Contact order revisited: influence of protein size on the folding rate DN Ivankov, SO Garbuzynskiy, E Alm, KW Plaxco, D Baker, AV Finkelstein Protein science 12 (9), 2057-2062, 2003 | 445 | 2003 |
FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence SO Garbuzynskiy, MY Lobanov, OV Galzitskaya Bioinformatics 26 (3), 326-332, 2010 | 424 | 2010 |
Prediction of amyloidogenic and disordered regions in protein chains OV Galzitskaya, SO Garbuzynskiy, MY Lobanov PLoS computational biology 2 (12), e177, 2006 | 212 | 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 |
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 | 104 | 2005 |
Golden triangle for folding rates of globular proteins SO Garbuzynskiy, DN Ivankov, NS Bogatyreva, AV Finkelstein Proceedings of the National Academy of Sciences 110 (1), 147-150, 2013 | 82 | 2013 |
Outlining folding nuclei in globular proteins SO Garbuzynskiy, AV Finkelstein, OV Galzitskaya Journal of molecular biology 336 (2), 509-525, 2004 | 79 | 2004 |
There and back again: Two views on the protein folding puzzle AV Finkelstein, AJ Badretdin, OV Galzitskaya, DN Ivankov, NS Bogatyreva, ... Physics of life reviews 21, 56-71, 2017 | 53 | 2017 |
Entropy capacity determines protein folding OV Galzitskaya, SO Garbuzynskiy Proteins: Structure, Function, and Bioinformatics 63 (1), 144-154, 2006 | 46 | 2006 |
More compact protein globules exhibit slower folding rates OV Galzitskaya, DC Reifsnyder, NS Bogatyreva, DN Ivankov, ... Proteins: Structure, Function, and Bioinformatics 70 (2), 329-332, 2008 | 45 | 2008 |
Is it possible to predict amyloidogenic regions from sequence alone? OV Galzitskaya, SO Garbuzynskiy, M YU. LOBANOV Journal of bioinformatics and computational biology 4 (02), 373-388, 2006 | 34 | 2006 |
ComSin: database of protein structures in bound (complex) and unbound (single) states in relation to their intrinsic disorder MY Lobanov, BA Shoemaker, SO Garbuzynskiy, JH Fong, AR Panchenko, ... Nucleic acids research 38 (suppl_1), D283-D287, 2010 | 33 | 2010 |
Backbone carbonyl group basicities are related to gas-phase fragmentation of peptides and protein folding MM Savitski, F Kjeldsen, ML Nielsen, SO Garbuzynskiy, OV Galzitskaya, ... Angewandte Chemie International Edition 46 (9), 1481-1484, 2007 | 33 | 2007 |
Restrictions to protein folding determined by the protein size AV Finkelstein, NS Bogatyreva, SO Garbuzynskiy FEBS letters 587 (13), 1884-1890, 2013 | 29 | 2013 |
Understanding the folding rates and folding nuclei of globular proteins AV Finkelstein, DN Ivankov, SO Garbuzynskiy, OV Galzitskaya Current Protein and Peptide Science 8 (6), 521-536, 2007 | 24 | 2007 |
Prediction of natively unfolded regions in protein chains OV Galzitskaya, SO Garbuzynskiy, MY Lobanov Molecular biology 40, 298-304, 2006 | 20 | 2006 |