| Year |
Citation |
Score |
| 2023 |
Gupta A, Kumar A, Singh N, Patel M, Studitsky VM, Zhang KYJ, Akhtar S. The Ser7 of RNA Pol II-CTD influences the recruitment of Cdc73 for mRNA transcription. International Journal of Biological Macromolecules. 127881. PMID 37944716 DOI: 10.1016/j.ijbiomac.2023.127881 |
0.346 |
|
| 2023 |
Maluchenko N, Saulina A, Geraskina O, Kotova E, Korovina A, Feofanov A, Studitsky V. Zinc-dependent Nucleosome Reorganization by PARP2. Biorxiv : the Preprint Server For Biology. PMID 37904948 DOI: 10.1101/2023.10.17.562808 |
0.353 |
|
| 2023 |
Oleinikov PD, Fedulova AS, Armeev GA, Motorin NA, Singh-Palchevskaia L, Sivkina AL, Feskin PG, Glukhov GS, Afonin DA, Komarova GA, Kirpichnikov MP, Studitsky VM, Feofanov AV, Shaytan AK. Interactions of Nucleosomes with Acidic Patch-Binding Peptides: A Combined Structural Bioinformatics, Molecular Modeling, Fluorescence Polarization, and Single-Molecule FRET Study. International Journal of Molecular Sciences. 24. PMID 37894874 DOI: 10.3390/ijms242015194 |
0.309 |
|
| 2023 |
Gupta A, Kumar A, Singh N, Sudarshan N, Studitsky VM, Zhang KYJ, Akhtar MS. The Saccharomyces cerevisiae SR protein Npl3 interacts with hyperphosphorylated CTD of RNA Polymerase II. International Journal of Biological Macromolecules. 253: 127541. PMID 37858651 DOI: 10.1016/j.ijbiomac.2023.127541 |
0.311 |
|
| 2023 |
Andreeva TV, Maluchenko NV, Efremenko AV, Lyubitelev AV, Korovina AN, Afonin DA, Kirpichnikov MP, Studitsky VM, Feofanov AV. Epigallocatechin Gallate Affects the Structure of Chromatosomes, Nucleosomes and Their Complexes with PARP1. International Journal of Molecular Sciences. 24. PMID 37762491 DOI: 10.3390/ijms241814187 |
0.516 |
|
| 2023 |
Stefanova ME, Volokh OI, Chertkov OV, Armeev GA, Shaytan AK, Feofanov AV, Kirpichnikov MP, Sokolova OS, Studitsky VM. Structure and Dynamics of Compact Dinucleosomes: Analysis by Electron Microscopy and spFRET. International Journal of Molecular Sciences. 24. PMID 37569503 DOI: 10.3390/ijms241512127 |
0.411 |
|
| 2023 |
Gerasimova NS, Pestov NA, Studitsky VM. Role of Histone Tails and Single Strand DNA Breaks in Nucleosomal Arrest of RNA Polymerase. International Journal of Molecular Sciences. 24. PMID 36768621 DOI: 10.3390/ijms24032295 |
0.557 |
|
| 2022 |
Volokh OI, Sivkina AL, Moiseenko AV, Popinako AV, Karlova MG, Valieva ME, Kotova EY, Kirpichnikov MP, Formosa T, Studitsky VM, Sokolova OS. Mechanism of curaxin-dependent nucleosome unfolding by FACT. Frontiers in Molecular Biosciences. 9: 1048117. PMID 36483541 DOI: 10.3389/fmolb.2022.1048117 |
0.457 |
|
| 2022 |
Maluchenko N, Koshkina D, Korovina A, Studitsky V, Feofanov A. Interactions of PARP1 Inhibitors with PARP1-Nucleosome Complexes. Cells. 11. PMID 36359739 DOI: 10.3390/cells11213343 |
0.426 |
|
| 2022 |
Malinina DK, Sivkina AL, Korovina AN, McCullough LL, Formosa T, Kirpichnikov MP, Studitsky VM, Feofanov AV. Hmo1 Protein Affects the Nucleosome Structure and Supports the Nucleosome Reorganization Activity of Yeast FACT. Cells. 11. PMID 36230893 DOI: 10.3390/cells11192931 |
0.485 |
|
| 2022 |
Gerasimova NS, Volokh OI, Pestov NA, Armeev GA, Kirpichnikov MP, Shaytan AK, Sokolova OS, Studitsky VM. Structure of an Intranucleosomal DNA Loop That Senses DNA Damage during Transcription. Cells. 11. PMID 36078089 DOI: 10.3390/cells11172678 |
0.549 |
|
| 2022 |
Chang HW, Feofanov AV, Lyubitelev AV, Armeev GA, Kotova EY, Hsieh FK, Kirpichnikov MP, Shaytan AK, Studitsky VM. N-Terminal Tails of Histones H2A and H2B Differentially Affect Transcription by RNA Polymerase II In Vitro. Cells. 11. PMID 36010552 DOI: 10.3390/cells11162475 |
0.565 |
|
| 2022 |
Kotova EY, Hsieh FK, Chang HW, Maluchenko NV, Langelier MF, Pascal JM, Luse DS, Feofanov AV, Studitsky VM. Human PARP1 Facilitates Transcription through a Nucleosome and Histone Displacement by Pol II In Vitro. International Journal of Molecular Sciences. 23. PMID 35806109 DOI: 10.3390/ijms23137107 |
0.621 |
|
| 2022 |
Andreeva TV, Maluchenko NV, Sivkina AL, Chertkov OV, Valieva ME, Kotova EY, Kirpichnikov MP, Studitsky VM, Feofanov AV. Na and K Ions Differently Affect Nucleosome Structure, Stability, and Interactions with Proteins. Microscopy and Microanalysis : the Official Journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada. 28: 243-253. PMID 35177143 DOI: 10.1017/S1431927621013751 |
0.31 |
|
| 2022 |
