메뉴 건너뛰기




Volumn 121, Issue 4, 1997, Pages 787-797

Linear polymerization caused by the defective folding of a non-inhibitory serpin ovalbumin

Author keywords

BiP; Defective folding; Linear polymerization; Ovalbumin; Serpin superfamily

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ANION; CYSTEINE; EPITOPE; IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY; OVALBUMIN; SERINE PROTEINASE INHIBITOR; SODIUM CHLORIDE; TRYPSIN INHIBITOR;

EID: 0030947918     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021654     Document Type: Article
Times cited : (26)

References (49)
  • 1
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P.S. and Baldwin, K.L. (1990) Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59, 631-660
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, K.L.2
  • 2
    • 0027313673 scopus 로고
    • Pathways of protein folding
    • Matthews, C.R. (1993) Pathways of protein folding. Annu. Rev. Biochem. 62, 653-683
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 653-683
    • Matthews, C.R.1
  • 3
    • 0029117494 scopus 로고
    • Finding the right fold
    • Dobson, C.M. (1995) finding the right fold. Nature Struct, Biol. 2, 513-517
    • (1995) Nature Struct, Biol. , vol.2 , pp. 513-517
    • Dobson, C.M.1
  • 4
    • 0029589824 scopus 로고
    • What do dysfunctional serpins tell us about molecular mobility and disease?
    • Stein, P.K. and Carrell, R.W. (1995) What do dysfunctional serpins tell us about molecular mobility and disease? Nature Struct. Biol. 2, 96-113
    • (1995) Nature Struct. Biol. , vol.2 , pp. 96-113
    • Stein, P.K.1    Carrell, R.W.2
  • 5
    • 0020643467 scopus 로고
    • Human plasma proteinase inhibitors
    • Travis, J. and Salvosen, G.S. (1983) Human plasma proteinase inhibitors. Annu. Rev. Biochem. 52, 655-709
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 655-709
    • Travis, J.1    Salvosen, G.S.2
  • 7
    • 0019453831 scopus 로고
    • Antielastases of the human alveolar structures: Implications for the protease-antiprotease theory of emphysema
    • Gadek, J.K., Fells, G.A., Zimmerman, R.L., Rennard, S.I., and Crystal, R.G. (1981) Antielastases of the human alveolar structures: Implications for the protease-antiprotease theory of emphysema. J. Clin. Invest. 68, 889-898
    • (1981) J. Clin. Invest. , vol.68 , pp. 889-898
    • Gadek, J.K.1    Fells, G.A.2    Zimmerman, R.L.3    Rennard, S.I.4    Crystal, R.G.5
  • 8
    • 84907041622 scopus 로고
    • The electrophoretic α-globulin pattern of serum in α-antitrypsin deficiency
    • Laurell, C.H. and Eriksson, S. (1963) The electrophoretic α-globulin pattern of serum in α-antitrypsin deficiency. Scand. J. Clin. Lab. Invest. 15, 132-140
    • (1963) Scand. J. Clin. Lab. Invest. , vol.15 , pp. 132-140
    • Laurell, C.H.1    Eriksson, S.2
  • 10
    • 0023898432 scopus 로고
    • Molecular basis of alpha-1-antitrypsin deficiency
    • Brantly, M., Nukiwa, Y., and Crystal, R.G. (1988) Molecular basis of alpha-1-antitrypsin deficiency. Am. J. Med. 84, 13-31
    • (1988) Am. J. Med. , vol.84 , pp. 13-31
    • Brantly, M.1    Nukiwa, Y.2    Crystal, R.G.3
  • 11
    • 0024842004 scopus 로고
    • 1 antitrypsin gene and its deficiency states
    • 1 antitrypsin gene and its deficiency states. Trends Genet. 5, 411-417
    • (1989) Trends Genet. , vol.5 , pp. 411-417
    • Crystal, R.G.1
  • 12
    • 0024763969 scopus 로고
