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Prediction of ID and Its Use in Functional Proteomics 87AcknowledgmentsThe Indiana Genomics Initiative, funded in part by the Lilly Endowment, andNational Institute of Health Grant no. 1 R01 LM007688-0A1 provided supportfor P.R., V.N.U, Z.O, and A.K.D. This work received additional support fromthe Programs of the Russian Academy of Sciences for the “Molecular and cellularbiology” and “Fundamental science for medicine” especially for V.N.U. L.M.I.was supported by National Science Foundation (NSF) grant no. MCB0444818.References1. Fischer, E. (1894) Einfluss der configuration auf die wirkung der enzyme. Ber.Dtsch. Chem. Ges. 27, 2985–2993.2. Obradovic, Z., Peng, K., Vucetic, S., Radivojac, P., Brown, C. J., and Dunker,A. K. (2003) Predicting intrinsic disorder from amino acid sequence. Proteins 53,566–572.3. Linderstrom-Lang, K. U. and Schellman, J. A. (1959) Protein structure andenzyme activity, in The Enzymes, (Boyer, P. D., Lardy, H., and Myrback, K.,eds.), Academic Press, New York, pp. 443–510.4. Pullen, R. A., Jenkins, J. A., Tickle, I. J., Wood, S. P., and Blundell, T. L. (1975)The relation of polypeptide hormone structure and flexibility to receptor binding:the relevance of X-ray studies on insulins, glucagon and human placental lactogen.Mol. Cell Biochem. 8, 5–20.5. Cary, P. D., Moss, T., and Bradbury, E. M. (1978) High-resolution proton-magneticresonancestudies of chromatin core particles. Eur. J. Biochem. 89, 475–482.6. Holt, C. and Sawyer, L. (1993) Caseins as rheomorphic proteins: interpretation ofprimary and secondary structures of the αs1-, β-, and κ-caseins. J. Chem. Soc.Faraday Trans. 89, 2683–2692.7. Schweers, O., Schoenbrunn-Hanebeck, E., Marx, A., and Mandelkow, E. (1994)Structural studies of tau protein and alzheimer paired helical filaments show noevidence for β-structure. J. Biol. Chem. 269, 24,290–24,297.8. Weinreb, P. H., Zhen, W., Poon, A. W., Conway, K. A., and Lansbury, P. T., Jr.(1996) NACP, a protein implicated in Alzheimer’s disease and learning, is nativelyunfolded. Biochemistry 35, 13,709–13,715.9. Wright, P. E. and Dyson, H. J. (1999) Intrinsically unstructured proteins: re-assessingthe protein structure-function paradigm. J. Mol. Biol. 293, 321–331.10. Dunker, A. K., Lawson, J. D., Brown, C. J., et al. (2001) Intrinsically disorderedprotein. J. Mol. Graph. Model 19, 26–59.11. Daughdrill, G. W., Pielak, G. J., Uversky, V. N., Cortese, M. S., and Dunker, A. K.(2005) Natively disordered protein, in Protein Folding Handbook, (Buchner, J.and Kiefhaber, T. eds.), Wiley-VCH: Verlag GmbH & Co., KGaA, Weinheim,pp. 271–353.12. Uversky, V. N. (2003) A protein-chameleon: conformational plasticity of alphasynuclein,a disordered protein involved in neurodegenerative disorders. J. Biomol.Struct. Dyn. 21, 211–234.