Radius of gyration as an indicator of protein structure compactness MY Lobanov, NS Bogatyreva, OV Galzitskaya Molecular Biology 42, 623-628, 2008 | 991 | 2008 |
FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence SO Garbuzynskiy, MY Lobanov, OV Galzitskaya Bioinformatics 26 (3), 326-332, 2010 | 434 | 2010 |
A theoretical search for folding/unfolding nuclei in three-dimensional protein structures OV Galzitskaya, AV Finkelstein Proceedings of the National Academy of Sciences 96 (20), 11299-11304, 1999 | 382 | 1999 |
Radius of gyration is indicator of compactness of protein structure L MIu, NS Bogatyreva, OV Galzitskaia Molekuliarnaia biologiia 42 (4), 701-706, 2008 | 284 | 2008 |
Prediction of amyloidogenic and disordered regions in protein chains OV Galzitskaya, SO Garbuzynskiy, MY Lobanov PLoS computational biology 2 (12), e177, 2006 | 215 | 2006 |
FoldUnfold: web server for the prediction of disordered regions in protein chain OV Galzitskaya, SO Garbuzynskiy, MY Lobanov Bioinformatics 22 (23), 2948-2949, 2006 | 198 | 2006 |
Chain length is the main determinant of the folding rate for proteins with three‐state folding kinetics OV Galzitskaya, SO Garbuzynskiy, DN Ivankov, AV Finkelstein Proteins: Structure, Function, and Bioinformatics 51 (2), 162-166, 2003 | 185 | 2003 |
Physics of protein folding AV Finkelstein, OV Galzitskaya Physics of Life reviews 1 (1), 23-56, 2004 | 147 | 2004 |
Intrinsic disorder in protein interactions: insights from a comprehensive structural analysis JH Fong, BA Shoemaker, SO Garbuzynskiy, MY Lobanov, OV Galzitskaya, ... PLoS computational biology 5 (3), e1000316, 2009 | 138 | 2009 |
Different packing of external residues can explain differences in the thermostability of proteins from thermophilic and mesophilic organisms AV Glyakina, SO Garbuzynskiy, MY Lobanov, OV Galzitskaya Bioinformatics 23 (17), 2231-2238, 2007 | 110 | 2007 |
To be folded or to be unfolded? SO Garbuzynskiy, MY Lobanov, OV Galzitskaya Protein Science 13 (11), 2871-2877, 2004 | 107 | 2004 |
Comparison of X‐ray and NMR structures: is there a systematic difference in residue contacts between X‐ray‐and NMR‐resolved protein structures? SO Garbuzynskiy, BS Melnik, MY Lobanov, AV Finkelstein, ... Proteins: Structure, Function, and Bioinformatics 60 (1), 139-147, 2005 | 106 | 2005 |
Folding nuclei in proteins OV Galzitskaya, DN Ivankov, AV Finkelstein Molecular Biology 35, 605-613, 2001 | 105 | 2001 |
Trend of amino acid composition of proteins of different taxa NS Bogatyreva, AV Finkelstein, OV Galzitskaya Journal of bioinformatics and computational biology 4 (02), 597-608, 2006 | 102 | 2006 |
The role of β-amyloid peptide in neurodegenerative diseases AV Maltsev, S Bystryak, OV Galzitskaya Ageing research reviews 10 (4), 440-452, 2011 | 88 | 2011 |
Coupling between properties of the protein shape and the rate of protein folding DN Ivankov, NS Bogatyreva, MY Lobanov, OV Galzitskaya PloS one 4 (8), e6476, 2009 | 88 | 2009 |
Megahertz single-particle imaging at the European XFEL E Sobolev, S Zolotarev, K Giewekemeyer, J Bielecki, K Okamoto, ... Communications Physics 3 (1), 97, 2020 | 87 | 2020 |
The Ising model for prediction of disordered residues from protein sequence alone MY Lobanov, OV Galzitskaya Physical biology 8 (3), 035004, 2011 | 87 | 2011 |
Outlining folding nuclei in globular proteins SO Garbuzynskiy, AV Finkelstein, OV Galzitskaya Journal of molecular biology 336 (2), 509-525, 2004 | 80 | 2004 |
Library of disordered patterns in 3D protein structures MY Lobanov, EI Furletova, NS Bogatyreva, MA Roytberg, OV Galzitskaya PLoS Computational Biology 6 (10), e1000958, 2010 | 76 | 2010 |