Singh N, Asalam M, Ansari MO, Gerasimova NS, Studitsky VM, Akhtar MS. Transcription by RNA polymerase II and the CTD-chromatin crosstalk. Biochemical and Biophysical Research Communications. 599: 81-86. PMID 35176629 DOI: 10.1016/j.bbrc.2022.02.039 |
0.549 |
|
| 2022 |
Sivkina AL, Karlova MG, Valieva ME, McCullough LL, Formosa T, Shaytan AK, Feofanov AV, Kirpichnikov MP, Sokolova OS, Studitsky VM. Electron microscopy analysis of ATP-independent nucleosome unfolding by FACT. Communications Biology. 5: 2. PMID 35013515 DOI: 10.1038/s42003-021-02948-8 |
0.434 |
|
| 2021 |
Maluchenko NV, Nilov DK, Pushkarev SV, Kotova EY, Gerasimova NS, Kirpichnikov MP, Langelier MF, Pascal JM, Akhtar MS, Feofanov AV, Studitsky VM. Mechanisms of Nucleosome Reorganization by PARP1. International Journal of Molecular Sciences. 22. PMID 34830005 DOI: 10.3390/ijms222212127 |
0.515 |
|
| 2020 |
Nilov D, Maluchenko N, Kurgina T, Pushkarev S, Lys A, Kutuzov M, Gerasimova N, Feofanov A, Švedas V, Lavrik O, Studitsky VM. Molecular Mechanisms of PARP-1 Inhibitor 7-Methylguanine. International Journal of Molecular Sciences. 21. PMID 32245127 DOI: 10.3390/Ijms21062159 |
0.434 |
|
| 2020 |
Nizovtseva EV, Polikanov YS, Kulaeva OI, Clauvelin N, Postnikov YV, Olson WK, Studitsky VM. [Opposite Effects of Histone H1 and HMGN5 Protein on Distant Interactions in Chromatin]. Molekuliarnaia Biologiia. 53: 1038-1048. PMID 31876282 DOI: 10.1134/S002689331906013X |
0.505 |
|
| 2020 |
Andreeva T, Maluchenko N, Chertkov O, Studitsky V, Feofanov A, Kirpichnikov M. Length of DNA Linker Affects Nucleosomal DNA Structure Microscopy and Microanalysis. 1-3. DOI: 10.1017/S1431927620017948 |
0.466 |
|
| 2019 |
Maluchenko NV, Sultanov DS, Kotova EY, Kirpichnikov MP, Studitsky VM, Feofanov AV. Histone tails promote PARP1-dependent structural rearrangements in nucleosomes Doklady Biochemistry and Biophysics. 489: 377-379. PMID 32130604 DOI: 10.1134/S1607672919060061 |
0.555 |
|
| 2019 |
Chang HW, Nizovtseva EV, Razin SV, Formosa T, Gurova KV, Studitsky VM. Histone Chaperone FACT and Curaxins: Effects on Genome Structure and Function. Journal of Cancer Metastasis and Treatment. 5. PMID 31853507 DOI: 10.20517/2394-4722.2019.31 |
0.492 |
|
| 2019 |
Kantidze OL, Luzhin AV, Nizovtseva EV, Safina A, Valieva ME, Golov AK, Velichko AK, Lyubitelev AV, Feofanov AV, Gurova KV, Studitsky VM, Razin SV. The anti-cancer drugs curaxins target spatial genome organization. Nature Communications. 10: 1441. PMID 30926878 DOI: 10.1038/S41467-019-09500-7 |
0.381 |
|
| 2019 |
Chang HW, Hsieh FK, Patel SS, Studitsky VM. Time-Resolved Analysis of Transcription through Chromatin. Methods (San Diego, Calif.). PMID 30707952 DOI: 10.1016/J.Ymeth.2019.01.016 |
0.611 |
|
| 2019 |
Malyuchenko NV, Kotova EY, Kirpichnikov MP, Studitsky VM, Feofanov AV. PARP1 Binding to DNA Breaks and Hairpins Alters Nucleosome Structure Moscow University Biological Sciences Bulletin. 74: 158-162. DOI: 10.3103/S0096392519030076 |
0.462 |
|
| 2019 |
Maluchenko N, Feofanov A, Kirpichnikov M, Studitsky V, Gerasimova N. Abstract P-18: PARP1-Induced Structural Rearrangements are Enhanced in Cisplatin-Treated Nucleosomes International Journal of Biomedicine. 9. DOI: 10.21103/Ijbm.9.Suppl_1.P18 |
0.33 |
|
| 2019 |
Chertkov OV, Karlova MG, Studitsky VM, Sokolova OS. The Three-Dimensional Structure of (+39) RNA-Polymerase Elongation Complex Determined by Cryo-Electron Microscopy Microscopy and Microanalysis. 25: 1332-1333. DOI: 10.1017/S1431927619007396 |
0.385 |
|
| 2019 |
Maluchenko N, Nilov D, Feofanov A, Lys A, Kutuzov M, Gerasimova N, Studitsky V. 7-Methylguanine Traps PARP-1 on Nucleosomes: spFRET Microscopy Study Microscopy and Microanalysis. 25: 1282-1283. DOI: 10.1017/S1431927619007141 |
0.393 |
|
| 2018 |
Chang HW, Valieva ME, Safina A, Chereji RV, Wang J, Kulaeva OI, Morozov AV, Kirpichnikov MP, Feofanov AV, Gurova KV, Studitsky VM. Mechanism of FACT removal from transcribed genes by anticancer drugs curaxins. Science Advances. 4: eaav2131. PMID 30417101 DOI: 10.1126/Sciadv.Aav2131 |
0.528 |
|
| 2018 |
Shaytan AK, Xiao H, Armeev GA, Gaykalova DA, Komarova GA, Wu C, Studitsky VM, Landsman D, Panchenko AR. Structural interpretation of DNA-protein hydroxyl-radical footprinting experiments with high resolution using HYDROID. Nature Protocols. PMID 30341436 DOI: 10.1038/S41596-018-0048-Z |
0.428 |
|
| 2018 |
Gurova K, Chang HW, Valieva ME, Sandlesh P, Studitsky VM. Structure and function of the histone chaperone FACT - Resolving FACTual issues. Biochimica Et Biophysica Acta. PMID 30055319 DOI: 10.1016/J.Bbagrm.2018.07.008 |
