Voir la notice de l'article provenant de la source Math-Net.Ru
@article{MBB_2010_5_2_a5,
author = {M. Yu. Lobanov and O. V. Galzitskaya},
title = {Statistical analysis and prediction of disordered residues in protein structures},
journal = {Matemati\v{c}eska\^a biologi\^a i bioinformatika},
pages = {124--137},
publisher = {mathdoc},
volume = {5},
number = {2},
year = {2010},
language = {ru},
url = {http://geodesic.mathdoc.fr/item/MBB_2010_5_2_a5/}
}
TY - JOUR AU - M. Yu. Lobanov AU - O. V. Galzitskaya TI - Statistical analysis and prediction of disordered residues in protein structures JO - Matematičeskaâ biologiâ i bioinformatika PY - 2010 SP - 124 EP - 137 VL - 5 IS - 2 PB - mathdoc UR - http://geodesic.mathdoc.fr/item/MBB_2010_5_2_a5/ LA - ru ID - MBB_2010_5_2_a5 ER -
%0 Journal Article %A M. Yu. Lobanov %A O. V. Galzitskaya %T Statistical analysis and prediction of disordered residues in protein structures %J Matematičeskaâ biologiâ i bioinformatika %D 2010 %P 124-137 %V 5 %N 2 %I mathdoc %U http://geodesic.mathdoc.fr/item/MBB_2010_5_2_a5/ %G ru %F MBB_2010_5_2_a5
M. Yu. Lobanov; O. V. Galzitskaya. Statistical analysis and prediction of disordered residues in protein structures. Matematičeskaâ biologiâ i bioinformatika, Tome 5 (2010) no. 2, pp. 124-137. http://geodesic.mathdoc.fr/item/MBB_2010_5_2_a5/
[1] Tompa P., “Intrinsically unstructured proteins”, Trends Biochem. Sci., 27 (2002), 527–533 | DOI
[2] Wright P. E., Dyson H. J., “Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm”, J. Mol. Biol., 293 (1999), 321–331 | DOI
[3] Sickmeier M., Hamilton J. A., LeGall T., Vacic V., Cortese M. S., Tantos A., Szabo B., Tompa P., Chen J., Uversky V. N., Obradovic Z., Dunker A. K., “DisProt: the database of disordered proteins”, Nucl. Acids Res., 35 (2007), D786–793 | DOI
[4] Dunker A. K., Brown C. J., Lawson J. D., Iakoucheva L. M., Obradovic Z., “Intrinsic disorder and protein function”, Biochemistry, 41 (2002), 6573–6582 | DOI
[5] Romero P., Obradovic Z., Kissinger C. R., Villafranca L. E., Dunker A. K., “Identifying disordered regions in proteins from amino acid sequence”, Proc. of the IEE International Conference on Neural Networks, 1997, 90–95
[6] Li X., Romero P., Rani M., Dunker A. K., Obradovic A. Z., “Prediction protein disordered for N-, C-, and internal regions”, Genome Inform., 10 (1999), 30–40
[7] Galzitskaya O. V., Garbuzynskiy S. O., Lobanov M. Yu., “Prediction of amyloidogenic and disordered regions in protein chain”, PLoS Comput. Biol., 2 (2006), e177 | DOI
[8] Galzitskaya O. V., Garbuzynskiy S. O., Lobanov M. Yu., “FoldUnfold: web server for the prediction of disorderred regions in protein chain”, Bioinformatics, 22 (2006), 2948–2949 | DOI
[9] Galzitskaya O. V., Garbuzinskii S. A., Lobanov M. Yu., “Predskazanie nativno-razvernutykh uchastkov belkovoi tsepi”, Molekulyar. biologiya, 40 (2006), 341–348
[10] Coeytaux K., Poupon A., “Prediction of unfolded segments in a protein sequence based on amino acid composition”, Bioinformatics, 21 (2005), 1891–1900 | DOI
[11] Dosztanyi Z., Csizmok V., Tompa P., Simon I., “The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins”, J. Mol. Biol., 347 (2005), 827–839 | DOI
[12] Dosztanyi Z., Csizmok V., Tompa P., Simon I., “IUPred: web server for the prediction of intrinsically unstructured regions based on estimated energy content”, Bioinformatics, 21 (2005), 3433–3434 | DOI
[13] Linding R., Russell R. B., Neduva V., Gibson T. J., “GlobPlot: Exploring protein sequences for globularity and disorder”, Nucl. Acids Res., 31 (2003), 3701–3708 | DOI
[14] Prilusky J., Felder C. E., Zeev-Ben-Mordehai T., Rydberg E. H., Man O., Beckmann J. S., Silman I., Sussman J. L., “FoldIndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded”, Bioinformatics, 21 (2005), 3435–3438 | DOI
[15] Yang Z. R., Thomson R., McNeil P., Esnouf R. M., “RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins”, Bioinformatics, 21 (2005), 3369–3376 | DOI
[16] Linding R., Jensen L., Diella F., Bork P., Gibson T., Russell R., “Protein disorder prediction: implications for structural proteomics”, Structure, 11 (2003), 1453–1459 | DOI
[17] Ward J. J., McGuffin L. J., Bryson K., Buxton B. F., Jones D. T., “The DISOPRED server for the prediction of protein disorder”, Bioinformatics, 20 (2004), 2138–2139 | DOI
[18] Ising E., “Beitrag zut Theorie des Ferromagnetizmus”, Zeitschr. Phys., 31 (1925), 253–258 | DOI
[19] Zimm B. H., Bragg J. K., “Theory of the phase transition between helix and random coil in polypeptide chains”, J. Chem. Phys., 31 (1959), 526–535 | DOI
[20] Finkelstein A. V., “Theory of protein molecule self-organization. III. A calculating method for the probabilities of the secondary structure formation in an unfolded protein chain”, Biopolymers., 16 (1977), 525–529 | DOI
[21] Finkelstein A. V., Roytberg M. A., “Computation of biopolymers: A general approach to different problems”, BioSystems, 30 (1993), 1–19 | DOI
[22] Melamud E., Moult J., “Evaluation of disorder predictions in CASP5”, Proteins, 53, Suppl. 6 (2003), 561–565 | DOI
[23] Jin Y., Dunbrack R. L. Jr., “Assessment of disorder predictions in CASP6”, Proteins, 61, Suppl. 7 (2005), 167–175 | DOI
[24] Bordoli L., Kiefer F., Schwede T., “Assessment of disordered predictions in CASP7”, Proteins, 69, Suppl. 8 (2007), 129–136 | DOI
[25] Noivirt-Brik O., Prilusky J., Sussman J. L., “Assessment of disordered predictions in CASP8”, Proteins, 77, Suppl. 9 (2009), 210–216 | DOI