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Gennady V. Semisotnov - Publications

Affiliations: 
Laboratory of Protein Physics Institute of Protein Research, Russian Academy of Sciences 
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39 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2022 Marchenkov V, Lekontseva N, Marchenko N, Kashparov I, Murina V, Nikulin A, Filimonov V, Semisotnov G. The Denaturant- and Mutation-Induced Disassembly of Hexameric Hfq Y55W Mutant. Molecules (Basel, Switzerland). 27. PMID 35744948 DOI: 10.3390/molecules27123821  0.319
2020 Marchenkov V, Gorokhovatsky A, Marchenko N, Ivashina T, Semisotnov G. Back to GroEL-Assisted Protein Folding: GroES Binding-Induced Displacement of Denatured Proteins from GroEL to Bulk Solution. Biomolecules. 10. PMID 31968530 DOI: 10.3390/biom10010162  0.34
2018 Marchenkov VV, Kotova NV, Muranova TA, Semisotnov GV. [Limited Trypsinolysis of GroES: The Effect on the Interaction with GroEL and Assembly In Vitro]. Molecular Biology. 52: 69-74. DOI: 10.1134/S0026893318010107  0.379
2016 Marchenkov VV, Marchenko NY, Kaysheva AL, Kotova NV, Kashparov IA, Semisotnov GV. Dataset concerning GroEL chaperonin interaction with proteins. Data in Brief. 6: 619-624. PMID 26909376 DOI: 10.1016/J.Dib.2016.01.008  0.365
2016 Marchenko NY, Sikorskaya EV, Marchenkov VV, Kashparov IA, Semisotnov GV. Affinity chromatography of chaperones based on denatured proteins: Analysis of cell lysates of different origin Protein Expression and Purification. 119: 117-123. PMID 26644295 DOI: 10.1016/J.Pep.2015.11.020  0.415
2015 Marchenko NY, Marchenkov VV, Semisotnov GV, Finkelstein AV. Strict experimental evidence that apo-chaperonin GroEL does not accelerate protein folding, although it does accelerate one of its steps. Proceedings of the National Academy of Sciences of the United States of America. PMID 26604318 DOI: 10.1073/Pnas.1517712112  0.302
2013 Ryabova NA, Marchenkov VV, Marchenkova SY, Kotova NV, Semisotnov GV. Molecular chaperone GroEL/ES: unfolding and refolding processes. Biochemistry. 78: 1405-1414. PMID 24490731 DOI: 10.1134/S0006297913130038  0.426
2013 Guryanov SG, Filimonov VV, Timchenko AA, Melnik BS, Kihara H, Kutyshenko VP, Ovchinnikov LP, Semisotnov GV. The major mRNP protein YB-1: structural and association properties in solution. Biochimica Et Biophysica Acta. 1834: 559-67. PMID 23220387 DOI: 10.1016/J.Bbapap.2012.11.007  0.453
2010 Samatova EN, Melnik BS, Balobanov VA, Katina NS, Dolgikh DA, Semisotnov GV, Finkelstein AV, Bychkova VE. Folding intermediate and folding nucleus for I-->N and U-->I-->N transitions in apomyoglobin: contributions by conserved and nonconserved residues. Biophysical Journal. 98: 1694-702. PMID 20409491 DOI: 10.1016/J.Bpj.2009.12.4326  0.4
2009 Marchenkov VV, Semisotnov GV. GroEL-assisted protein folding: does it occur within the chaperonin inner cavity? International Journal of Molecular Sciences. 10: 2066-83. PMID 19564940 DOI: 10.3390/Ijms10052066  0.44
2009 Gráczer É, Varga A, Melnik B, Semisotnov G, Závodszky P, Vas M. Symmetrical refolding of protein domains and subunits: Example of the dimeric two-domain 3-isopropylmalate dehydrogenases Biochemistry. 48: 1123-1134. PMID 19154118 DOI: 10.1021/Bi801857T  0.42
2009 Baryshnikova EN, Melnik BS, Balobanov VA, Katina NS, Finkelshtein AV, Semisotnov GV, Bychkova VE. On the role of some conserved and nonconserved amino acid residues in the transitional state and intermediate of apomyoglobin folding Molecular Biology. 43: 123-133. DOI: 10.1134/S0026893309010178  0.456