0.432 |
|
| 2018 |
McCullough LL, Connell Z, Xin H, Studitsky VM, Feofanov AV, Valieva ME, Formosa T. Functional roles of the DNA-binding HMGB domain in the histone chaperone FACT in nucleosome reorganization. The Journal of Biological Chemistry. PMID 29514976 DOI: 10.1074/Jbc.Ra117.000199 |
0.545 |
|
| 2018 |
Feofanov AV, Andreeva TV, Studitsky VM, Kirpichnikov MP. Reversibility of Structural Rearrangements in Mononucleosomes Induced by Ionic Strength Moscow University Biological Sciences Bulletin. 73: 157-161. DOI: 10.3103/S0096392518030070 |
0.433 |
|
| 2018 |
Gerasimov ES, Gerasimova NS, Kozlova AL, Studitsky VM. Yeast Protein Nhp6A Binds to Short GC-Rich Genes Moscow University Biological Sciences Bulletin. 73: 88-91. DOI: 10.3103/S0096392518020013 |
0.427 |
|
| 2018 |
Kozlova AL, Valieva ME, Maluchenko NV, Studitsky VM. HMGB Proteins as DNA Chaperones That Modulate Chromatin Activity Molecular Biology. 52: 637-647. DOI: 10.1134/S0026893318050096 |
0.574 |
|
| 2018 |
Armeev GA, Lubitelev AV, Studitsky VM, Feofanov AV, Kirpichnikov MP. spFRET Microscopy Analysis of Distances Between DNA Linkers in Mononucleosomes Microscopy and Microanalysis. 24: 1394-1395. DOI: 10.1017/S1431927618007456 |
0.417 |
|
| 2017 |
Sultanov DC, Gerasimova NS, Kudryashova KS, Maluchenko NV, Kotova EY, Langelier MF, Pascal JM, Kirpichnikov MP, Feofanov AV, Studitsky VM. Unfolding of core nucleosomes by PARP-1 revealed by spFRET microscopy. Aims Genetics. 4: 21-31. PMID 28804761 DOI: 10.3934/genet.2017.1.21 |
0.522 |
|
| 2017 |
Nizovtseva EV, Todolli S, Olson WK, Studitsky VM. Towards quantitative analysis of gene regulation by enhancers. Epigenomics. PMID 28799793 DOI: 10.2217/Epi-2017-0061 |
0.487 |
|
| 2017 |
Chang HW, Studitsky VM. Chromatin replication: TRANSmitting the histone code. Journal of Nature and Science. 3. PMID 28393112 |
0.457 |
|
| 2017 |
Valieva ME, Gerasimova NS, Kudryashova KS, Kozlova AL, Kirpichnikov MP, Hu Q, Botuyan MV, Mer G, Feofanov AV, Studitsky VM. Stabilization of Nucleosomes by Histone Tails and by FACT Revealed by spFRET Microscopy. Cancers. 9. PMID 28067802 DOI: 10.3390/Cancers9010003 |
0.543 |
|
| 2017 |
Hsieh FK, Kozlova AL, Gerasimova NS, Kotova EY, Formosa T, Studitsky VM. Role of the Nhp6 Protein in In Vitro Transcription through the Nucleosome Moscow University Biological Sciences Bulletin. 72: 218-221. DOI: 10.3103/S009639251704006X |
0.621 |
|
| 2017 |
Lyubitelev AV, Studitsky VM, Feofanov AV, Kirpichnikov MP. Effect of sodium and potassium ions on conformation of linker parts of nucleosomes Moscow University Biological Sciences Bulletin. 72: 146-150. DOI: 10.3103/S0096392517030075 |
0.478 |
|
| 2017 |
Karlova MG, Volokh OI, Chertkov OV, Kirpichnikov MP, Studitsky VM, Sokolova OS. Purification and concentration of RNA polymerase on Ni-lipid monolayers Russian Journal of Bioorganic Chemistry. 43: 658-663. DOI: 10.1134/S1068162017060048 |
0.469 |
|
| 2016 |
Nizovtseva EV, Clauvelin N, Todolli S, Polikanov YS, Kulaeva OI, Wengrzynek S, Olson WK, Studitsky VM. Nucleosome-free DNA regions differentially affect distant communication in chromatin. Nucleic Acids Research. PMID 27940560 DOI: 10.1093/Nar/Gkw1240 |
0.551 |
|
| 2016 |
Chang HW, Pandey M, Kulaeva OI, Patel SS, Studitsky VM. Overcoming a nucleosomal barrier to replication. Science Advances. 2: e1601865. PMID 27847876 DOI: 10.1126/Sciadv.1601865 |
0.565 |
|
| 2016 |
Valieva ME, Armeev GA, Kudryashova KS, Gerasimova NS, Shaytan AK, Kulaeva OI, McCullough LL, Formosa T, Georgiev PG, Kirpichnikov MP, Studitsky VM, Feofanov AV. Large-scale ATP-independent nucleosome unfolding by a histone chaperone. Nature Structural & Molecular Biology. PMID 27820806 DOI: 10.1038/Nsmb.3321 |
0.575 |
|
| 2016 |
Studitsky VM, Nizovtseva EV, Shaytan AK, Luse DS. Nucleosomal Barrier to Transcription: Structural Determinants and Changes in Chromatin Structure. Biochemistry & Molecular Biology Journal. 2. PMID 27754494 DOI: 10.21767/2471-8084.100017 |
0.616 |
|
| 2016 |
Gerasimova NS, Pestov NA, Kulaeva OI, Clark DJ, Studitsky VM. Transcription-induced DNA supercoiling: New roles of intranucleosomal DNA loops in DNA repair and transcription. Transcription. 0. PMID 27115204 DOI: 10.1080/21541264.2016.1182240 |
0.525 |
|
| 2016 |
