 51
    • 0030051756 scopus 로고    scopus 로고
    • Molecular medicine: Antisense-oligonucleotide therapy
    • Askari FK, McDonnell WM. Molecular medicine: Antisense-oligonucleotide therapy. N. Engl. J. Med. 1996; 334: 316-18.
    • (1996) N. Engl. J. Med. , vol.334 , pp. 316-318
    • Askari, F.K.1    McDonnell, W.M.2
  • 52
    • 0028933117 scopus 로고
    • Conceptual advances in the pathogenesis and treatment of childhood metabolic liver disease
    • Teckman JH, Perlmutter DH. Conceptual advances in the pathogenesis and treatment of childhood metabolic liver disease. Gastroenterology 1995; 108: 1263-79.
    • (1995) Gastroenterology , vol.108 , pp. 1263-1279
    • Teckman, J.H.1    Perlmutter, D.H.2
  • 55
    • 0005937986 scopus 로고
    • 1-antitrypsin for structure and function of serpins
    • 1-antitrypsin for structure and function of serpins. Biochemistry 1990; 117: 48-53.
    • (1990) Biochemistry , vol.117 , pp. 48-53
    • Huber, R.1    Carrell, R.W.2
  • 57
    • 0029012309 scopus 로고
    • 52deleted) forms loop-sheet polymers in vivo: Evidence for the C-sheet mechanism of polymerization
    • 52deleted) forms loop-sheet polymers in vivo: Evidence for the C-sheet mechanism of polymerization. J. Biol. Chem. 1995; 270: 16 864-74.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16864-16874
    • Lomas, D.A.1    Elliott, P.R.2    Sidhar, S.K.3
  • 59
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • Hurtley SM, Helenius A. Protein oligomerization in the endoplasmic reticulum. Annu. Rev. Cell Biol. 1989; 5: 277-307.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 60
    • 0028906029 scopus 로고
    • Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment
    • Tatu U, Hammond C, Helenius A. Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment. EMBO J. 1995; 7: 1340-8.
    • (1995) EMBO J. , vol.7 , pp. 1340-1348
    • Tatu, U.1    Hammond, C.2    Helenius, A.3
  • 61
    • 0028908402 scopus 로고
    • 1-antitrypsin suppresses the folding defect of the Z-type variant
    • 1-antitrypsin suppresses the folding defect of the Z-type variant. J. Biol. Chem. 1995; 270: 8597-601.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8597-8601
    • Kim, J.1    Lee, K.N.2    Yi, G.-S.3    Yu, M.-H.4
  • 63
    • 0028855465 scopus 로고
    • COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization
    • Eldering E, Verpy E, Roem D, Meo T, Tosi M. COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization. J. Biol. Chem. 1995; 270: 2579-87.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2579-2587
    • Eldering, E.1    Verpy, E.2    Roem, D.3    Meo, T.4    Tosi, M.5
  • 64
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman JE, Wieland FT. Protein sorting by transport vesicles. Science 1996; 272: 227-34.
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 65
    • 0029558526 scopus 로고
    • COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast
    • Bednarek SY, Ravazzola M, Hosobuchi M et al. COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast. Cell 1995; 83: 1183-96.
    • (1995) Cell , vol.83 , pp. 1183-1196
    • Bednarek, S.Y.1    Ravazzola, M.2    Hosobuchi, M.3
  • 66
    • 0028964475 scopus 로고
    • The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected protein to the Golgi
    • Schimmoller F, Singer-Kruger B, Schroder S, Kruger U, Barlowe C, Reizman H. The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected protein to the Golgi. EMBO J. 1995; 14: 1329-39.
    • (1995) EMBO J. , vol.14 , pp. 1329-1339
    • Schimmoller, F.1    Singer-Kruger, B.2    Schroder, S.3    Kruger, U.4    Barlowe, C.5    Reizman, H.6
  • 67
    • 0029147574 scopus 로고
    • An integral membrane component of coatomer-coated transport vesicles defines a family of proteins involved in budding
    • Stamnes MA, Craighead MW, Hoe MH et al. An integral membrane component of coatomer-coated transport vesicles defines a family of proteins involved in budding. Proc. Natl Acad. Sci. USA 1995; 92: 8011-15.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8011-8015
    • Stamnes, M.A.1    Craighead, M.W.2    Hoe, M.H.3
  • 68
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething M-J, Sambrook J. Protein folding in the cell. Nature 1992; 355: 34-45.
    • (1992) Nature , vol.355 , pp. 34-45
    • Gething, M.-J.1    Sambrook, J.2
  • 70
    • 0027936075 scopus 로고
    • Several endoplasmic reticulum stress proteins, including ERp72, interact with thyroglobulin during its maturation
    • Kuznetsov G, Chen LB, Nigam SK. Several endoplasmic reticulum stress proteins, including ERp72, interact with thyroglobulin during its maturation. J. Biol. Chem. 1994; 269: 22 990-5.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22990-22995
    • Kuznetsov, G.1    Chen, L.B.2    Nigam, S.K.3
  • 71
    • 0026022577 scopus 로고
    • Participation of a novel 88 kDa protein in the biogenesis of murine class histocompatibility molecules
    • Degen W, Williams DB. Participation of a novel 88 kDa protein in the biogenesis of murine class histocompatibility molecules. J. Cell Biol. 1991; 112: 1099-115.
