Art

J-GLOBAL ID：200902251025837562   Reference number：09A0711633

Amyloid fibrillation rate differs greatly among single-disulfide variants of hen lysozyme

アミロイド線維化速度はニワトリリゾチームの単一シスルフィド変異体間で大きく異なる

Author (5)： KONO Ryohei (Kinki Univ., Wakayama, JPN) ,  FUJISAWA Tetsuro (Gifu Univ., Gifu, JPN) ,  FUJISAWA Tetsuro (RIKEN SPring-8 center, Hyogo, JPN) ,  AKASAKA Kazuyuki (Kinki Univ., Wakayama, JPN) ,  TACHIBANA Hideki (Kinki Univ., Wakayama, JPN)
Material： 生物高分子  (Journal of Biological Macromolecules)
Volume： 9  Issue： 1  Page： 23-30  Publication year： Mar. 01, 2009 
JST Material Number： L4559A  ISSN： 1347-2194  CODEN： JBM0A6  Document type： Article
Article type： 原著論文  Country of issue： Japan (JPN)  Language： ENGLISH (EN)

Thesaurus term： Gallus gallus domesticus ,...

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JST classification (1)： Proteins and peptides in general  (EB03010N)

Reference (25)：

• Dobson, C. M.(1999). Protein misfolding, evolution and disease. Trends Biochem. Sci.24, 329-332.
• Uversky, V. N. and Fink, A. L.(2004). Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim. Biophys. Acta 1698, 131-153
• Smith, D. P., Jones, S., Serpell, L. C., Sunde, M. and Radford, S. E.(2003). A systematic investigation into the effect of protein destabilisation on 132-microglobulin amyloid formation. J. Mol. Biol.330, 943-954.
• Tachibana, H. and Segawa, S.(2004). Disulfide-bond associated protein folding. In Encyclopedia of Nanoscience and Nanotechnology (Nalwa, H. S., ed.), pp. 443-473. American Scientific Publishers.
• Sawano, H., Koumoto, Y., Ohta, K., Sasaki, Y., Segawa, S. and Tachibana, H.(1992). Efficient in vitro folding of the three-disulfide derivatives of hen lysozyme in the presence of glycerol. FEBS Lett.303, 11-14.

Terms in the title (4)： アミロイド線維 ,  ニワトリ ,  リゾチーム ,  変異体