Gross S, Kotova EY, Maluchenko NV, Pascal JM, Studitsky VM. Evaluating Parp1 domains as gossypol targets Moscow University Biological Sciences Bulletin. 71: 235-239. DOI: 10.3103/S0096392516040106 |
0.379 |
|
| 2016 |
Valieva ME, Feofanov AV, Studitsky VM. Histone chaperones: Variety and functions Moscow University Biological Sciences Bulletin. 71: 165-169. DOI: 10.3103/S0096392516030123 |
0.618 |
|
| 2016 |
Lyubitelev AV, Kudryashova KS, Mikhaylova MS, Malyuchenko NV, Chertkov OV, Studitsky VM, Feofanov AV, Kirpichnikov MP. Change in linker DNA conformation upon histone H1.5 binding to nucleosome: Fluorescent microscopy of single complexes Moscow University Biological Sciences Bulletin. 71: 108-113. DOI: 10.3103/S0096392516020061 |
0.502 |
|
| 2016 |
Gerasimova NS, Studitsky VM. Hydroxyl radical footprinting of fluorescently labeled DNA Moscow University Biological Sciences Bulletin. 71: 93-96. DOI: 10.3103/S0096392516020036 |
0.307 |
|
| 2016 |
Volokh OI, Hsieh FK, Karlova MG, Trifonova ES, Studitsky VM, Sokolova OS. Study of RNA polymerase transcription through nucleosome using the cryo-electron microscopy approach Moscow University Biological Sciences Bulletin. 71: 34-38. DOI: 10.3103/S0096392516010120 |
0.453 |
|
| 2016 |
Volokh OI, Derkacheva NI, Studitsky VM, Sokolova OS. Structural studies of chromatin remodeling factors Molecular Biology. 50: 812-822. DOI: 10.1134/S0026893316060212 |
0.388 |
|
| 2016 |
Lyubitelev AV, Nikitin DV, Shaytan AK, Studitsky VM, Kirpichnikov MP. Structure and functions of linker histones Biochemistry (Moscow). 81: 213-223. DOI: 10.1134/S0006297916030032 |
0.498 |
|
| 2015 |
Bondarenko MT, Maluchenko NV, Valieva ME, Gerasimova NS, Kulaeva OI, Georgiev PG, Studitsky VM. [Structure and function of histone chaperone FACT]. Molekuliarnaia Biologiia. 49: 891-904. PMID 26710768 DOI: 10.7868/S0026898415060026 |
0.642 |
|
| 2015 |
Pestov NA, Gerasimova NS, Kulaeva OI, Studitsky VM. Structure of transcribed chromatin is a sensor of DNA damage. Science Advances. 1: e1500021. PMID 26601207 DOI: 10.1126/Sciadv.1500021 |
0.603 |
|
| 2015 |
Gaykalova DA, Kulaeva OI, Volokh O, Shaytan AK, Hsieh FK, Kirpichnikov MP, Sokolova OS, Studitsky VM. Structural analysis of nucleosomal barrier to transcription. Proceedings of the National Academy of Sciences of the United States of America. 112: E5787-95. PMID 26460019 DOI: 10.1073/Pnas.1508371112 |
0.676 |
|
| 2015 |
Kudryashova KS, Chertkov OV, Nikitin DV, Pestov NA, Kulaeva OI, Efremenko AV, Solonin AS, Kirpichnikov MP, Studitsky VM, Feofanov AV. Preparation of mononucleosomal templates for analysis of transcription with RNA polymerase using spFRET. Methods in Molecular Biology (Clifton, N.J.). 1288: 395-412. PMID 25827893 DOI: 10.1007/978-1-4939-2474-5_23 |
0.607 |
|
| 2015 |
Kulaeva OI, Studitsky VM. Preparation and analysis of positioned mononucleosomes. Methods in Molecular Biology (Clifton, N.J.). 1288: 15-26. PMID 25827872 DOI: 10.1007/978-1-4939-2474-5_2 |
0.571 |
|
| 2015 |
Hsieh FK, Kulaeva OI, Studitsky VM. Experimental analysis of hFACT action during Pol II transcription in vitro. Methods in Molecular Biology (Clifton, N.J.). 1276: 315-26. PMID 25665573 DOI: 10.1007/978-1-4939-2392-2_19 |
0.597 |
|
| 2015 |
Clauvelin N, Lo P, Kulaeva OI, Nizovtseva EV, Diaz-Montes J, Zola J, Parashar M, Studitsky VM, Olson WK. Nucleosome positioning and composition modulate in silico chromatin flexibility. Journal of Physics. Condensed Matter : An Institute of Physics Journal. 27: 064112. PMID 25564155 DOI: 10.1088/0953-8984/27/6/064112 |
0.52 |
|
| 2015 |
Kudryashova KS, Nikitin DV, Chertkov OV, Gerasimova NS, Valieva ME, Studitsky VM, Feofanov AV. Development of fluorescently labeled mononucleosomes for the investigation of transcription mechanisms by single complex microscopy Moscow University Biological Sciences Bulletin. 70: 189-193. DOI: 10.3103/S0096392515040069 |
0.586 |
|
| 2015 |
Gerasimova NS, Pestov NA, Kulaeva OI, Nikitin DV, Kirpichnikov MP, Studitsky VM. Repair of chromatinized DNA Moscow University Biological Sciences Bulletin. 70: 122-126. DOI: 10.3103/S0096392515030050 |
0.468 |
|
| 2015 |
Bondarenko MT, Maluchenko NV, Valieva ME, Gerasimova NS, Kulaeva OI, Georgiev PG, Studitsky VM. Structure and function of histone chaperone FACT Molecular Biology. 49: 796-809. DOI: 10.1134/S0026893315060023 |
0.579 |
|
| 2015 |
Maluchenko NV, Kulaeva OI, Kotova EY, Chupyrkina AA, Nikitin DV, Kirpichnikov MP, Studitsky VM. Molecular mechanisms of transcriptional regulation by Poly(ADP-ribose) polymerase 1 Molecular Biology. 49: 86-98. DOI: 10.1134/S0026893315010094 |
