Polymerization mechanism of polypeptide chain aggregation.
暂无分享,去创建一个
[1] J. King,et al. Mutational analysis of protein folding pathways: the P22 tailspike endorhamnosidase. , 1986, Methods in enzymology.
[2] D A Agard,et al. Kinetics versus thermodynamics in protein folding. , 1994, Biochemistry.
[3] G. A. Bowden,et al. The Effect of Sugars on β‐Lactamase Aggregation in Escherichia coli , 1988 .
[4] A. Minton,et al. Confinement as a determinant of macromolecular structure and reactivity. , 1992, Biophysical journal.
[5] J. King,et al. Reconstitution of the thermostable trimeric phage P22 tailspike protein from denatured chains in vitro. , 1989, The Journal of biological chemistry.
[6] R. Jaenicke,et al. Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation. , 1979, Biochemistry.
[7] J. King,et al. Protein Folding Intermediates and Inclusion Body Formation. , 1989, Bio/Technology.
[8] D L Caspar,et al. Movement and self-control in protein assemblies. Quasi-equivalence revisited. , 1980, Biophysical journal.
[9] J. King,et al. Genetic analysis of the folding pathway for the tail spike protein of phage P22. , 1983, Proceedings of the National Academy of Sciences of the United States of America.
[10] S. Asakura,et al. RECONSTITUTION OF BACTERIAL FLAGELLA IN VITRO. , 1964, Journal of molecular biology.
[11] Daniel I. C. Wang,et al. Molecular thermodynamic model for Helix‐Helix docking and protein aggregation , 1995 .
[12] Charles R.scriver,et al. The Metabolic basis of inherited disease , 1989 .
[13] C. Frank,et al. Dynamic light-scattering studies of the fractal aggregation of poly(methacrylic acid) and poly(ethylene glycol) , 1990 .
[14] B Fane,et al. Global suppression of protein folding defects and inclusion body formation. , 1991, Science.
[15] R. Wetzel. Mutations and off-pathway aggregation of proteins. , 1994, Trends in biotechnology.
[16] R. Seckler,et al. Mechanism of phage P22 tailspike protein folding mutations , 1993, Protein science : a publication of the Protein Society.
[17] J. King,et al. Nucleation and growth phases in the polymerization of coat and scaffolding subunits into icosahedral procapsid shells. , 1993, Biophysical journal.
[18] P. S. Kim,et al. Intermediates in the folding reactions of small proteins. , 1990, Annual review of biochemistry.
[19] G. Dollinger,et al. Practical on-line determination of biopolymer molecular weights by high-performance liquid chromatography with classical light-scattering detection , 1992 .
[20] R. Seckler,et al. In vitro folding pathway of phage P22 tailspike protein. , 1991, Biochemistry.
[21] E. Korn,et al. The kinetics of actin nucleation and polymerization. , 1983, The Journal of biological chemistry.
[22] P. Lansbury,et al. Amyloid fibril formation requires a chemically discriminating nucleation event: studies of an amyloidogenic sequence from the bacterial protein OsmB. , 1992, Biochemistry.
[23] 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 .
[24] Daniel I. C. Wang,et al. Equilibrium Association of a Molten Globule Intermediate in the Refolding of Bovine Carbonic Anhydrase , 1991 .
[25] 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.
[26] J. King,et al. Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates , 1996, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[27] J. King,et al. Trimeric intermediate in the in vivo folding and subunit assembly of the tail spike endorhamnosidase of bacteriophage P22. , 1982, Proceedings of the National Academy of Sciences of the United States of America.
[28] J. Hofrichter,et al. Kinetic studies on photolysis-induced gelation of sickle cell hemoglobin suggest a new mechanism. , 1980, Biophysical journal.
[29] W. F. Harrington,et al. Collagen structure in solution. II. Analysis of refolding kinetics in terms of nucleation and growth processes. , 1970, Biochemistry.
[30] Ken A. Dill,et al. Aggregation of globular proteins , 1993 .
[31] S. Katz,et al. Some problems in particle technology: A statistical mechanical formulation , 1964 .
[32] Todd M. Przybycien,et al. Secondary structure characterization of beta-lactamase inclusion bodies. , 1994, Protein engineering.
[33] G. Georgiou,et al. Inclusion Bodies and Recovery of Proteins from the Aggregated State , 1991 .
[34] J. King,et al. Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains , 1995, Protein science : a publication of the Protein Society.
[35] Robert M. Ziff. AGGREGATION KINETICS VIA SMOLUCHOWSKI'S EQUATION , 1984 .
[36] P. Lansbury,et al. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. , 1993, Biochemistry.
[37] J. King,et al. Intracellular trapping of a cytoplasmic folding intermediate of the phage P22 tailspike using iodoacetamide. , 1994, The Journal of biological chemistry.
[38] J. King,et al. Temperature-sensitive mutations and second-site suppressor substitutions affect folding of the P22 tailspike protein in vitro. , 1993, The Journal of biological chemistry.
[39] A. Fink,et al. Nativelike secondary structure in interleukin-1 beta inclusion bodies by attenuated total reflectance FTIR. , 1994, Biochemistry.
[40] S. Steinbacher,et al. Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer. , 1994, Science.
[41] B. Vincent,et al. Coagulation kinetics and structure formation , 1987 .
[42] D. Brems. Solubility of different folding conformers of bovine growth hormone , 1988 .