    • (1991) J. Cell Biol. , vol.112 , pp. 1099-1115
    • Degen, W.1    Williams, D.B.2
  • 72
    • 0026511275 scopus 로고
    • Endoplasmic reticulum resident protein of 90 kilodaltons associates with T- and B-cell antigen receptors and major histocompatibility complex antigens during their assembly
    • Hochstenbach F, David V, Watkins J, Brenner MB. Endoplasmic reticulum resident protein of 90 kilodaltons associates with T- and B-cell antigen receptors and major histocompatibility complex antigens during their assembly. Proc. Nad Acad. Sci. USA 1992; 89: 4734-8.
    • (1992) Proc. Nad Acad. Sci. USA , vol.89 , pp. 4734-4738
    • Hochstenbach, F.1    David, V.2    Watkins, J.3    Brenner, M.B.4
  • 73
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou W-J, Cameron PH, Thomas DY, Bergeron JJM. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 1993; 364: 771-6.
    • (1993) Nature , vol.364 , pp. 771-776
    • Ou, W.-J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.M.4
  • 75
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Herbert DN, Foellmer B, Helenius A. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 1995; 81: 425-53.
    • (1995) Cell , vol.81 , pp. 425-453
    • Herbert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 76
    • 0026500202 scopus 로고
    • Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-glucose:glycoprotein glucosyltransferase
    • Sousa MC, Ferrero-Garcia MA, Parodi AJ. Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-glucose:glycoprotein glucosyltransferase. Biochemistry 1992; 31: 97-105.
    • (1992) Biochemistry , vol.31 , pp. 97-105
    • Sousa, M.C.1    Ferrero-Garcia, M.A.2    Parodi, A.J.3
  • 77
    • 0024345717 scopus 로고
    • Pre-Golgi degradation of newly synthesized T-cell antigen receptor chains: Intrinsic sensitivity and the role of subunit assembly
    • Bonifacino JS, Suzuki CK, Lippincott-Schwartz J, Weissman AM, Klausner RD. Pre-Golgi degradation of newly synthesized T-cell antigen receptor chains: Intrinsic sensitivity and the role of subunit assembly. J. Cell Biol. 1989; 109: 73-83.
    • (1989) J. Cell Biol. , vol.109 , pp. 73-83
    • Bonifacino, J.S.1    Suzuki, C.K.2    Lippincott-Schwartz, J.3    Weissman, A.M.4    Klausner, R.D.5
  • 78
    • 0029564918 scopus 로고
    • Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-GoIgi intermediate compartment
    • Raposo G, van Santen HM, Liejendekker R, Geuze HJ, Ploegh HL. Misfolded major histocompatibility complex class I molecules accumulate in an expanded ER-GoIgi intermediate compartment. J. Cell Biol. 1995; 131: 1403-19.
    • (1995) J. Cell Biol. , vol.131 , pp. 1403-1419
    • Raposo, G.1    Van Santen, H.M.2    Liejendekker, R.3    Geuze, H.J.4    Ploegh, H.L.5
  • 79
    • 0026035501 scopus 로고
    • 1-antitrypsin deficiency
    • 1-antitrypsin deficiency. Hepatology 1991; 13: 172-85.
    • (1991) Hepatology , vol.13 , pp. 172-185
    • Perlmutter, D.H.1
  • 80
    • 0017232527 scopus 로고
    • Alpha-1-antitrypsin: Molecular abnormality of S variant
    • Owen MC, Carrell RW. Alpha-1-antitrypsin: Molecular abnormality of S variant. BMJ 1976; 1: 130-1.
    • (1976) BMJ , vol.1 , pp. 130-131
    • Owen, M.C.1    Carrell, R.W.2
  • 81
    • 0025242929 scopus 로고
    • Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
    • Cheng SH, Gregory RJ, Marshall J et al. Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis. Cell 1990; 63: 827-34.
    • (1990) Cell , vol.63 , pp. 827-834
    • Cheng, S.H.1    Gregory, R.J.2    Marshall, J.3
  • 82
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward CL, Omura S, Kopito RR. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 1995; 83: 121-7.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 83
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen TJ, Loo MA, Pind S, Williams DB, Goldberg AL, Riordan JR. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 1995; 83: 129-35.
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 84
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko A, Ciechanover A. The ubiquitin system for protein degradation. Annu. Rev. Biochem. 1992; 61: 761-807.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 85
    • 0028181429 scopus 로고
    • Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90)
    • Jackson MR, Cohen-Doyle MF, Petersen PA, Williams DB. Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90). Science 1994; 263: 384-7.
