Abundance of intrinsic disorder in protein associated with cardiovascular disease
作者： Yugong Cheng , Tanguy LeGall , Christopher J. Oldfield , A. Keith Dunker , Vladimir N. Uversky
DOI: 10.1021/BI060981D
关键词:
摘要: Evidence that many protein regions and even entire proteins lacking stable tertiary and/or secondary structure in solution (i.e., intrinsically disordered proteins) might be involved protein−protein interactions, regulation, recognition, signal transduction is rapidly accumulating. These signaling play a crucial role the development of several pathological conditions, including cancer. To test hypothesis intrinsic disorder also abundant cardiovascular disease (CVD), data set 487 CVD-related was extracted from SWISS-PROT. are depleted major order-promoting residues (Trp, Phe, Tyr, Ile, Val) enriched some disorder-promoting (Arg, Gln, Ser, Pro, Glu). The application neural network predictor natural (PONDR VL-XT) together with cumulative distribution function (CDF) analysis, charge−hydropathy plot (CH plot) α-helical molecular recognition feature (α-MoRF) indicator revealed t...
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sci-hub.se 参考文章(34)
J M Maraganore, B Chao, M L Joseph, J Jablonski, K L Ramachandran, Anticoagulant activity of synthetic hirudin peptides. Journal of Biological Chemistry. ,vol. 264, pp. 8692- 8698 ,(1989) , 10.1016/S0021-9258(18)81848-8
Vladimir N. Uversky, What does it mean to be natively unfolded? European Journal of Biochemistry. ,vol. 269, pp. 2- 12 ,(2002) , 10.1046/J.0014-2956.2001.02649.X
Russell F. Doolittle, Stephen J. Everse, Glen Spraggon, Human fibrinogen: anticipating a 3-dimensional structure. The FASEB Journal. ,vol. 10, pp. 1464- 1470 ,(1996) , 10.1096/FASEBJ.10.13.8940292
A K Dunker, A J Kenyon, Mobility of sodium dodecyl sulphate - protein complexes Biochemical Journal. ,vol. 153, pp. 191- 197 ,(1976) , 10.1042/BJ1530191
Keiichi Namba, Roles of partly unfolded conformations in macromolecular self-assembly. Genes to Cells. ,vol. 6, pp. 1- 12 ,(2001) , 10.1046/J.1365-2443.2001.00384.X
Angelo Fontana, Marcello Zambonin, Patrizia Polverino de Laureto, Vincenzo De Filippis, Angelica Clementi, Elena Scaramella, Probing the conformational state of apomyoglobin by limited proteolysis 1 1Edited by P. E. Wright Journal of Molecular Biology. ,vol. 266, pp. 223- 230 ,(1997) , 10.1006/JMBI.1996.0787
Alexander P. Demchenko, Recognition between flexible protein molecules: induced and assisted folding. Journal of Molecular Recognition. ,vol. 14, pp. 42- 61 ,(2001) , 10.1002/1099-1352(200101/02)14:1<42::AID-JMR518>3.0.CO;2-8
Jack Kyte, Russell F. Doolittle, A simple method for displaying the hydropathic character of a protein Journal of Molecular Biology. ,vol. 157, pp. 105- 132 ,(1982) , 10.1016/0022-2836(82)90515-0
Monika Fuxreiter, István Simon, Peter Friedrich, Peter Tompa, Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. Journal of Molecular Biology. ,vol. 338, pp. 1015- 1026 ,(2004) , 10.1016/J.JMB.2004.03.017
B. E. H. MADEN, M. SALIM, D. F. SUMMERS, Maturation Pathway for Ribosomal RNA in the Hela Cell Nucleolus Nature. ,vol. 237, pp. 5- 9 ,(1972) , 10.1038/NEWBIO237005A0