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222 related items for PubMed ID: 8519775
1. Kinetically trapped structure in the renaturation of reduced oxindolealanine 62 lysozyme. Ueda T, Abe Y, Ohkuri T, Kawano K, Terada Y, Imoto T. Biochemistry; 1995 Dec 12; 34(49):16178-85. PubMed ID: 8519775 [Abstract] [Full Text] [Related]
2. A study of renaturation of reduced hen egg white lysozyme. Enzymically active intermediates formed during oxidation of the reduced protein. Acharya AS, Taniuchi H. J Biol Chem; 1976 Nov 25; 251(22):6934-46. PubMed ID: 1033181 [Abstract] [Full Text] [Related]
3. Cooperative folding of the isolated alpha-helical domain of hen egg-white lysozyme. Bai P, Peng Z. J Mol Biol; 2001 Nov 23; 314(2):321-9. PubMed ID: 11718563 [Abstract] [Full Text] [Related]
4. Effect of the structure of the denatured state of lysozyme on the aggregation reaction at the early stages of folding from the reduced form. Ohkuri T, Shioi S, Imoto T, Ueda T. J Mol Biol; 2005 Mar 18; 347(1):159-68. PubMed ID: 15733925 [Abstract] [Full Text] [Related]
7. Analysis of catalytic properties of hen egg white lysozyme during renaturation from denatured and reduced material. Fischer B, Sumner I, Goodenough P. Arch Biochem Biophys; 1992 Nov 01; 298(2):361-4. PubMed ID: 1416967 [Abstract] [Full Text] [Related]
8. The role of net charge on the renaturation of reduced lysozyme by the sulfhydryl-disulfide interchange reaction. Maeda Y, Ueda T, Yamada H, Imoto T. Protein Eng; 1994 Oct 01; 7(10):1249-54. PubMed ID: 7855140 [Abstract] [Full Text] [Related]
9. Characterisation of the dominant oxidative folding intermediate of hen lysozyme. van den Berg B, Chung EW, Robinson CV, Dobson CM. J Mol Biol; 1999 Jul 16; 290(3):781-96. PubMed ID: 10395829 [Abstract] [Full Text] [Related]
10. [Studies on formation of aggregates from denatured lysozymes upon renaturing with size exclusion chromatography]. Bian L, Yang X, Liu L. Se Pu; 2005 Mar 16; 23(2):129-33. PubMed ID: 16013553 [Abstract] [Full Text] [Related]
11. The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge. Yokota A, Izutani K, Takai M, Kubo Y, Noda Y, Koumoto Y, Tachibana H, Segawa S. J Mol Biol; 2000 Feb 04; 295(5):1275-88. PubMed ID: 10653703 [Abstract] [Full Text] [Related]
12. Effect of chemical modifications of tryptophan residues on the folding of reduced hen egg-white lysozyme. Ueda T, Yamada H, Aoki H, Imoto T. J Biochem; 1990 Nov 04; 108(5):886-92. PubMed ID: 2081739 [Abstract] [Full Text] [Related]
13. Identification of the peptide region that folds native conformation in the early stage of the renaturation of reduced lysozyme. Ueda T, Ohkuri T, Imoto T. Biochem Biophys Res Commun; 1996 Nov 01; 228(1):203-8. PubMed ID: 8912660 [Abstract] [Full Text] [Related]
16. Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme. Eyles SJ, Radford SE, Robinson CV, Dobson CM. Biochemistry; 1994 Nov 08; 33(44):13038-48. PubMed ID: 7947709 [Abstract] [Full Text] [Related]
17. Formation of alpha-helix 88-98 is essential in the establishment of higher-order structure from reduced lysozyme. Ueda T, Nakashima A, Hashimoto Y, Miki T, Yamada H, Imoto T. J Mol Biol; 1994 Jan 28; 235(4):1312-7. PubMed ID: 8308893 [Abstract] [Full Text] [Related]
18. Relationship between the optimal temperature for oxidative refolding and the thermal stability of refolded state of hen lysozyme three-disulfide derivatives. Tachibana H, Ohta K, Sawano H, Koumoto Y, Segawa S. Biochemistry; 1994 Dec 20; 33(50):15008-16. PubMed ID: 7999758 [Abstract] [Full Text] [Related]
19. Evidence for an initiation site for hen lysozyme folding from the reduced form using its dissected peptide fragments. Ohkuri T, Ueda T, Tsurumaru M, Imoto T. Protein Eng; 2001 Nov 20; 14(11):829-33. PubMed ID: 11742101 [Abstract] [Full Text] [Related]
20. The unfolding mechanism and the disulfide structures of denatured lysozyme. Chang JY, Li L. FEBS Lett; 2002 Jan 30; 511(1-3):73-8. PubMed ID: 11821052 [Abstract] [Full Text] [Related] Page: [Next] [New Search]