2008 Nikitina J, Shutova T, Melnik B, Chernyshov S, Marchenkov V, Semisotnov G, Klimov V, Samuelsson G. Importance of a single disulfide bond for the PsbO protein of photosystem II: protein structure stability and soluble overexpression in Escherichia coli. Photosynthesis Research. 98: 391-403. PMID 18709441 DOI: 10.1007/S11120-008-9327-9  0.426
2007 Gráczer É, Varga A, Hajdú I, Melnik B, Szilágyi A, Semisotnov G, Závodszky P, Vas M. Rates of unfolding, rather than refolding, determine thermal stabilities of thermophilic, mesophilic, and psychrotrophic 3-isopropylmalate dehydrogenases. Biochemistry. 46: 11536-11549. PMID 17887729 DOI: 10.1021/Bi700754Q  0.419
2007 Baryshnikova EN, Balobanov VA, Katina NS, Melnik BS, Dolgikh DA, Semisotnov GV, Bychkova VE. Equilibrium unfolding of mutant apomyoglobins carrying substitutions of conserved nonfunctional residues with alanine Molecular Biology. 41: 609-615. DOI: 10.1134/S0026893307040139  0.488
2006 Marchenko NY, Marchenkov VV, Kaysheva AL, Kashparov IA, Kotova NV, Kaliman PA, Semisotnov GV. Affinity chromatography of GroEL chaperonin based on denatured proteins: role of electrostatic interactions in regulation of GroEL affinity for protein substrates. Biochemistry. 71: 1357-1364. PMID 17223789 DOI: 10.1134/S000629790612011X  0.398
2005 Baryshnikova EN, Melnik BS, Finkelstein AV, Semisotnov GV, Bychkova VE. Three-state protein folding: experimental determination of free-energy profile. Protein Science : a Publication of the Protein Society. 14: 2658-67. PMID 16155199 DOI: 10.1110/Ps.051402705  0.459
2005 Kashparov IA, Semisotnov GV, Alakhov YB. Interaction of the N-Terminal and C-Terminal Domains of Elongation Factor G on Formation of Complexes with Guanyl Nucleotides Febs Journal. 118: 417-421. PMID 7285933 DOI: 10.1111/J.1432-1033.1981.Tb06418.X  0.308
2005 Baryshnikova EN, Melnik BS, Semisotnov GV, Bychkova VE. Folding/Unfolding Kinetics of Apomyoglobin Molecular Biology. 39: 884-891. DOI: 10.1007/S11008-005-0109-6  0.467
2004 Gorokhovatsky AY, Marchenkov VV, Rudenko NV, Ivashina TV, Ksenzenko VN, Burkhardt N, Semisotnov GV, Vinokurov LM, Alakhov YB. Fusion of Aequorea victoria GFP and aequorin provides their Ca(2+)-induced interaction that results in red shift of GFP absorption and efficient bioluminescence energy transfer. Biochemical and Biophysical Research Communications. 320: 703-11. PMID 15240105 DOI: 10.1016/J.Bbrc.2004.06.014  0.334
2003 Gorokhovatsky AY, Rudenko NV, Marchenkov VV, Skosyrev VS, Arzhanov MA, Burkhardt N, Zakharov MV, Semisotnov GV, Vinokurov LM, Alakhov YB. Homogeneous assay for biotin based on Aequorea victoria bioluminescence resonance energy transfer system. Analytical Biochemistry. 313: 68-75. PMID 12576060 DOI: 10.1016/S0003-2697(02)00514-6  0.32
2003 Vinokurov LM, Gorokhovatsky AY, Rudenko NV, Marchenkov VV, Skosyrev VS, Arzhanov MA, Zakharov MV, Burkhardt N, Semisotnov GV, Alakhov YB. Detection of protein-protein interactions using Aequorea victoria bioluminescence resonance energy transfer Biomedical Optics. 4967: 46-54. DOI: 10.1117/12.477881  0.4
2001 Szilágyi AN, Kotova NV, Semisotnov GV, Vas M. Incomplete refolding of a fragment of the N-terminal domain of pig muscle 3-phosphoglycerate kinase that lacks a subdomain. Comparison with refolding of the complementary C-terminal fragment. Febs Journal. 268: 1851-1860. DOI: 10.1046/J.1432-1327.2001.02060.X  0.337
2000 Timchenko AA, Melnik BS, Kihara H, Kimura K, Semisotnov GV. GroES co-chaperonin small-angle X-ray scattering study shows ring orifice increase in solution. Febs Letters. 471: 211-214. PMID 10767425 DOI: 10.1016/S0014-5793(00)01402-2  0.341
