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Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions.
Hober S, Lundström Ljung J, Uhlén M, Nilsson B. Hober S, et al. FEBS Lett. 1999 Jan 29;443(3):271-6. doi: 10.1016/s0014-5793(98)01737-2. FEBS Lett. 1999. PMID: 10025946 Free article.
Insulin-like growth factor (IGF) I does not quantitatively form its three native disulfide bonds in the presence of 10 mM reduced and 1 mM oxidized glutathione in vitro [Hober, S. et al. (1992) Biochemistry 31, 1749-1756]. In this paper, we show (i) that both IGF-I …
Insulin-like growth factor (IGF) I does not quantitatively form its three native disulfide bonds in the presence of 10 mM reduced and 1 mM o …
Structure, specificity, and mode of interaction for bacterial albumin-binding modules.
Johansson MU, Frick IM, Nilsson H, Kraulis PJ, Hober S, Jonasson P, Linhult M, Nygren PA, Uhlén M, Björck L, Drakenberg T, Forsén S, Wikström M. Johansson MU, et al. Among authors: hober s. J Biol Chem. 2002 Mar 8;277(10):8114-20. doi: 10.1074/jbc.M109943200. Epub 2001 Dec 18. J Biol Chem. 2002. PMID: 11751858 Free article.
181 results