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Sergiy Garbuzynskiy
Sergiy Garbuzynskiy
Institute of Protein Research, Russian Academy of Sciences
Verified email at phys.protres.ru
Title
Cited by
Cited by
Year
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
4412003
FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence
SO Garbuzynskiy, MY Lobanov, OV Galzitskaya
Bioinformatics 26 (3), 326-332, 2010
4202010
Prediction of amyloidogenic and disordered regions in protein chains
OV Galzitskaya, SO Garbuzynskiy, MY Lobanov
PLoS computational biology 2 (12), e177, 2006
2112006
FoldUnfold: web server for the prediction of disordered regions in protein chain
OV Galzitskaya, SO Garbuzynskiy, MY Lobanov
Bioinformatics 22 (23), 2948-2949, 2006
1972006
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
1842003
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
1362009
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
1102007
To be folded or to be unfolded?
SO Garbuzynskiy, MY Lobanov, OV Galzitskaya
Protein Science 13 (11), 2871-2877, 2004
1072004
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
1042005
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
812013
Outlining folding nuclei in globular proteins
SO Garbuzynskiy, AV Finkelstein, OV Galzitskaya
Journal of molecular biology 336 (2), 509-525, 2004
792004
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
522017
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
452008
Entropy capacity determines protein folding
OV Galzitskaya, SO Garbuzynskiy
Proteins: Structure, Function, and Bioinformatics 63 (1), 144-154, 2006
452006
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
342006
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
332010
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
332007
Restrictions to protein folding determined by the protein size
AV Finkelstein, NS Bogatyreva, SO Garbuzynskiy
FEBS letters 587 (13), 1884-1890, 2013
292013
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
242007
Prediction of natively unfolded regions in protein chains
OV Galzitskaya, SO Garbuzynskiy, MY Lobanov
Molecular biology 40, 298-304, 2006
202006
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