**Vitamin D and Cancer**

[51] Levine, H. 3rd. Quantification of β-sheet amyloid fibril structures with thioflavin T.

[53] Tjernberg, L. O.; Naslund, J.; Lindqvist, F.; Johansson, J.; Karlstrom, A. R.; Thyberg, J.; Terenius, L.; Nordstedt, C. Controlling amyloid β peptide fibril formation with

[54] Matsunaga, Y.; Saito, N, Fujii, A.; Yokutani, J.; Takakura, T.; Nishimura, T.; Esaki, H.; Yamada, T. A pH-dependent conformational transition of Aβ peptide and physicochemical properties of the conformers in the glial cell. *Biochem J* 361: 547–556; 2002.

[55] Hatip, F. F.; Suenaga, M.; Yamada, T.; Matsunaga, Y. Reversal of temperature-induced conformational changes in the amyloid-beta peptide, Aβ40, by the β-sheet breaker

[56] Matsunaga, Y.; Peretz, D.; Williamson, A.; Burton, D.; Mehlhorn, I.; Groth, D.; Cohen, F. E.; Prusiner, S. B.; Baldwin, M. Cryptic epitopes in N-terminally truncated prion protein are exposed in the full-length molecule: dependence of conformation on pH.

[57] Hoffmann, R. W. Allylic 1,3-strain as a controlling factor in stereoselective transforma-

[58] Wiberg, K. B.; Martin, E. Barriers to rotation adjacent to double bonds. *J Am Chem Soc*

oligomerization in vitro. *PRION* 7: 1–7; 2013.

(90–

[52] Suenaga, M.; Hiramoto, Y.; Matsunaga, Y. Vitamin D2 interacts with human PrPc

protease-stable ligands. *J Biol Chem* 272: 12601–12605; 1997.

peptides 16–23 and 17–24. *J Pharmacol* 158: 1165–1172 ; 2009.

*Methods Enzymol* 309: 274–284; 1999.

231) and breaks PrPc

102 A Critical Evaluation of Vitamin D - Clinical Overview

*Protein* 44: 110–118; 2001.

107: 5035–5041; 1985.

tions. *Chem Rev* 89: 1841–1860; 1989.

**Provisional chapter**
