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The ZipperDB database and server is restricted to academic and non-profit users. Commercial users must obtain a license. Please contact us for more information.

Questions regarding the fibrillation predictions in this database or this web server, please email us at zipperdb@mbi.ucla.edu.

If you find this database useful, please cite:
Goldschmidt L, Teng PK, Riek R, Eisenberg D (2010). The amylome, all proteins capable of forming amyloid-like fibrils. PNAS, 107(8): 3487-3492.

References:

Thompson M.J., Sievers S.A., Karanicolas J., Ivanova M.I., Baker D. and Eisenberg D. (2006). The 3D profile method for identifying fibril-forming segments of proteins. Proc. Natl. Acad. Sci. U.S.A., 103(11):4074-4078.
Sawaya M.R., Sambashivan S., Nelson, R., Ivanova M.I., Sievers S.A., Apostol M.I., Thompson M.J., Balbirnie M., Wiltzius J.W.W., McFarlane H.T., Madsen A.Ø., Riekel C., Eisenberg D. (2006). Atomic structures of amyloid cross-beta spines reveal varied steric zippers. Nature., 447:453-457.
Nelson R., Sawaya M.R., Balbirnie M., Madsen A.Ø., Riekel C., Grothe G., Eisenberg D. (2005). Structure of the cross-beta spine of amyloid-like fibrils. Nature., 435:773-778.
Kuhlman B., Baker D. (2000). Native protein sequences are close to optimal for their structures. Proc. Natl. Acad. Sci. U.S.A., 97:10383–10388.