    • (1994) Science , vol.263 , pp. 384-387
    • Jackson, M.R.1    Cohen-Doyle, M.F.2    Petersen, P.A.3    Williams, D.B.4
  • 87
    • 0027214605 scopus 로고
    • Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes
    • Gaczynska M, Rock KL, Goldberg AL. Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes. Nature 1993; 365: 264-7.
    • (1993) Nature , vol.365 , pp. 264-267
    • Gaczynska, M.1    Rock, K.L.2    Goldberg, A.L.3
  • 88
    • 0024818649 scopus 로고
    • Molecular pathogenesis of hepatocellular carcinoma in hepatitis B virus transgenic mice
    • Chisari FV, Klopchin K, Moriyama T et al. Molecular pathogenesis of hepatocellular carcinoma in hepatitis B virus transgenic mice. Cell 1989; 59: 1145-56.
    • (1989) Cell , vol.59 , pp. 1145-1156
    • Chisari, F.V.1    Klopchin, K.2    Moriyama, T.3
  • 89
    • 0029148749 scopus 로고
    • Hepatitis B virus transgenic mice: Insights into the virus and the disease
    • Chisari FV. Hepatitis B virus transgenic mice: Insights into the virus and the disease. Hepatology 1995; 22: 1317-25.
    • (1995) Hepatology , vol.22 , pp. 1317-1325
    • Chisari, F.V.1
  • 90
    • 0021809277 scopus 로고
    • Human Z alpha-1-antitrypsin accumulates intracellularly and stimulates lysosomal activity when synthesized in the Xenopus oocyte
    • Bathurst IC, Errington DM, Foreman RC, Judah JD, Carrell RW. Human Z alpha-1-antitrypsin accumulates intracellularly and stimulates lysosomal activity when synthesized in the Xenopus oocyte. FEBS Lett. 1985; 183: 304-8.
    • (1985) FEBS Lett. , vol.183 , pp. 304-308
    • Bathurst, I.C.1    Errington, D.M.2    Foreman, R.C.3    Judah, J.D.4    Carrell, R.W.5
  • 91
    • 0025363276 scopus 로고
    • Studies on the mechanism of autophagy: Formation of autophagic vacuole
    • Dunn WA. Studies on the mechanism of autophagy: Formation of autophagic vacuole. J. Cell Biol. 1991; 110: 1923-33.
    • (1991) J. Cell Biol. , vol.110 , pp. 1923-1933
    • Dunn, W.A.1
  • 92
    • 0021271399 scopus 로고
    • Amino acid control of autophagic sequestration and protein degradation in isolated rat hepatocytes
    • Seglen PO, Gordon P. Amino acid control of autophagic sequestration and protein degradation in isolated rat hepatocytes. J. Cell Biol. 1984; 99: 435-44.
    • (1984) J. Cell Biol. , vol.99 , pp. 435-444
    • Seglen, P.O.1    Gordon, P.2
  • 93
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox JS, Shamu CE, Walter P. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 1994; 73: 1197-206.
    • (1994) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 94
    • 0027305620 scopus 로고
    • A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus
    • Mori K, Ma W, Gething M-J, Sambrook J. A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell 1993; 74: 743-56.
    • (1993) Cell , vol.74 , pp. 743-756
    • Mori, K.1    Ma, W.2    Gething, M.-J.3    Sambrook, J.4
  • 95
    • 0029130373 scopus 로고
    • Inhibition of adipogenesis by the stress-induced protein CHOP (gadd153)
    • Batchvarova N, Wang X-Z, Ron D. Inhibition of adipogenesis by the stress-induced protein CHOP (gadd153). EMBO J. 1995; 14: 4654-61.
    • (1995) EMBO J. , vol.14 , pp. 4654-4661
    • Batchvarova, N.1    Wang, X.-Z.2    Ron, D.3
  • 96
    • 0030053047 scopus 로고    scopus 로고
    • Activation of transcription factor NF-κB by the adenovirus E3/19K protein requires its ER retention
    • Pahl HL, Sester M, Gurgert H-G, Baeuerle PA. Activation of transcription factor NF-κB by the adenovirus E3/19K protein requires its ER retention. J. Cell Biol. 1996; 132: 511-22.
    • (1996) J. Cell Biol. , vol.132 , pp. 511-522
    • Pahl, H.L.1    Sester, M.2    Gurgert, H.-G.3    Baeuerle, P.A.4
  • 98
    • 0016840757 scopus 로고
    • Induced thermal resistance in HeLa cells
    • Gerner EW, Schneider MJ. Induced thermal resistance in HeLa cells. Nature 1975; 256: 500-3.
    • (1975) Nature , vol.256 , pp. 500-503
    • Gerner, E.W.1    Schneider, M.J.2
  • 99
    • 0025936528 scopus 로고
    • Mobile reactive centre of serpins and the control of thrombosis
    • Carrell RW, Evans DL, Stein DE. Mobile reactive centre of serpins and the control of thrombosis. Nature 1991; 353: 576.
    • (1991) Nature , vol.353 , pp. 576
    • Carrell, R.W.1    Evans, D.L.2    Stein, D.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.