    • Alpha-1-antitrypsin deficiency: Accumulation or degradation of mutant variants within the hepatic endoplasmic reticulum
    • Sifers, R.N., Finegold, M.J., and Woo, S.L.C. (1989) Alpha-1-antitrypsin deficiency: Accumulation or degradation of mutant variants within the hepatic endoplasmic reticulum. Am. J. Respir. Cell Mol. Biol. 1, 341-345
    • (1989) Am. J. Respir. Cell Mol. Biol. , vol.1 , pp. 341-345
    • Sifers, R.N.1    Finegold, M.J.2    Woo, S.L.C.3
  • 13
    • 0029048542 scopus 로고    scopus 로고
    • The Z type variation of human α -antitrypsin causes a protein folding defect
    • Yu, M.-H., Leu, K.N., and Kim, J. (1996) The Z type variation of human α -antitrypsin causes a protein folding defect. Nature Struct. Biol. 2, 363-367
    • (1996) Nature Struct. Biol. , vol.2 , pp. 363-367
    • Yu, M.-H.1    Leu, K.N.2    Kim, J.3
  • 14
    • 0029011597 scopus 로고
    • Defective protein folding as a cause of disease
    • Sifers, R.N. (1995) Defective protein folding as a cause of disease. Nature Struct. Biol. 2, 355-357
    • (1995) Nature Struct. Biol. , vol.2 , pp. 355-357
    • Sifers, R.N.1
  • 16
    • 0026625802 scopus 로고
    • Protein transport. Z and the insoluble water
    • Sifers, R.N. (1992) Protein transport. Z and the insoluble water. Nature 357, 541-542
    • (1992) Nature , vol.357 , pp. 541-542
    • Sifers, R.N.1
  • 19
    • 0024423930 scopus 로고
    • 1-antitrypsin for structure and function of serpins
    • 1-antitrypsin for structure and function of serpins. Biochemistry 28, 8951-8966
    • (1989) Biochemistry , vol.28 , pp. 8951-8966
    • Huber, R.1    Carrell, R.W.2
  • 20
  • 21
    • 0023508036 scopus 로고
    • Trypsin-inhibitory activity of ovalbumin preparations is due to ovomucoid
    • Odum, I., (1987) Trypsin-inhibitory activity of ovalbumin preparations is due to ovomucoid. Biol. Chem. Hoppe-Seyler Ovalbumm, 1603-1606
    • (1987) Biol. Chem. Hoppe-Seyler Ovalbumm , pp. 1603-1606
    • Odum, I.1
  • 22
    • 0021711639 scopus 로고
    • Ovalbumin is an elastase substrate
    • Wright, H.T. (1984) Ovalbumin is an elastase substrate. J. Biol. Chem. 259, 14335-143336
    • (1984) J. Biol. Chem. , vol.259 , pp. 14335-143336
    • Wright, H.T.1
  • 23
    • 0025949027 scopus 로고
    • Crystal structure of uncleaced ovalbumin at 1.90 A resolution
    • Stein, P.E., Leslie, A.G., Finch, J.T., and Carrell, R.W. (1991) Crystal structure of uncleaced ovalbumin at 1.90 A resolution. J. Mol. Biol. 221, 941-959
    • (1991) J. Mol. Biol. , vol.221 , pp. 941-959
    • Stein, P.E.1    Leslie, A.G.2    Finch, J.T.3    Carrell, R.W.4
  • 24
    • 0027968024 scopus 로고
    • Denstused state of ovalbumin in high concentrations of urea us evaluated by disulfide rearrangement analysis
    • Tatsumi, E., Takahashi, N., and Hirose, M. (1994) Denstused state of ovalbumin in high concentrations of urea us evaluated by disulfide rearrangement analysis. J. Biol. Chem. 269, 28062-28067
    • (1994) J. Biol. Chem. , vol.269 , pp. 28062-28067
    • Tatsumi, E.1    Takahashi, N.2    Hirose, M.3
  • 25
    • 0026736742 scopus 로고
    • Reversible denaturatics of disulfide-rcduced ovalbumin and its reoxidation generating the native cystine cross-link
    • Takahashi, N. and Hirose, M. (1992) Reversible denaturatics of disulfide-rcduced ovalbumin and its reoxidation generating the native cystine cross-link. J. Biol. Chem. 267, 11565-11572
    • (1992) J. Biol. Chem. , vol.267 , pp. 11565-11572
