Year |
Citation |
Score |
2023 |
Anisenko A, Galkin S, Mikhaylov AA, Khrenova MG, Agapkina Y, Korolev S, Garkul L, Shirokova V, Ikonnikova VA, Korlyukov A, Dorovatovskii P, Baranov M, Gottikh M. KuINins as a New Class of HIV-1 Inhibitors That Block Post-Integration DNA Repair. International Journal of Molecular Sciences. 24. PMID 38139188 DOI: 10.3390/ijms242417354 |
0.42 |
|
2023 |
Kyriukha Y, Watkins MB, Redington JM, Dastvan R, Uversky VN, Hopkins J, Pozzi N, Korolev S. The PALB2 DNA-binding domain is an intrinsically disordered recombinase. Research Square. PMID 37790553 DOI: 10.21203/rs.3.rs-3235465/v1 |
0.541 |
|
2023 |
Kyriukha Y, Watkins MB, Redington JM, Dastvan R, Hopkins J, Pozzi N, Korolev S. The PALB2 DNA binding domain is an intrinsically disordered recombinase. Biorxiv : the Preprint Server For Biology. PMID 37333393 DOI: 10.1101/2023.06.01.543259 |
0.557 |
|
2021 |
Redington J, Deveryshetty J, Kanikkannan L, Miller I, Korolev S. Structural Insight into the Mechanism of PALB2 Interaction with MRG15. Genes. 12. PMID 34946951 DOI: 10.3390/genes12122002 |
0.379 |
|
2020 |
Shadrina O, Garanina I, Korolev S, Zatsepin T, Van Assche J, Daouad F, Wallet C, Rohr O, Gottikh M. Analysis of RNA binding properties of human Ku protein reveals its interactions with 7SK snRNA and protein components of 7SK snRNP complex. Biochimie. PMID 32105815 DOI: 10.1016/j.biochi.2020.02.016 |
0.371 |
|
2020 |
Koval VS, Arutyunyan AF, Salyanov VI, Kostyukov AA, Melkina OE, Zavilgelsky GB, Klimova RR, Kushch AA, Korolev SP, Agapkina YY, Gottikh MB, Vaiman AV, Rybalkina EY, Susova OY, Zhuze AL. DNA sequence-specific ligands. XVIII. Synthesis, physico-chemical properties; genetic, virological, and biochemical studies of fluorescent dimeric bisbenzimidazoles DBPA(n). Bioorganic & Medicinal Chemistry. 115378. PMID 32089391 DOI: 10.1016/j.bmc.2020.115378 |
0.36 |
|
2019 |
Deveryshetty J, Peterlini T, Ryzhikov M, Brahati N, Dellaire G, Masson JY, Korolev S. Novel RNA and DNA strand exchange activity of the PALB2 DNA Binding Domain and its critical role for DNA repair in cells. Elife. 8. PMID 31017574 DOI: 10.7554/Elife.44063 |
0.608 |
|
2019 |
Deveryshetty J, Peterlini T, Ryzhikov M, Brahiti N, Dellaire G, Masson J, Korolev S. Author response: Novel RNA and DNA strand exchange activity of the PALB2 DNA binding domain and its critical role for DNA repair in cells Elife. DOI: 10.7554/Elife.44063.033 |
0.578 |
|
2018 |
Malley KR, Koroleva O, Miller I, Sanishvili R, Jenkins CM, Gross RW, Korolev S. The structure of iPLAβ reveals dimeric active sites and suggests mechanisms of regulation and localization. Nature Communications. 9: 765. PMID 29472584 DOI: 10.1038/S41467-018-03193-0 |
0.392 |
|
2017 |
Korolev S. Advances in structural studies of recombination mediator proteins. Biophysical Chemistry. 225: 27-37. PMID 27974172 DOI: 10.1016/J.Bpc.2016.12.001 |
0.638 |
|
2016 |
Lu X, Malley KR, Brenner CC, Koroleva O, Korolev S, Downes BP. A MUB E2 structure reveals E1 selectivity between cognate ubiquitin E2s in eukaryotes. Nature Communications. 7: 12580. PMID 27550514 DOI: 10.1038/Ncomms12580 |
0.335 |
|
2014 |