0.54 |
|
| 2015 |
Feofanov AV, Kudryashova KS, Chertkov OV, Nikitin DV, Pestov NA, Kulaeva OI, Studitsky VM, Kirpichnikov MP. Analysis of nucleosome transcription using single-particle FRET Springer Proceedings in Physics. 164: 255-260. DOI: 10.1007/978-3-319-16919-4_33 |
0.566 |
|
| 2014 |
Chang HW, Kulaeva OI, Shaytan AK, Kibanov M, Kuznedelov K, Severinov KV, Kirpichnikov MP, Clark DJ, Studitsky VM. Analysis of the mechanism of nucleosome survival during transcription. Nucleic Acids Research. 42: 1619-27. PMID 24234452 DOI: 10.1093/Nar/Gkt1120 |
0.628 |
|
| 2013 |
Erokhin M, Davydova A, Parshikov A, Studitsky VM, Georgiev P, Chetverina D. Transcription through enhancers suppresses their activity in Drosophila. Epigenetics & Chromatin. 6: 31. PMID 24279291 DOI: 10.1186/1756-8935-6-31 |
0.449 |
|
| 2013 |
Kyrchanova O, Maksimenko O, Stakhov V, Ivlieva T, Parshikov A, Studitsky VM, Georgiev P. Effective blocking of the white enhancer requires cooperation between two main mechanisms suggested for the insulator function. Plos Genetics. 9: e1003606. PMID 23861668 DOI: 10.1371/Journal.Pgen.1003606 |
0.413 |
|
| 2013 |
Kyrchanova O, Leman D, Parshikov A, Fedotova A, Studitsky V, Maksimenko O, Georgiev P. New properties of Drosophila scs and scs' insulators. Plos One. 8: e62690. PMID 23638134 DOI: 10.1371/Journal.Pone.0062690 |
0.326 |
|
| 2013 |
Hsieh FK, Kulaeva OI, Patel SS, Dyer PN, Luger K, Reinberg D, Studitsky VM. Histone chaperone FACT action during transcription through chromatin by RNA polymerase II. Proceedings of the National Academy of Sciences of the United States of America. 110: 7654-9. PMID 23610384 DOI: 10.1073/Pnas.1222198110 |
0.682 |
|
| 2013 |
Kulaeva OI, Hsieh FK, Chang HW, Luse DS, Studitsky VM. Mechanism of transcription through a nucleosome by RNA polymerase II. Biochimica Et Biophysica Acta. 1829: 76-83. PMID 22982194 DOI: 10.1016/J.Bbagrm.2012.08.015 |
0.644 |
|
| 2013 |
Chang H, Kulaeva OI, Shaytan A, Kibanov M, Severinov K, Clark DJ, Studitsky VM. Pausing as a mechanism of nucleosome recovery Epigenetics & Chromatin. 6. DOI: 10.1186/1756-8935-6-S1-P14 |
0.553 |
|
| 2013 |
Kulaeva OI, Malyuchenko NV, Nikitin DV, Demidenko AV, Chertkov OV, Efimova NS, Kirpichnikov MP, Studitsky VM. Molecular mechanisms of transcription through a nucleosome by RNA polymerase II Molecular Biology. 47: 655-667. DOI: 10.1134/S0026893313050099 |
0.651 |
|
| 2013 |
Chang J, Messieres Md, Li P, Kulaeva OI, Studitsky VM, Yu ET, Porta AL. Mechanical Stability of Mononucleosome Revealed by Optical Torque Wrench Biophysical Journal. 104. DOI: 10.1016/J.Bpj.2012.11.3220 |
0.567 |
|
| 2012 |
Kulaeva OI, Nizovtseva EV, Polikanov YS, Ulianov SV, Studitsky VM. Distant activation of transcription: mechanisms of enhancer action. Molecular and Cellular Biology. 32: 4892-7. PMID 23045397 DOI: 10.1128/Mcb.01127-12 |
0.561 |
|
| 2012 |
Gaykalova DA, Kulaeva OI, Pestov NA, Hsieh FK, Studitsky VM. Experimental analysis of the mechanism of chromatin remodeling by RNA polymerase II. Methods in Enzymology. 512: 293-314. PMID 22910212 DOI: 10.1016/B978-0-12-391940-3.00013-5 |
0.603 |
|
| 2012 |
Kulaeva OI, Zheng G, Polikanov YS, Colasanti AV, Clauvelin N, Mukhopadhyay S, Sengupta AM, Studitsky VM, Olson WK. Internucleosomal interactions mediated by histone tails allow distant communication in chromatin. The Journal of Biological Chemistry. 287: 20248-57. PMID 22518845 DOI: 10.1074/Jbc.M111.333104 |
0.525 |
|
| 2012 |
Sokolova O, Volokh O, Hsieh F, Studitsky V, Pechnikova E. 3D Structure of Intermediate Complexes Formed During Transcription Through Nucleosome by RNA Polymerase Microscopy and Microanalysis. 18: 120-121. DOI: 10.1017/S1431927612002450 |
0.498 |
|
| 2012 |
Clauvelin N, Studitsky V, Olson WK. Looping and Long-Distance Communication on Chromatin Biophysical Journal. 102: 482a. DOI: 10.1016/J.Bpj.2011.11.2642 |
0.585 |
|
| 2012 |
Chang J, Messieres Md, Kulaeva OI, Studitsky VM, Porta AL. Single-Molecule Twist and Stretch of Mononucleosome using Optical Torque Wrench Biophysical Journal. 102. DOI: 10.1016/J.Bpj.2011.11.2639 |
0.544 |
|
| 2012 |
Studitsky VM. Mechanisms of Gene Regulation Over a Distance on DNA and in Chromatin Biophysical Journal. 102. DOI: 10.1016/J.Bpj.2011.11.1279 |
0.447 |
|
| 2011 |