    • Takahashi, N.1    Hirose, M.2
  • 26
    • 0001731813 scopus 로고
    • Irreveesible thermal denaturation and formation of linear aggregates of ovalbumin
    • Koseki, T., Kitabatake, N., and Doi, E. (1989) Irreveesible thermal denaturation and formation of linear aggregates of ovalbumin. Food Hydrocolloids 3, 123-134
    • (1989) Food Hydrocolloids , vol.3 , pp. 123-134
    • Koseki, T.1    Kitabatake, N.2    Doi, E.3
  • 27
    • 33751154874 scopus 로고
    • Molten globule state of protein molecules in induced transparent food gels
    • Tani, F., Murata, M., Higasa, T., Goto, M., Kitabatake, N., and Doi, E. (1995) Molten globule state of protein molecules in induced transparent food gels. J. Agric. Food Chem. 43, 2326-2331
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 2326-2331
    • Tani, F.1    Murata, M.2    Higasa, T.3    Goto, M.4    Kitabatake, N.5    Doi, E.6
  • 28
    • 0042852414 scopus 로고
    • Studies on proteins, I. on the preparation of egg-albumin solutions of well-defined composition, and on the analytical methods used
    • Sörensen, S.P.L. and Höyrup, M. (1915) Studies on proteins, I. On the preparation of egg-albumin solutions of well-defined composition, and on the analytical methods used. Compt. Trav. Lab. Carlsberg 12, 12-67
    • (1915) Compt. Trav. Lab. Carlsberg , vol.12 , pp. 12-67
    • Sörensen, S.P.L.1    Höyrup, M.2
  • 29
    • 0022462428 scopus 로고
    • As ancient developmental induction: Heat shock proteins induced is sporulation and oogenesis
    • Kurtz, S., Rossi, J., Petko, L., and Lindquist, S. (1986) As ancient developmental induction: Heat shock proteins induced is sporulation and oogenesis. Science 231, 1154-1157
    • (1986) Science , vol.231 , pp. 1154-1157
    • Kurtz, S.1    Rossi, J.2    Petko, L.3    Lindquist, S.4
  • 30
    • 0024393778 scopus 로고
    • Peptide binding and release by proteins implicated as catalysts of assembly
    • Flynn, G.C., Chappell, T.G., and Rothman, J.E. (1989) Peptide binding and release by proteins implicated as catalysts of assembly. Science 245, 385-390
    • (1989) Science , vol.245 , pp. 385-390
    • Flynn, G.C.1    Chappell, T.G.2    Rothman, J.E.3
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 32
    • 0024609909 scopus 로고
    • Microsequence analysis of winged bean and proteins electroblotted from two-dimensional gel
    • Hirano, H. (1989) Microsequence analysis of winged bean and proteins electroblotted from two-dimensional gel. J. P Chem. 8, 115-130
    • (1989) J. P Chem. , vol.8 , pp. 115-130
    • Hirano, H.1
  • 33
    • 0018963435 scopus 로고
    • A prepriming DNA reption enzyme of Escherichia coli. 1. Purification of protein sequence-specific, DNA-dependent ATPase
    • Shlomai, J. and Kornberg, A. (1980) A prepriming DNA reption enzyme of Escherichia coli. 1. Purification of protein sequence-specific, DNA-dependent ATPase. J. Biol. Chem. 6789-6793
    • (1980) J. Biol. Chem. , pp. 6789-6793
    • Shlomai, J.1    Kornberg, A.2
  • 35
    • 0025944815 scopus 로고
    • Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors
    • Johnsson, B., Löfas, S., and Lindquist, G. (1991) Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors. Anal. Biochem. 198, 268-277
    • (1991) Anal. Biochem. , vol.198 , pp. 268-277
    • Johnsson, B.1    Löfas, S.2    Lindquist, G.3
  • 36
    • 34247513828 scopus 로고
    • Zur lehre von der wirkung der salze. Zweite mittheilung