Ryzhikov M, Gupta R, Glickman M, Korolev S. RecO protein initiates DNA recombination and strand annealing through two alternative DNA binding mechanisms. The Journal of Biological Chemistry. 289: 28846-55. PMID 25170075 DOI: 10.1074/Jbc.M114.585117 |
0.62 |
|
2014 |
Pandey KK, Bera S, Korolev S, Campbell M, Yin Z, Aihara H, Grandgenett DP. Rous sarcoma virus synaptic complex capable of concerted integration is kinetically trapped by human immunodeficiency virus integrase strand transfer inhibitors. The Journal of Biological Chemistry. 289: 19648-58. PMID 24872410 DOI: 10.1074/Jbc.M114.573311 |
0.336 |
|
2013 |
Hassan MI, Waheed A, Grubb JH, Klei HE, Korolev S, Sly WS. High resolution crystal structure of human β-glucuronidase reveals structural basis of lysosome targeting. Plos One. 8: e79687. PMID 24260279 DOI: 10.1371/Journal.Pone.0079687 |
0.348 |
|
2013 |
Gupta R, Ryzhikov M, Koroleva O, Unciuleac M, Shuman S, Korolev S, Glickman MS. A dual role for mycobacterial RecO in RecA-dependent homologous recombination and RecA-independent single-strand annealing. Nucleic Acids Research. 41: 2284-95. PMID 23295671 DOI: 10.1093/Nar/Gks1298 |
0.597 |
|
2012 |
Ryzhikov M, Korolev S. Structural studies of SSB interaction with RecO. Methods in Molecular Biology (Clifton, N.J.). 922: 123-31. PMID 22976180 DOI: 10.1007/978-1-62703-032-8_7 |
0.636 |
|
2012 |
Antony E, Weiland EA, Korolev S, Lohman TM. Plasmodium falciparum SSB tetramer wraps single-stranded DNA with similar topology but opposite polarity to E. coli SSB. Journal of Molecular Biology. 420: 269-83. PMID 22543099 DOI: 10.1016/J.Jmb.2012.04.021 |
0.636 |
|
2012 |
Jia H, Korolev S, Niedziela-Majka A, Maluf NK, Gauss GH, Myong S, Ha T, Waksman G, Lohman TM. Corrigendum to “Rotations of the 2B Sub-Domain of E. coli UvrD Helicase/Translocase Coupled to Nucleotide and DNA Binding” [J. Mol. Biol. 411/3 (2011) 633–648] Journal of Molecular Biology. 418: 264-265. DOI: 10.1016/J.Jmb.2012.02.030 |
0.451 |
|
2011 |
Zhou R, Kozlov AG, Roy R, Zhang J, Korolev S, Lohman TM, Ha T. SSB functions as a sliding platform that migrates on DNA via reptation. Cell. 146: 222-32. PMID 21784244 DOI: 10.1016/J.Cell.2011.06.036 |
0.577 |
|
2011 |
Jia H, Korolev S, Niedziela-Majka A, Maluf NK, Gauss GH, Myong S, Ha T, Waksman G, Lohman TM. Rotations of the 2B sub-domain of E. coli UvrD helicase/translocase coupled to nucleotide and DNA binding. Journal of Molecular Biology. 411: 633-48. PMID 21704638 DOI: 10.1016/J.Jmb.2011.06.019 |
0.574 |
|
2011 |
Ryzhikov M, Koroleva O, Postnov D, Tran A, Korolev S. Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein. Nucleic Acids Research. 39: 6305-14. PMID 21504984 DOI: 10.1093/Nar/Gkr199 |
0.561 |
|
2011 |
Zhou R, Kozlov AG, Roy R, Zhang J, Korolev S, Lohman TM, Ha T. Erratum: SSB functions as a sliding platform that migrates on DNA via reptation (Cell (2011) 146 (222-232)) Cell. 146. DOI: 10.1016/J.Cell.2011.07.027 |
0.478 |
|
2010 |
Grandgenett D, Korolev S. Retrovirus Integrase-DNA Structure Elucidates Concerted Integration Mechanisms. Viruses. 2: 1185-9. PMID 20882120 DOI: 10.3390/V2051185 |
0.497 |
|
2010 |
Korolev SP, Tashlitskiǐ VN, Smolov MA, Gromyko AV, Zhuze AL, Agapkina II, Gottikh MB. [HIV-1 integrase inhibition by dimeric bisbenzimidazoles having different spacers] Molekuliarnaia Biologiia. 44: 718-727. PMID 20873232 |