Mukhopadhyay S, Schedl P, Studitsky VM, Sengupta AM. Theoretical analysis of the role of chromatin interactions in long-range action of enhancers and insulators. Proceedings of the National Academy of Sciences of the United States of America. 108: 19919-24. PMID 22123989 DOI: 10.1073/Pnas.1103845108 |
0.374 |
|
| 2011 |
Hsieh FK, Kulaeva OI, Orlovsky IV, Studitsky VM. FACT in Cell Differentiation and Carcinogenesis. Oncotarget. 2: 830-2. PMID 22095465 DOI: 10.18632/Oncotarget.356 |
0.611 |
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| 2011 |
Luse DS, Studitsky VM. The mechanism of nucleosome traversal by RNA polymerase II: roles for template uncoiling and transcript elongation factors. Rna Biology. 8: 581-5. PMID 21519186 DOI: 10.4161/Rna.8.4.15389 |
0.668 |
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| 2011 |
Gaykalova DA, Nagarajavel V, Bondarenko VA, Bartholomew B, Clark DJ, Studitsky VM. A polar barrier to transcription can be circumvented by remodeler-induced nucleosome translocation. Nucleic Acids Research. 39: 3520-8. PMID 21245049 DOI: 10.1093/Nar/Gkq1273 |
0.518 |
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| 2011 |
Clauvelin N, Olson WK, Studitsky V. Long-Range Interactions in Chromatin Biophysical Journal. 100: 67a. DOI: 10.1016/J.Bpj.2010.12.565 |
0.547 |
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| 2011 |
Schauer G, Pestov N, Fagerburg MV, Studitsky V, Leuba SH. Transcription in Chromatin: Single-Molecule Observation of Active Mononucleosomal Elongation Complexes Biophysical Journal. 100: 66a. DOI: 10.1016/J.Bpj.2010.12.558 |
0.635 |
|
| 2010 |
Kulaeva OI, Studitsky VM. Mechanism of histone survival during transcription by RNA polymerase II. Transcription. 1: 85-8. PMID 21326897 DOI: 10.4161/trns.1.2.12519 |
0.509 |
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| 2010 |
Hsieh FK, Fisher M, Ujvári A, Studitsky VM, Luse DS. Histone Sin mutations promote nucleosome traversal and histone displacement by RNA polymerase II. Embo Reports. 11: 705-10. PMID 20706221 DOI: 10.1038/Embor.2010.113 |
0.617 |
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| 2010 |
Kulaeva OI, Hsieh FK, Studitsky VM. RNA polymerase complexes cooperate to relieve the nucleosomal barrier and evict histones. Proceedings of the National Academy of Sciences of the United States of America. 107: 11325-30. PMID 20534568 DOI: 10.1073/Pnas.1001148107 |
0.636 |
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| 2009 |
Kulaeva OI, Gaykalova DA, Pestov NA, Golovastov VV, Vassylyev DG, Artsimovitch I, Studitsky VM. Mechanism of chromatin remodeling and recovery during passage of RNA polymerase II. Nature Structural & Molecular Biology. 16: 1272-8. PMID 19935686 DOI: 10.1038/Nsmb.1689 |
0.642 |
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| 2009 |
Morozov AV, Fortney K, Gaykalova DA, Studitsky VM, Widom J, Siggia ED. Using DNA mechanics to predict in vitro nucleosome positions and formation energies. Nucleic Acids Research. 37: 4707-22. PMID 19509309 DOI: 10.1093/Nar/Gkp475 |
0.521 |
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| 2009 |
Gaykalova DA, Kulaeva OI, Bondarenko VA, Studitsky VM. Preparation and analysis of uniquely positioned mononucleosomes. Methods in Molecular Biology (Clifton, N.J.). 523: 109-23. PMID 19381918 DOI: 10.1007/978-1-59745-190-1_8 |
0.514 |
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| 2009 |
Polikanov YS, Studitsky VM. Analysis of distant communication on defined chromatin templates in vitro. Methods in Molecular Biology (Clifton, N.J.). 543: 563-76. PMID 19378187 DOI: 10.1007/978-1-60327-015-1_33 |
0.445 |
|
| 2009 |
Studitsky VM. Mechanisms of distant enhancer action on DNA and in chromatin Molecular Biology. 43: 188-197. DOI: 10.1134/S0026893309020022 |
0.494 |
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| 2008 |
Ujvári A, Hsieh FK, Luse SW, Studitsky VM, Luse DS. Histone N-terminal tails interfere with nucleosome traversal by RNA polymerase II. The Journal of Biological Chemistry. 283: 32236-43. PMID 18815126 DOI: 10.1074/Jbc.M806636200 |
0.619 |
|
| 2007 |
Polikanov YS, Bondarenko VA, Tchernaenko V, Jiang YI, Lutter LC, Vologodskii A, Studitsky VM. Probability of the site juxtaposition determines the rate of protein-mediated DNA looping. Biophysical Journal. 93: 2726-31. PMID 17573434 DOI: 10.1529/Biophysj.107.111245 |
0.476 |
|
| 2007 |
Kulaeva OI, Gaykalova DA, Studitsky VM. Transcription through chromatin by RNA polymerase II: histone displacement and exchange. Mutation Research. 618: 116-29. PMID 17313961 DOI: 10.1016/J.Mrfmmm.2006.05.040 |
