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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
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]. ...
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 …
Charge engineering of a protein domain to allow efficient ion-exchange recovery.
Gräslund T, Lundin G, Uhlén M, Nygren PA, Hober S. Gräslund T, et al. Protein Eng. 2000 Oct;13(10):703-9. doi: 10.1093/protein/13.10.703. Protein Eng. 2000. PMID: 11112509
Strategy for highly selective ion-exchange capture using a charge-polarizing fusion partner.
Gräslund T, Ehn M, Lundin G, Hedhammar M, Uhlén M, Nygren PA, Hober S. Gräslund T, et al. J Chromatogr A. 2002 Jan 4;942(1-2):157-66. doi: 10.1016/s0021-9673(01)01413-3. J Chromatogr A. 2002. PMID: 11822381
Engineering streptococcal protein G for increased alkaline stability.
Gülich S, Linhult M, Ståhl S, Hober S. Gülich S, et al. Protein Eng. 2002 Oct;15(10):835-42. doi: 10.1093/protein/15.10.835. Protein Eng. 2002. PMID: 12468718
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