0.323 |
|
2010 |
Michel-Marks E, Courcelle CT, Korolev S, Courcelle J. ATP binding, ATP hydrolysis, and protein dimerization are required for RecF to catalyze an early step in the processing and recovery of replication forks disrupted by DNA damage. Journal of Molecular Biology. 401: 579-89. PMID 20558179 DOI: 10.1016/J.Jmb.2010.06.013 |
0.616 |
|
2010 |
Korolev SP, Tashlitsky VN, Smolov MA, Gromyko AV, Zhuze AL, Agapkina YY, Gottikh MB. HIV-1 integrase inhibition by dimeric bisbenzimidazoles with different spacer structures Molecular Biology. 44: 633-641. DOI: 10.1134/S0026893310040199 |
0.335 |
|
2010 |
Jia H, Niedziela-Majka A, Korolev S, Ha T, Lohman T. Fret Studies of the Conformational Changes in the 2b Sub-Domain of UvrD Helicase Biophysical Journal. 98: 23a. DOI: 10.1016/J.Bpj.2009.12.136 |
0.547 |
|
2009 |
Michel F, Crucifix C, Granger F, Eiler S, Mouscadet JF, Korolev S, Agapkina J, Ziganshin R, Gottikh M, Nazabal A, Emiliani S, Benarous R, Moras D, Schultz P, Ruff M. Structural basis for HIV-1 DNA integration in the human genome, role of the LEDGF/P75 cofactor. The Embo Journal. 28: 980-91. PMID 19229293 DOI: 10.1038/Emboj.2009.41 |
0.389 |
|
2009 |
Makharashvili N, Mi T, Koroleva O, Korolev S. RecR-mediated modulation of RecF dimer specificity for single- and double-stranded DNA. The Journal of Biological Chemistry. 284: 1425-34. PMID 19017635 DOI: 10.1074/Jbc.M806378200 |
0.756 |
|
2007 |
Gromyko AV, Salianov VI, Strel'tsov SA, Oleǐnikov VA, Korolev SP, Gottikh MB, Zhuze AL. DNA sequence-specific ligands: XIII. New Dimeric Hoechst 33258 molecules, inhibitors of HIV-1 integrase in vitro Bioorganicheskaia Khimiia. 33: 613-623. PMID 18173124 DOI: 10.1134/S1068162007060064 |
0.46 |
|
2007 |
Scaglione KM, Bansal PK, Deffenbaugh AE, Kiss A, Moore JM, Korolev S, Cocklin R, Goebl M, Kitagawa K, Skowyra D. SCF E3-mediated autoubiquitination negatively regulates activity of Cdc34 E2 but plays a nonessential role in the catalytic cycle in vitro and in vivo. Molecular and Cellular Biology. 27: 5860-70. PMID 17562869 DOI: 10.1128/Mcb.01555-06 |
0.325 |
|
2007 |
Koroleva O, Makharashvili N, Courcelle CT, Courcelle J, Korolev S. Structural conservation of RecF and Rad50: implications for DNA recognition and RecF function. The Embo Journal. 26: 867-77. PMID 17255941 DOI: 10.1038/Sj.Emboj.7601537 |
0.764 |
|
2006 |
Smolov M, Gottikh M, Tashlitskii V, Korolev S, Demidyuk I, Brochon JC, Mouscadet JF, Deprez E. Kinetic study of the HIV-1 DNA 3′-end processing: Single-turnover property of integrase Febs Journal. 273: 1137-1151. PMID 16519680 DOI: 10.1111/j.1742-4658.2006.05139.x |
0.387 |
|
2005 |
Zhang R, Minh T, Lezondra L, Korolev S, Moy SF, Collart F, Joachimiak A. 1.6 Å crystal structure of YteR protein from Bacillus subtilis, a predicted lyase Proteins: Structure, Function and Genetics. 60: 561-565. PMID 15906318 DOI: 10.1002/Prot.20410 |
0.44 |
|
2005 |
Lubman OY, Kopan R, Waksman G, Korolev S. The crystal structure of a partial mouse Notch-1 ankyrin domain: repeats 4 through 7 preserve an ankyrin fold. Protein Science : a Publication of the Protein Society. 14: 1274-81. PMID 15802643 DOI: 10.1110/Ps.041184105 |
