References
- Siekierka, J. J.; Hung, S. H. Y.; Poe, M.; Lin, C. S.; Sigal, N. H. Nature 1989, 341, 755. https://doi.org/10.1038/341755a0
- Deleersnijder, A.; Van Rompuy, A. S.; Desender, L.; Pottel, H.; Buee, L.; Debyser, Z.; Baekelandt, V.; Gerard, M. J. Biol. Chem. 2011, 286, 26687. https://doi.org/10.1074/jbc.M110.182303
- Gerard, M.; Debyser, Z.; Desender, L.; Kahle, P. J.; Baert, J.; Baekelandt, V.; Engelborghs, Y. FASEB J. 2006, 20, 524.
- Gerard, M.; Deleersnijder, A.; Daniëls, V.; Schreurs, S.; Munck, S.; Reumers, V.; Pottel, H.; Engelborghs, Y.; Van den Haute, C.; Taymans, J. M.; Debyser, Z.; Baekelandt, V. J. Neurosci. 2010, 30, 2454. https://doi.org/10.1523/JNEUROSCI.5983-09.2010
- Knappe, T. A.; Eckert, B.; Schaarschmidt, P.; Scholz, C.; Schmid, F. X. J. Mol. Biol. 2007, 368, 1458. https://doi.org/10.1016/j.jmb.2007.02.097
- Shin, E.; Lee, K. Bull. Chem. Korean Soc. 2012, 33, 281. https://doi.org/10.5012/bkcs.2012.33.1.281
- Weininger, U.; Haupt, C.; Schweimer, K.; Graubner, W.; Kovermann, M.; Bruser, T.; Scholz, C.; Schaarschmidt, P.; Zoldak, G.; Schmid, F. X.; Balbach, J. J. Mol. Biol. 2009, 387, 295. https://doi.org/10.1016/j.jmb.2009.01.034
- Yang, W.; Rozamus, L. W.; Narula, S.; Rollins, C. T.; Yuan, R.; Andrade, L. J.; Ram, M. K.; Phillips, T. B.; van Schravendijk, M. R.; Dalgarno, D.; Clackson, T.; Holt, D. A. J. Med. Chem. 2000, 43, 1135. https://doi.org/10.1021/jm9904396
- Banaszynski, L. A.; Chen, L. C.; Maynard-Smith, L. A.; Ooi, A. G.; Wandless, T. J. Cell 2006, 126, 995. https://doi.org/10.1016/j.cell.2006.07.025
- Kullertz, G.; Lüthe, S.; Fischer, G. Clin. Chem. 1998, 44, 502.
- Hottenrott, S.; Schumann, T.; Pluckthun, A.; Fischer, G.; Rahfeld, U. J. Biol. Chem. 1997, 272, 15697. https://doi.org/10.1074/jbc.272.25.15697
- Outeiro, T. F.; Klucken, J.; Strathearn, K. E.; Liu, F.; Nguyen, P.; Rochet, J. C.; Hyman, B. T.; McLean, P. J. Biochem. Biophys. Res. Commun. 2006, 351, 631. https://doi.org/10.1016/j.bbrc.2006.10.085
- Kong, B.; Chae, Y. K.; Lee, K. Protein. Pept. Lett. 2003, 10, 491. https://doi.org/10.2174/0929866033478717
- Selkoe, D. J. Annu. Rev. Neurosci. 1989, 12, 463. https://doi.org/10.1146/annurev.ne.12.030189.002335
- Liu, F. L.; Liu, P. H.; Shao, H. W.; Kung, F. L. Biochem. Biophys. Res. Commun. 2006, 350, 472. https://doi.org/10.1016/j.bbrc.2006.09.073
- Eggert, S.; Midthune, B.; Cottrell, B.; Koo, E. H. J. Biol. Chem. 2009, 284, 28943. https://doi.org/10.1074/jbc.M109.038646
- Meuvis J.; Gerard, M.; Desender, L.; Baekelandt, V.; Engelborghs, Y. Biochemistry 2010, 49, 9345. https://doi.org/10.1021/bi1010927
- Bradford, M. M. Anal. Biochem. 1976, 72, 248. https://doi.org/10.1016/0003-2697(76)90527-3
Cited by
- Expression of Chaperone-Synuclein Fusion Proteins and Their Regulatory Effects on Amyloid Fibril Formation vol.36, pp.11, 2015, https://doi.org/10.1002/bkcs.10546
- Regulation of Amyloid Fibril Formation from Human Islet Amyloid Polypeptide by a Ligand Binding to the Fusion of FK506-binding Protein and the Insertion-in-Flap Domain vol.38, pp.11, 2017, https://doi.org/10.1002/bkcs.11282
- Amyloid Fibril Formation of α‐Synuclein Is Modulated via the Estrogen Receptor Ligand Binding Domain of Estrogen Receptor α Bound with Tamoxifen‐based Small Molecules vol.41, pp.3, 2020, https://doi.org/10.1002/bkcs.11956