0.657 |
|
| 2007 |
Polikanov YS, Rubtsov MA, Studitsky VM. Biochemical analysis of enhancer-promoter communication in chromatin. Methods (San Diego, Calif.). 41: 250-8. PMID 17309834 DOI: 10.1016/J.Ymeth.2006.11.003 |
0.521 |
|
| 2006 |
Rubtsov MA, Polikanov YS, Bondarenko VA, Wang YH, Studitsky VM. Chromatin structure can strongly facilitate enhancer action over a distance. Proceedings of the National Academy of Sciences of the United States of America. 103: 17690-5. PMID 17101994 DOI: 10.1073/Pnas.0603819103 |
0.596 |
|
| 2006 |
Bondarenko VA, Steele LM, Ujvári A, Gaykalova DA, Kulaeva OI, Polikanov YS, Luse DS, Studitsky VM. Nucleosomes can form a polar barrier to transcript elongation by RNA polymerase II. Molecular Cell. 24: 469-79. PMID 17081995 DOI: 10.1016/J.Molcel.2006.09.009 |
0.644 |
|
| 2006 |
Angelov D, Bondarenko VA, Almagro S, Menoni H, Mongélard F, Hans F, Mietton F, Studitsky VM, Hamiche A, Dimitrov S, Bouvet P. Nucleolin is a histone chaperone with FACT-like activity and assists remodeling of nucleosomes. The Embo Journal. 25: 1669-79. PMID 16601700 DOI: 10.1038/Sj.Emboj.7601046 |
0.561 |
|
| 2006 |
Doyen CM, An W, Angelov D, Bondarenko V, Mietton F, Studitsky VM, Hamiche A, Roeder RG, Bouvet P, Dimitrov S. Mechanism of polymerase II transcription repression by the histone variant macroH2A. Molecular and Cellular Biology. 26: 1156-64. PMID 16428466 DOI: 10.1128/Mcb.26.3.1156-1164.2006 |
0.542 |
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| 2005 |
Kireeva ML, Hancock B, Cremona GH, Walter W, Studitsky VM, Kashlev M. Nature of the nucleosomal barrier to RNA polymerase II. Molecular Cell. 18: 97-108. PMID 15808512 DOI: 10.1016/J.Molcel.2005.02.027 |
0.781 |
|
| 2005 |
Studitsky VM. Chromatin remodeling by RNA polymerase II Molecular Biology. 39: 549-563. DOI: 10.1007/S11008-005-0071-3 |
0.665 |
|
| 2004 |
Angelov D, Verdel A, An W, Bondarenko V, Hans F, Doyen CM, Studitsky VM, Hamiche A, Roeder RG, Bouvet P, Dimitrov S. SWI/SNF remodeling and p300-dependent transcription of histone variant H2ABbd nucleosomal arrays. The Embo Journal. 23: 3815-24. PMID 15372075 DOI: 10.1038/Sj.Emboj.7600400 |
0.447 |
|
| 2004 |
Walter W, Studitsky VM. Construction, analysis, and transcription of model nucleosomal templates. Methods (San Diego, Calif.). 33: 18-24. PMID 15039083 DOI: 10.1016/J.Ymeth.2003.10.016 |
0.8 |
|
| 2004 |
Studitsky VM, Walter W, Kireeva M, Kashlev M, Felsenfeld G. Chromatin remodeling by RNA polymerases. Trends in Biochemical Sciences. 29: 127-35. PMID 15003270 DOI: 10.1016/J.Tibs.2004.01.003 |
0.777 |
|
| 2004 |
Walter W, Kashlev M, Studitsky VM. Transcription Through the Nucleosome by mRNA-Producing RNA Polymerases Methods in Enzymology. 377: 445-460. PMID 14979044 DOI: 10.1016/S0076-6879(03)77029-3 |
0.697 |
|
| 2003 |
Walter W, Kireeva ML, Tchernajenko V, Kashlev M, Studitsky VM. Assay of the Fate of the Nucleosome during Transcription by RNA Polymerase II Methods in Enzymology. 371: 564-577. PMID 14712729 DOI: 10.1016/S0076-6879(03)71042-8 |
0.79 |
|
| 2003 |
Bondarenko V, Liu YV, Ninfa AJ, Studitsky VM. Assay of prokaryotic enhancer activity over a distance in vitro. Methods in Enzymology. 370: 324-37. PMID 14712657 DOI: 10.1016/S0076-6879(03)70029-9 |
0.513 |
|
| 2003 |
Bondarenko VA, Jiang YI, Studitsky VM. Rationally designed insulator-like elements can block enhancer action in vitro. The Embo Journal. 22: 4728-37. PMID 12970185 DOI: 10.1093/Emboj/Cdg468 |
0.474 |
|
| 2003 |
Belotserkovskaya R, Oh S, Bondarenko VA, Orphanides G, Studitsky VM, Reinberg D. FACT facilitates transcription-dependent nucleosome alteration. Science (New York, N.Y.). 301: 1090-3. PMID 12934006 DOI: 10.1126/Science.1085703 |
0.656 |
|
| 2003 |
Bondarenko VA, Liu YV, Jiang YI, Studitsky VM. Communication over a large distance: enhancers and insulators. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 81: 241-51. PMID 12897858 DOI: 10.1139/O03-051 |
0.469 |
|
| 2003 |
Walter W, Kireeva ML, Studitsky VM, Kashlev M. Bacterial polymerase and yeast polymerase II use similar mechanisms for transcription through nucleosomes. The Journal of Biological Chemistry. 278: 36148-56. PMID 12851391 DOI: 10.1074/Jbc.M305647200 |
0.787 |
|
| 2003 |
Liu YV, Clark DJ, Tchernajenko V, Dahmus ME, Studitsky VM. Role of C-terminal domain phosphorylation in RNA polymerase II transcription through the nucleosome. Biopolymers. 68: 528-38. PMID 12666177 DOI: 10.1002/Bip.10302 |