    • Hofmeister, F. (1888) Zur lehre von der wirkung der salze. Zweite mittheilung. Arch. Exptl. Pathol. Pharmakol. 24. 247-260
    • (1888) Arch. Exptl. Pathol. Pharmakol. , vol.24 , pp. 247-260
    • Hofmeister, F.1
  • 37
    • 33745503743 scopus 로고
    • Ion effects on the solution structure of biological macromolecules
    • von Hippel, P.H. and Schleich, T. (1969) Ion effects on the solution structure of biological macromolecules. Acc. Chem. Res. 2, 257-265
    • (1969) Acc. Chem. Res. , vol.2 , pp. 257-265
    • Von Hippel, P.H.1    Schleich, T.2
  • 38
    • 0014499213 scopus 로고
    • Solubilization of particulate proteins and nonelectrolytes by chaotropic agents
    • Hatefi, Y. and Hanstein. W.G. (1969) Solubilization of particulate proteins and nonelectrolytes by chaotropic agents. Proc. Natl. Acad. Sci. USA 62, 1129-1136
    • (1969) Proc. Natl. Acad. Sci. USA , vol.62 , pp. 1129-1136
    • Hatefi, Y.1    Hanstein, W.G.2
  • 39
    • 0013807126 scopus 로고
    • On the conformational stability of globular proteins: The effects of various electrolytes and nonelectrolytes on the thermal ribonuclease transition
    • von Hippel. P.H. and Wong, K.Y. (1965) On the conformational stability of globular proteins: The effects of various electrolytes and nonelectrolytes on the thermal ribonuclease transition. J. Biol. Chem. 240, 3909-3923
    • (1965) J. Biol. Chem. , vol.240 , pp. 3909-3923
    • Von Hippel, P.H.1    Wong, K.Y.2
  • 40
    • 0025877774 scopus 로고
    • The Hofmeister series and ionic strength
    • Leberman, R. (1991) The Hofmeister series and ionic strength. FEBS Lett. 284, 293-294
    • (1991) FEBS Lett. , vol.284 , pp. 293-294
    • Leberman, R.1
  • 41
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • Flynn, G.C., Pohl, J., Flocco, M.T., and Rothman, J.E. (1991) Peptide-binding specificity of the molecular chaperone BiP. Nature 353, 726-730
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 42
    • 0027484417 scopus 로고
    • Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP
    • Blond-Elguindi, S., Cwirla, S.E., Dawer, W.J., Lipshutz, R.J., Sprang, S.R., Sambrook, J., and Gething, M.J.H. (1993) Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 75, 717-728
    • (1993) Cell , vol.75 , pp. 717-728
    • Blond-Elguindi, S.1    Cwirla, S.E.2    Dawer, W.J.3    Lipshutz, R.J.4    Sprang, S.R.5    Sambrook, J.6    Gething, M.J.H.7
  • 43
    • 0021747157 scopus 로고
    • 1-proteinase inhibitor: Crystal structure analysis of two crystal modifications. molecular model and preliminary analysis of the implications for function
    • 1-proteinase inhibitor: crystal structure analysis of two crystal modifications. molecular model and preliminary analysis of the implications for function. J. Mol. Biol. 177, 531-556
    • (1984) J. Mol. Biol. , vol.177 , pp. 531-556
    • Loebermann, H.1    Tokuoka, R.2    Deisenhofer, J.3    Huber, R.4
  • 46
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R.F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 48
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 49
    • 0028057108 scopus 로고
    • Raster3D version 2.0. A program for photorealistic molecular graphies
    • Merritt, E.A. and Murphy, E.P. (1994) Raster3D version 2.0. A program for photorealistic molecular graphies. Acta. Crystallog. sect. D 50, 869-873
    • (1994) Acta. Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.