0.439 |
|
2005 |
Singh S, Korolev S, Koroleva O, Zarembinski T, Collart F, Joachimiak A, Christendat D. Crystal structure of a novel shikimate dehydrogenase from Haemophilus influenzae. The Journal of Biological Chemistry. 280: 17101-8. PMID 15735308 DOI: 10.1074/Jbc.M412753200 |
0.339 |
|
2005 |
Cuff ME, Miller DJ, Korolev S, Xu X, Anderson WF, Edwards A, Joachimiak A, Savchenko A. Crystal structure of a predicted precorrin-8x methylmutase from Thermoplasma acidophilum. Proteins. 58: 751-4. PMID 15609338 DOI: 10.1002/Prot.20022 |
0.328 |
|
2004 |
Makharashvili N, Koroleva O, Bera S, Grandgenett DP, Korolev S. A novel structure of DNA repair protein RecO from Deinococcus radiodurans. Structure (London, England : 1993). 12: 1881-9. PMID 15458636 DOI: 10.1016/J.Str.2004.08.006 |
0.763 |
|
2003 |
Korolev S, Pinelis D, Savransky V, Komisar J, Vogel P, Fegeding K. Toxicity of the staphylococcal enterotoxin B mutants with histidine-to-tyrosine substitutions. Toxicology. 187: 229-38. PMID 12699911 DOI: 10.1016/S0300-483X(03)00049-0 |
0.347 |
|
2003 |
Lohman TM, Hsieh J, Maluf NK, Cheng W, Lucius AL, Fischer CJ, Brendza KM, Korolev S, Waksman G. DNA helicases, motors that move along nucleic acids: Lessons from the SF1 helicase superfamily Enzymes. 23: 303-369,III-VII. DOI: 10.1016/S1874-6047(04)80008-8 |
0.579 |
|
2002 |
Korolev S, Koroleva O, Petterson K, Gu M, Collart F, Dementieva I, Joachimiak A. Autotracing of Escherichia coli acetate CoA-transferase α-subunit structure using 3.4 Å MAD and 1.9 Å native data Acta Crystallographica Section D-Biological Crystallography. 58: 2116-2121. PMID 12454473 DOI: 10.1107/S0907444902017055 |
0.38 |
|
2002 |
Cheng W, Brendza KM, Gauss GH, Korolev S, Waksman G, Lohman TM. The 2B domain of the Escherichia coli Rep protein is not required for DNA helicase activity. Proceedings of the National Academy of Sciences of the United States of America. 99: 16006-11. PMID 12441398 DOI: 10.1073/Pnas.242479399 |
0.617 |
|
2002 |
Korolev S, Skarina T, Evdokimova E, Beasley S, Edwards A, Joachimiak A, Savchenko A. Crystal structure of glutamine amidotransferase from Thermotoga maritima Proteins. 49: 420-422. PMID 12360532 DOI: 10.1002/Prot.10161 |
0.404 |
|
2002 |
Yeo HJ, Ziegelin G, Korolev S, Calendar R, Lanka E, Waksman G. Phage P4 origin-binding domain structure reveals a mechanism for regulation of DNA-binding activity by homo- and heterodimerization of winged helix proteins. Molecular Microbiology. 43: 855-67. PMID 11929537 DOI: 10.1046/J.1365-2958.2002.02796.X |
0.528 |
|
2002 |
Bochkareva E, Korolev S, Lees-Miller SP, Bochkarev A. Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA. The Embo Journal. 21: 1855-63. PMID 11927569 DOI: 10.1093/Emboj/21.7.1855 |
0.581 |
|
2002 |
Korolev S, Ikeguchi Y, Skarina T, Beasley S, Arrowsmith C, Edwards A, Joachimiak A, Pegg AE, Savchenko A. The crystal structure of spermidine synthase with a multisubstrate adduct inhibitor. Nature Structural Biology. 9: 27-31. PMID 11731804 DOI: 10.1038/Nsb737 |
0.437 |
|
2002 |
Bochkarev A, Bochkareva E, Korolev S. Structure of the RPA trimerization core Acta Crystallographica Section A. 58: 273-273. DOI: 10.1107/S0108767302095910 |
