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Understanding nucleosome dynamics and their links to gene expression and DNA replication
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Advances in genomics technology have provided the means to probe myriad chromatin interactions at unprecedented spatial and temporal resolution. This has led to a profound understanding of nucleosome organization within the genome, revealing that nucleosomes are highly dynamic. Nucleosome dynamics are governed by a complex interplay of histone composition, histone post-translational modifications, nucleosome occupancy and positioning within chromatin, which are influenced by numerous regulatory factors, including general regulatory factors, chromatin remodellers, chaperones and polymerases. It is now known that these dynamics regulate diverse cellular processes ranging from gene transcription to DNA replication and repair.
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Cites
An integrated encyclopedia of DNA elements in the human genome
The ENCODE Project Consortium (2012) · Nature · doi:10.1038/nature11247 · Cited by 18,072
Crystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466
The language of covalent histone modifications
Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679
Buenrostro, J. D., Giresi, P. G., Zaba, L. C., Chang, H. Y., & Greenleaf, W. J. (2013) · Nature Methods · doi:10.1038/nmeth.2688 · Cited by 6,422
Chromatin Structure: A Repeating Unit of Histones and DNA
Kornberg, R. D. (1974) · Science · doi:10.1126/science.184.4139.868 · Cited by 2,662
ChIP-seq guidelines and practices of the ENCODE and modENCODE consortia
Landt, S. G., Marinov, G. K., Kundaje, A., Kheradpour, P., Pauli, F., Batzoglou, S., Bernstein, B. E., Bickel, P., Brown, J. B., Cayting, P., et al. (2012) · Genome Research · doi:10.1101/gr.136184.111 · Cited by 2,033
A general method for the covalent labeling of fusion proteins with small molecules in vivo
Keppler, A., Gendreizig, S., Gronemeyer, T., Pick, H. M., Vogel, H., & Johnsson, K. (2002) · Nature Biotechnology · doi:10.1038/nbt765 · Cited by 1,964
Twenty-Five Years of the Nucleosome, Fundamental Particle of the Eukaryote Chromosome
Kornberg, R. D., & Lorch, Y. (1999) · Cell · doi:10.1016/s0092-8674(00)81958-3 · Cited by 1,833
A genomic code for nucleosome positioning
Segal, E., Fondufe‐Mittendorf, Y. N., Chen, L., Thåström, A., Field, Y., Moore, I. K., Wang, J.-P. Z., & Widom, J. (2006) · Nature · doi:10.1038/nature04979 · Cited by 1,492
Genome-wide Map of Nucleosome Acetylation and Methylation in Yeast
Pokholok, D., Harbison, C. T., Levine, S. S., Cole, M. F., Hannett, N. M., Lee, T. I., Bell, G. W., Walker, K., Rolfe, A., Herbolsheimer, E., et al. (2005) · Cell · doi:10.1016/j.cell.2005.06.026 · Cited by 1,477
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Millán-Zambrano, G., Burton, A., Bannister, A. J., & Schneider, R. (2022) · Nature Reviews Genetics · doi:10.1038/s41576-022-00468-7 · Cited by 1,116
Ultrastructural Details of Mammalian Chromosome Architecture
Krietenstein, N., Abraham, S., Venev, S. V., Abdennur, N., Gibcus, J., Hsieh, T.-H. S., Parsi, K. M., Yang, L., Maehr, R., Mirny, L. A., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.03.003 · Cited by 622
Transcription regulation by the Mediator complex
Soutourina, J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.115 · Cited by 635
Chromatin accessibility profiling by ATAC-seq
Grandi, F. C., Modi, H., Kampman, L., & Corces, M. R. (2022) · Nature Protocols · doi:10.1038/s41596-022-00692-9 · Cited by 557
Born to run: control of transcription elongation by RNA polymerase II
Chen, F. X., Smith, E. R., & Shilatifard, A. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0010-5 · Cited by 447
Epigenetic Regulation in Neurodegenerative Diseases
Berson, A., Nativio, R., Berger, S. L., & Bonini, N. M. (2018) · Trends in Neurosciences · doi:10.1016/j.tins.2018.05.005 · Cited by 408
Epigenetics in hepatocellular carcinoma
Nagaraju, G. P., Dariya, B., Kasa, P., Peela, S., & El‐Rayes, B. F. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.07.017 · Cited by 355
The epigenetic basis of cellular heterogeneity
Carter, B. C., & Zhao, K. (2020) · Nature Reviews Genetics · doi:10.1038/s41576-020-00300-0 · Cited by 324
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Skvortsova, K., Stirzaker, C., & Taberlay, P. C. (2019) · Essays in Biochemistry · doi:10.1042/ebc20190037 · Cited by 325
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Fursova, N. A., Blackledge, N. P., Nakayama, M., Ito, S., Koseki, Y., Farcas, A. M., King, H. W., Koseki, H., & Klose, R. J. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.03.024 · Cited by 267
