Defective protein folding as a cause of disease

A defined, spontaneous protein folding defect can act as a common link between lung and liver diseases associated with the Z type of plasma α1-antitrypsin deficiency.

[1]  P. Stein,et al.  What do dysfunctional serpins tell us about molecular mobility and disease? , 1995, Nature Structural Biology.

[2]  R. Crystal,et al.  Antielastases of the human alveolar structures. Implications for the protease-antiprotease theory of emphysema. , 1981, The Journal of clinical investigation.

[3]  J. Potempa,et al.  The serpin superfamily of proteinase inhibitors: structure, function, and regulation. , 1994, The Journal of biological chemistry.

[4]  J. Jeppsson.  Amino acid substitution Glu→Lys in α1‐antitrypsin PiZ , 1976 .

[5]  P. Pedersen,et al.  Altered protein folding may be the molecular basis of most cases of cystic fibrosis , 1992, FEBS letters.

[6]  A. Le,et al.  Accumulation of the insoluble PiZ variant of human alpha 1-antitrypsin within the hepatic endoplasmic reticulum does not elevate the steady-state level of grp78/BiP. , 1990, The Journal of biological chemistry.

[7]  G. Salvesen,et al.  Human plasma proteinase inhibitors. , 1983, Annual review of biochemistry.

[8]  R. Huber,et al.  Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. , 1984, Journal of molecular biology.

[9]  D. Lomas,et al.  Effect of the Z mutation on the physical and inhibitory properties of alpha 1-antitrypsin. , 1993, Biochemistry.

[10]  T. Sveger.  The Natural History of Liver Disease in (α1‐Antitrypsin Deficient Children , 1988 .

[11]  Cliff,et al.  Accumulation of PiZ alpha 1-antitrypsin causes liver damage in transgenic mice. , 1989, The Journal of clinical investigation.

[12]  F. DeMayo,et al.  Tissue specific expression of the human alpha-1-antitrypsin gene in transgenic mice. , 1987, Nucleic acids research.

[13]  D. Johnson,et al.  Structural evidence for methionine at the reactive site of human alpha-1-proteinase inhibitor. , 1978, The Journal of biological chemistry.

[14]  D. Lomas,et al.  The mechanism of Z α1-antitrypsin accumulation in the liver , 1993, Nature.

[15]  J. Sambrook,et al.  Protein folding in the cell , 1992, Nature.

[16]  M. Finegold,et al.  Alpha-1-antitrypsin deficiency: accumulation or degradation of mutant variants within the hepatic endoplasmic reticulum. , 1989, American journal of respiratory cell and molecular biology.

[17]  Myeong-Hee Yu,et al.  The Z type variation of human α1-antitrypsin causes a protein folding defect , 1995, Nature Structural Biology.

[18]  K. E. Moore,et al.  A lag in intracellular degradation of mutant alpha 1-antitrypsin correlates with the liver disease phenotype in homozygous PiZZ alpha 1-antitrypsin deficiency. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[19]  R. Crystal,et al.  Molecular basis of alpha-1-antitrypsin deficiency. , 1988, The American journal of medicine.

[20]  A. Le,et al.  Intracellular degradation of the transport-impaired human PiZ alpha 1-antitrypsin variant. Biochemical mapping of the degradative event among compartments of the secretory pathway. , 1990, The Journal of biological chemistry.

[21]  A. Helenius,et al.  Protein oligomerization in the endoplasmic reticulum. , 1989, Annual review of cell biology.

[22]  W. Bode,et al.  Structural aspects of serpin inhibition , 1994, FEBS letters.

[23]  P. H. Cameron,et al.  Association of folding intermediates of glycoproteins with calnexin during protein maturation , 1993, Nature.

[24]  A. Le,et al.  Association between calnexin and a secretion-incompetent variant of human alpha 1-antitrypsin. , 1994, The Journal of biological chemistry.

[25]  A. Leslie,et al.  Crystal structure of ovalbumin as a model for the reactive centre of serpins , 1990, Nature.

[26]  R. Carrell,et al.  Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins. , 1989, Biochemistry.