0.328 |
|
2001 |
Korolev S, Dementieva I, Sanishvili R, Minor W, Otwinowski Z, Joachimiak A. Using surface-bound rubidium ions for protein phasing Acta Crystallographica Section D-Biological Crystallography. 57: 1008-1012. PMID 11418770 DOI: 10.1107/S0907444901007302 |
0.341 |
|
2001 |
Bochkareva E, Belegu V, Korolev S, Bochkarev A. Structure of the major single-stranded DNA-binding domain of replication protein A suggests a dynamic mechanism for DNA binding. The Embo Journal. 20: 612-8. PMID 11157767 DOI: 10.1093/Emboj/20.3.612 |
0.638 |
|
2000 |
Bochkareva E, Korolev S, Bochkarev A. The role for zinc in replication protein A. The Journal of Biological Chemistry. 275: 27332-8. PMID 10856290 DOI: 10.1074/Jbc.M000620200 |
0.563 |
|
1999 |
Lu D, Fütterer K, Korolev S, Zheng X, Tan K, Waksman G, Sadler JE. Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide Journal of Molecular Biology. 292: 361-373. PMID 10493881 DOI: 10.1006/Jmbi.1999.3089 |
0.343 |
|
1998 |
Li Y, Korolev S, Waksman G. Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: Structural basis for nucleotide incorporation Embo Journal. 17: 7514-7525. PMID 9857206 DOI: 10.1093/Emboj/17.24.7514 |
0.57 |
|
1998 |
Bhatnagar RS, Fütterer K, Farazi TA, Korolev S, Murray CL, Jackson-Machelski E, Gokel GW, Gordon JI, Waksman G. Structure of N-myristoyltransferase with bound myristoylCoA and peptide substrate analogs. Nature Structural Biology. 5: 1091-7. PMID 9846880 DOI: 10.1038/4202 |
0.334 |
|
1998 |
Li Y, Kong Y, Korolev S, Waksman G. Crystal structures of the Klenow fragment of Thermus aquaticus DNA polymerase I complexed with deoxyribonucleoside triphosphates Protein Science. 7: 1116-1123. PMID 9605316 DOI: 10.1002/Pro.5560070505 |
0.566 |
|
1998 |
Korolev S, Yao N, Lohman TM, Weber PC, Waksman G. Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super-families of helicases. Protein Science : a Publication of the Protein Society. 7: 605-10. PMID 9541392 DOI: 10.1002/Pro.5560070309 |
0.406 |
|
1997 |
Korolev S, Hsieh J, Gauss GH, Lohman TM, Waksman G. Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell. 90: 635-47. PMID 9288744 DOI: 10.1016/S0092-8674(00)80525-5 |
0.628 |
|
1996 |
Korolev S, Nayal M, Barnes WM, Di Cera E, Waksman G. Crystal structure of Klenow-analogous fragment ofThermus aquaticusDNA polymerase I at 2.5 Å resolution Acta Crystallographica Section a Foundations of Crystallography. 52: C156-C156. DOI: 10.1107/S0108767396092987 |
0.34 |
|
1995 |
Korolev S, Nayal M, Barnes WM, Di Cera E, Waksman G. Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5-Å resolution: Structural basis for thermostability Proceedings of the National Academy of Sciences of the United States of America. 92: 9264-9268. PMID 7568114 DOI: 10.1073/Pnas.92.20.9264 |
0.579 |
|
1993 |
Makarov A, Protasevich I, Kuznetsova N, Fedorov B, Korolev S, Struminskaya N, Leshchinskaya I, Yakovlev G, Esipova N. Comparative study of thermostability and structure of close homologs – barnase and binase Studies in Organic Chemistry. 47: 377-382. DOI: 10.1016/B978-0-444-89372-7.50049-X |
0.339 |
|
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