Global suppression of protein folding defects and inclusion body formation.
暂无分享,去创建一个
B Fane | J. King | J. Sturtevant | A. Mitraki | B. Fane | C Haase-Pettingell | A Mitraki | C. Haase-Pettingell | J Sturtevant | J King
[1] E. W. Kauffman,et al. Characterization of an associated equilibrium folding intermediate of bovine growth hormone. , 1986, Biochemistry.
[2] R. Larossa,et al. Demonstration by genetic suppression of interaction of GroE products with many proteins , 1989, Nature.
[3] P. S. Kim,et al. Intermediates in the folding reactions of small proteins. , 1990, Annual review of biochemistry.
[4] A. Lesk,et al. Determinants of a protein fold. Unique features of the globin amino acid sequences. , 1987, Journal of molecular biology.
[5] J. Sambrook,et al. Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport , 1986, Cell.
[6] J. King,et al. Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein: II. Active mutant proteins matured at 30 °C , 1981 .
[7] Intragenic suppression of a capsid assembly-defective P22 tailspike mutation. , 1990, Genetics.
[8] J. King,et al. Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein: III. Inactive polypeptide chains synthesized at 39 °C , 1981 .
[9] J. King,et al. Conformational stability of P22 tailspike proteins carrying temperature-sensitive folding mutations. , 1990, Biochemistry.
[10] J. King,et al. Formation of aggregates from a thermolabile in vivo folding intermediate in P22 tailspike maturation. A model for inclusion body formation. , 1988, The Journal of biological chemistry.
[11] P. Berget,et al. Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail-spike protein. I. Fine-structure mapping. , 1980, Genetics.
[12] M. Desmadril,et al. Quasi-irreversibility in the unfolding-refolding transition of phosphoglycerate kinase induced by guanidine hydrochloride. , 1987, European journal of biochemistry.
[13] J. King,et al. Secondary structure and thermostability of the phage P22 tailspike. XX. Analysis by Raman spectroscopy of the wild-type protein and a temperature-sensitive folding mutant. , 1988, Journal of molecular biology.
[14] R. Jaenicke,et al. Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation. , 1979, Biochemistry.
[15] J. King,et al. Protein Folding Intermediates and Inclusion Body Formation. , 1989, Bio/Technology.
[16] T. Creighton,et al. Experimental studies of protein folding and unfolding. , 1978, Progress in biophysics and molecular biology.
[17] J. King,et al. Thermostability of temperature-sensitive folding mutants of the P22 tailspike protein. , 1989, The Journal of biological chemistry.
[18] B. Fane,et al. Intragenic suppressors of folding defects in the P22 tailspike protein. , 1991, Genetics.
[19] F. Marston. The purification of eukaryotic polypeptides synthesized in Escherichia coli. , 1986, The Biochemical journal.
[20] P. Berget,et al. Structure and Functions of the Bacteriophage P22 Tail Protein , 1980, Journal of virology.
[21] J. King,et al. Maturation of the tail spike endorhamnosidase of Salmonella phage P22. , 1982, The Journal of biological chemistry.
[22] J. King,et al. Reconstitution of the thermostable trimeric phage P22 tailspike protein from denatured chains in vitro. , 1989, The Journal of biological chemistry.
[23] D. I. Wang,et al. Refolding and aggregation of bovine carbonic anhydrase B: quasi-elastic light scattering analysis. , 1990, Biochemistry.
[24] D. Goldenberg. Genetic studies of protein stability and mechanisms of folding. , 1988, Annual review of biophysics and biophysical chemistry.
[25] T. Alber,et al. Mutational effects on protein stability. , 1989, Annual review of biochemistry.
[26] G. Lorimer,et al. GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli , 1989, Nature.
[27] Peter Walter,et al. Protein translocation across the endoplasmic reticulum , 1984, Cell.
[28] G. N. Ramachandran,et al. Conformation of polypeptides and proteins. , 1968, Advances in protein chemistry.
[29] D. Shortle,et al. Probing the determinants of protein folding and stability with amino acid substitutions. , 1989, The Journal of biological chemistry.
[30] M. Streuli,et al. Isolation and characterization of temperature-sensitive and thermostable mutants of the human receptor-like protein tyrosine phosphatase LAR. , 1991, The Journal of biological chemistry.
[31] Roger W. Hendrix,et al. Homologous plant and bacterial proteins chaperone oligomeric protein assembly , 1988, Nature.
[32] J. Rothman. Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells , 1989, Cell.
[33] J. Richardson,et al. De novo design, expression, and characterization of Felix: a four-helix bundle protein of native-like sequence. , 1990, Science.
[34] R. Sauer,et al. Phage P22 tail protein: gene and amino acid sequence. , 1982, Biochemistry.
[35] W. F. Harrington,et al. Collagen structure in solution. I. Kinetics of helix regeneration in single-chain gelatins. , 1970, Biochemistry.
[36] W. Lim,et al. Deciphering the message in protein sequences: tolerance to amino acid substitutions. , 1990, Science.
[37] L. Gierasch,et al. Reduced tendency to form a beta turn in peptides from the P22 tailspike protein correlates with a temperature-sensitive folding defect. , 1990, Biochemistry.
[38] M. Goldberg,et al. Renaturation of Escherichia coli tryptophanase after exposure to 8 M urea. Evidence for the existence of nucleation centers. , 1974, European journal of biochemistry.
[39] Surface amino acids as sites of temperature-sensitive folding mutations in the P22 tailspike protein. , 1988, The Journal of biological chemistry.
[40] D. Goldenberg,et al. Mutational analysis of a protein-folding pathway , 1989, Nature.
[41] G. A. Bowden,et al. Folding and aggregation of beta-lactamase in the periplasmic space of Escherichia coli. , 1990, The Journal of biological chemistry.
[42] J. King,et al. Nature and distribution of sites of temperature-sensitive folding mutations in the gene for the P22 tailspike polypeptide chain. , 1988, Journal of molecular biology.