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Characterization of the denaturation and renaturation of human plasma vitronectin. II. Investigation into the mechanism of formation of multimers.
Zhuang P, Li H, Williams JG, Wagner NV, Seiffert D, Peterson CB. Zhuang P, et al. J Biol Chem. 1996 Jun 14;271(24):14333-43. doi: 10.1074/jbc.271.24.14333. J Biol Chem. 1996. PMID: 8663085 Free article.
A mechanism for the folding reactions of vitronectin has been proposed (Zhuang, P., Blackburn, M. N., and Peterson, C. B.(1996) J. Biol. Chem. 270, 14323-14332) in which vitronectin acquires a partially folded intermediate structure which is highly prone to oligomer …
A mechanism for the folding reactions of vitronectin has been proposed (Zhuang, P., Blackburn, M. N., and Peterson, C. B.(1996 …
Native and multimeric vitronectin exhibit similar affinity for heparin. Differences in heparin binding properties induced upon denaturation are due to self-association into a multivalent form.
Zhuang P, Chen AI, Peterson CB. Zhuang P, et al. J Biol Chem. 1997 Mar 14;272(11):6858-67. doi: 10.1074/jbc.272.11.6858. J Biol Chem. 1997. PMID: 9054371 Free article.
Denaturation and renaturation of vitronectin under near physiological solution conditions is accompanied invariably by self-association of the protein into a multimeric form (Zhuang, P., Blackburn, M. N., and Peterson, C. B. (1996) J. Biol. Chem. 271, 14323-14332), …
Denaturation and renaturation of vitronectin under near physiological solution conditions is accompanied invariably by self-association of t …
587 results