From Protein Structure to Function with Bioinformatics.pdf

140 P. TompaVacic V, Oldfield CJ, Mohan A, et al. (2007) Characterization of molecular recognition features,MoRFs, and their binding partners. J Proteome Res 6:2351–2366Vucetic S, Brown CJ, Dunker AK, et al. (2003) Flavors of protein disorder. Proteins 52:573–584Waizenegger I, Gimenez-Abian JF, Wernic D, et al. (2002) Regulation of human separase bysecurin binding and autocleavage. Curr Biol 12:1368–1378Ward JJ, Sodhi JS, McGuffin LJ, et al. (2004) Prediction and functional analysis of native disorderin proteins from the three kingdoms of life. J Mol Biol 337:635–645Weathers EA, Paulaitis ME, Woolf TB, et al. (2004) Reduced amino acid alphabet is sufficient toaccurately recognize intrinsically disordered protein. FEBS Lett 576:348–352Weinreb PH, Zhen W, Poon AW, et al. (1996) NACP, a protein implicated in Alzheimer’s diseaseand learning, is natively unfolded. Biochemistry 35:13709–13715Wickner RB, Edskes HK, Maddelein ML, et al. (1999) Prions of yeast and fungi. Proteins asgenetic material. J Biol Chem 274:555–558Wootton JC (1994a) Non-globular domains in protein sequences: automated segmentation usingcomplexity measures. Comput Chem 18:269–285Wootton JC (1994b) Sequences with “unusual” amino acid compositions. Curr Opin Struct Biol4:413–421Wright PE, Dyson HJ (1999) Intrinsically unstructured proteins: re-assessing the protein structure-functionparadigm. J Mol Biol 293:321–331Xie H, Vucetic S, Iakoucheva LM, et al. (2007) Functional anthology of intrinsic disorder. 1.Biological processes and functions of proteins with long disordered regions. J Proteome Res6:1882–1898