1998 Arai M, Ikura T, Semisotnov GV, Kihara H, Amemiya Y, Kuwajima K. Kinetic refolding of beta-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy. Journal of Molecular Biology. 275: 149-162. PMID 9451446 DOI: 10.1006/Jmbi.1997.1456  0.432
1997 Surin AK, Kotova NV, Kashparov IA, Marchenkov VV, Marchenkova SY, Semisotnov GV. Ligands regulate GroEL thermostability. Febs Letters. 405: 260-262. PMID 9108300 DOI: 10.1016/S0014-5793(97)00199-3  0.374
1996 Semisotnov GV, Kihara H, Kotova NV, Kimura K, Amemiya Y, Wakabayashi K, Serdyuk IN, Timchenko AA, Chiba K, Nikaido K, Ikura T, Kuwajima K. Protein globularization during folding. A study by synchrotron small-angle X-ray scattering Journal of Molecular Biology. 262: 559-574. PMID 8893863 DOI: 10.1006/Jmbi.1996.0535  0.475
1993 Kuwajima K, Semisotnov GV, Finkelstein AV, Sugai S, Ptitsyn OB. Secondary structure of globular proteins at the early and the final stages in protein folding. Febs Letters. 334: 265-8. PMID 8243629 DOI: 10.1016/0014-5793(93)80691-M  0.631
1992 Uversky VN, Semisotnov GV, Pain RH, Ptitsyn OB. 'All-or-none' mechanism of the molten globule unfolding. Febs Letters. 314: 89-92. PMID 1451808 DOI: 10.1016/0014-5793(92)81468-2  0.634
1991 Semisotnov GV, Rodionova NA, Razgulyaev OI, Uversky VN, Gripas' AF, Gilmanshin RI. Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers. 31: 119-28. PMID 2025683 DOI: 10.1002/Bip.360310111  0.552
1991 Semisotnov GV, Vas M, Chemeris VV, Kashparova NJ, Kotova NV, Razgulyaev OI, Sinev MA. Refolding kinetics of pig muscle and yeast 3-phosphoglycerate kinases and of their proteolytic fragments. Febs Journal. 202: 1083-1089. PMID 1765069 DOI: 10.1111/J.1432-1033.1991.Tb16474.X  0.377
1990 Vas M, Sinev MA, Kotova NV, Semisotnov GV. Reactivation of 3-phosphoglycerate kinase from its unfolded proteolytic fragments. Febs Journal. 189: 575-579. PMID 2351137 DOI: 10.1111/J.1432-1033.1990.Tb15525.X  0.324
1990 Ptitsyn OB, Pain RH, Semisotnov GV, Zerovnik E, Razgulyaev OI. Evidence for a molten globule state as a general intermediate in protein folding. Febs Letters. 262: 20-4. PMID 2318308 DOI: 10.1016/0014-5793(90)80143-7  0.635
1990 Semisotnov GV, Uversky VN, Sokolovsky IV, Gutin AM, Razgulyaev OI, Rodionova NA. Two slow stages in refolding of bovine carbonic anhydrase B are due to proline isomerization. Journal of Molecular Biology. 213: 561-8. PMID 2112610 DOI: 10.1016/S0022-2836(05)80215-3  0.531
1990 Goldberg ME, Semisotnov GV, Friguet B, Kuwajima K, Ptitsyn OB, Sugai S. An early immunoreactive folding intermediate of the tryptophan synthease beta 2 subunit is a 'molten globule'. Febs Letters. 263: 51-6. PMID 1691989 DOI: 10.1016/0014-5793(90)80703-L  0.612
1987 Semisotnov GV, Rodionova NA, Kutyshenko VP, Ebert B, Blanck J, Ptitsyn OB. Sequential mechanism of refolding of carbonic anhydrase B. Febs Letters. 224: 9-13. PMID 2824244 DOI: 10.1016/0014-5793(87)80412-X  0.588
1985 Dolgikh DA, Abaturov LV, Bolotina IA, Brazhnikov EV, Bychkova VE, Gilmanshin RI, Lebedev YuO, Semisotnov GV, Tiktopulo EI, Ptitsyn OB. Compact state of a protein molecule with pronounced small-scale mobility: bovine alpha-lactalbumin. European Biophysics Journal : Ebj. 13: 109-21. PMID 3843533 DOI: 10.1007/Bf00256531  0.607
1981 Dolgikh DA, Gilmanshin RI, Brazhnikov EV, Bychkova VE, Semisotnov GV, Venyaminov SYu, Ptitsyn OB. Alpha-Lactalbumin: compact state with fluctuating tertiary structure? Febs Letters. 136: 311-5. PMID 7327267 DOI: 10.1016/0014-5793(81)80642-4  0.65
1981 Semisotnov GV, Zikherman KK, Kasatkin SB, Ptitsyn OB, Anufrieva EV. Polarized luminescence and mobility of tryptophan residues in polypeptide chains Biopolymers. 20: 2287-2309. DOI: 10.1002/BIP.1981.360201102  0.487
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