0.584 |
|
| 2002 |
Kireeva ML, Walter W, Tchernajenko V, Bondarenko V, Kashlev M, Studitsky VM. Nucleosome remodeling induced by RNA polymerase II: loss of the H2A/H2B dimer during transcription. Molecular Cell. 9: 541-52. PMID 11931762 DOI: 10.1016/S1097-2765(02)00472-0 |
0.759 |
|
| 2002 |
Bondarenko V, Liu Y, Ninfa A, Studitsky VM. Action of prokaryotic enhancer over a distance does not require continued presence of promoter-bound sigma54 subunit. Nucleic Acids Research. 30: 636-42. PMID 11809874 DOI: 10.1093/Nar/30.3.636 |
0.521 |
|
| 2001 |
Liu Y, Bondarenko V, Ninfa A, Studitsky VM. DNA supercoiling allows enhancer action over a large distance Proceedings of the National Academy of Sciences of the United States of America. 98: 14883-14888. PMID 11742093 DOI: 10.1073/Pnas.261477898 |
0.505 |
|
| 2001 |
Walter W, Studitsky VM. Facilitated Transcription through the Nucleosome at High Ionic Strength Occurs via a Histone Octamer Transfer Mechanism Journal of Biological Chemistry. 276: 29104-29110. PMID 11390400 DOI: 10.1074/Jbc.M103704200 |
0.769 |
|
| 2001 |
Studitsky VM, Brodolin KL, Liu Y, Mirzabekov AD. Topography of lacUV5 initiation complexes Nucleic Acids Research. 29: 854-861. PMID 11160910 DOI: 10.1093/Nar/29.3.854 |
0.49 |
|
| 2001 |
Studitsky VM. Transcription Through Chromatin Molecular Biology. 35: 194-205. DOI: 10.1023/A:1010435300621 |
0.652 |
|
| 2000 |
Felsenfeld G, Clark D, Studitsky V. Transcription through nucleosomes. Biophysical Chemistry. 86: 231-7. PMID 11026687 DOI: 10.1016/S0301-4622(00)00134-4 |
0.64 |
|
| 1999 |
Bednar J, Studitsky VM, Grigoryev SA, Felsenfeld G, Woodcock CL. The nature of the nucleosomal barrier to transcription: direct observation of paused intermediates by electron cryomicroscopy. Molecular Cell. 4: 377-86. PMID 10518218 DOI: 10.1016/S1097-2765(00)80339-1 |
0.621 |
|
| 1997 |
Studitsky VM, Kassavetis GA, Geiduschek EP, Felsenfeld G. Mechanism of transcription through the nucleosome by eukaryotic RNA polymerase. Science (New York, N.Y.). 278: 1960-3. PMID 9395401 DOI: 10.1126/science.278.5345.1960 |
0.586 |
|
| 1996 |
Studitsky VM, Clark DJ, Felsenfeld G. Preparation of nucleosomal templates for transcription in vitro. Methods in Enzymology. 274: 246-56. PMID 8902809 DOI: 10.1016/S0076-6879(96)74021-1 |
0.617 |
|
| 1996 |
Felsenfeld G, Boyes J, Chung J, Clark D, Studitsky V. Chromatin structure and gene expression. Proceedings of the National Academy of Sciences of the United States of America. 93: 9384-8. PMID 8790338 DOI: 10.1073/Pnas.93.18.9384 |
0.569 |
|
| 1995 |
Studitsky VM, Clark DJ, Felsenfeld G. Overcoming a nucleosomal barrier to transcription. Cell. 83: 19-27. PMID 7553869 DOI: 10.1016/0092-8674(95)90230-9 |
0.632 |
|
| 1994 |
Studitsky VM, Clark DJ, Felsenfeld G. A histone octamer can step around a transcribing polymerase without leaving the template. Cell. 76: 371-82. PMID 8293470 DOI: 10.1016/0092-8674(94)90343-3 |
0.637 |
|
| 1993 |
Brodolin KL, Studitsky VM, Mirzabekov AD. Conformational changes in E.coli RNA polymerase during promoter recognition Nucleic Acids Research. 21: 5748-5753. PMID 8284224 DOI: 10.1093/Nar/21.24.5748 |
0.453 |
|
| 1993 |
Brodolin KL, Studitsky VM, Mirzabekov AD. Study of Escherichia coli RNA polymerase and its open complex with the lacUV5 promoter by protein-protein and DNA-protein crosslinks produced by formaldehyde Molekulyarnaya Biologiya. 27: 1085-1093. PMID 8246931 |
0.321 |
|
| 1993 |
Clark D, Reitman M, Studitsky V, Chung J, Westphal H, Lee E, Felsenfeld G. Chromatin structure of transcriptionally active genes. Cold Spring Harbor Symposia On Quantitative Biology. 58: 1-6. PMID 7956019 DOI: 10.1101/Sqb.1993.058.01.003 |
0.391 |
|
| 1991 |
Studitsky VM. Allosteric mechanism of enhancer action? Febs Letters. 280: 5-7. PMID 2009967 DOI: 10.1016/0014-5793(91)80191-5 |
0.469 |
|
| 1990 |
Studitsky VM, Chrapko KR. Enhancers, DNA loops and stable complexes: Mechanism of transcriptional activation (A hypothesis) Molekulyarnaya Biologiya. 24: 909-919. PMID 2250682 |
0.459 |
|
| 1988 |
Studitsky VM, Belyavsky AV, Melnikova AF, Mirzabekov AD. The structure of nucleosomal core particles within transcribed and repressed gene regions Nucleic Acids Research. 16: 11187-11205. PMID 3144704 DOI: 10.1093/nar/16.23.11187 |
0.477 |
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