Xavier, M. J., Roman, S. D., Aitken, R. J., & Nixon, B. (2019) · Human Reproduction Update · doi:10.1093/humupd/dmz017 · Cited by 272
Causes and consequences of RNA polymerase II stalling during transcript elongation
González, M. N., Blears, D., & Svejstrup, J. Q. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00308-8 · Cited by 262
FACT caught in the act of manipulating the nucleosome
Liu, Y., Zhou, K., Zhang, N., Wei, H., Tan, Y. Z., Zhang, Z., Carragher, B. O., Potter, C. S., D’Arcy, S., & Luger, K. (2019) · Nature · doi:10.1038/s41586-019-1820-0 · Cited by 224
Lee, I., Razaghi, R., Gilpatrick, T., Molnar, M. M., Gershman, A., Sadowski, N., Sedlazeck, F. J., Hansen, K. D., Simpson, J. T., & Timp, W. (2020) · Nature Methods · doi:10.1038/s41592-020-01000-7 · Cited by 219
Chromatin accessibility profiling methods
Minnoye, L., Marinov, G. K., Krausgruber, T., Pan, L., Marand, A. P., Secchia, S., Greenleaf, W. J., Furlong, E. E. M., Zhao, K., Schmitz, R. J., et al. (2021) · Nature Reviews Methods Primers · doi:10.1038/s43586-020-00008-9 · Cited by 206
Structural basis of the nucleosome transition during RNA polymerase II passage
Kujirai, T., Ehara, H., Fujino, Y., Shirouzu, M., Sekine, S., & Kurumizaka, H. (2018) · Science · doi:10.1126/science.aau9904 · Cited by 210
Li, F., Huang, Q., Luster, T. A., Hu, H., Zhang, H., Ng, W., Khodadadi‐Jamayran, A., Wang, W., Chen, T., Deng, J., et al. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-0780 · Cited by 209
Dangerous liaisons: interplay between SWI/SNF, NuRD, and Polycomb in chromatin regulation and cancerPreprint
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Aoi, Y., Smith, E. R., Shah, A. P., Rendleman, E. J., Marshall, S. A., Woodfin, A. R., Chen, F., Shiekhattar, R., & Shilatifard, A. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.02.014 · Cited by 171
Pampari, A., Shcherbina, A., Kvon, E. Z., Kosicki, M., Nair, S., Kundu, S., Kathiria, A. S., Risca, V. I., Kuningas, K., Alasoo, K., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.25.630221 · Cited by 183
Phase separation directs ubiquitination of gene-body nucleosomes
Gallego, L. D., Schneider, M., Mittal, C., Romanauska, A., Carrillo, R. M. G., Schubert, T., Pugh, B. F., & Köhler, A. (2020) · Nature · doi:10.1038/s41586-020-2097-z · Cited by 157
Self-citationEnergy-driven genome regulation by ATP-dependent chromatin remodellers
Eustermann, S., Patel, A. B., Hopfner, K., He, Y., & Korber, P. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00683-y · Cited by 143
Understanding the interplay between CpG island-associated gene promoters and H3K4 methylation
Hughes, A. L., Kelley, J. R., & Klose, R. J. (2020) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2020.194567 · Cited by 139
Epigenetic regulation of thermomorphogenesis and heat stress tolerance
Perrella, G., Bäurle, I., & van Zanten, M. (2022) · New Phytologist · doi:10.1111/nph.17970 · Cited by 138
RSC-Associated Subnucleosomes Define MNase-Sensitive Promoters in Yeast
Brahma, S., & Henikoff, S. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.10.046 · Cited by 139
Kubik, S., O’Duibhir, E., de Jonge, W. J., Mattarocci, S., Albert, B., Falcone, J.-L., Bruzzone, M. J., Holstege, F. C. P., & Shore, D. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.05.030 · Cited by 133
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Opposing chromatin remodelers control transcription initiation frequency and start site selection
Kubik, S., Bruzzone, M. J., Challal, D., Dreos, R., Mattarocci, S., Bucher, P., Libri, D., & Shore, D. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0273-3 · Cited by 126
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Super-enhancers: critical roles and therapeutic targets in hematologic malignancies
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Beads on a string—nucleosome array arrangements and folding of the chromatin fiber
Baldi, S., Korber, P., & Becker, P. B. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0368-x · Cited by 112
Beh, L. Y., Debelouchina, G. T., Clay, D. M., Thompson, R. E., Lindblad, K. A., Hutton, E. R., Bracht, J. R., Sebra, R., Muir, T. W., & Landweber, L. F. (2019) · Cell · doi:10.1016/j.cell.2019.04.028 · Cited by 115
Jerónimo, C., Poitras, C., & Robert, F. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.06.097 · Cited by 114
Le, J., Dian, Y., Zhao, D., Guo, Z., Luo, Z., Chen, X., Zeng, F., & Deng, G. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02426-3 · Cited by 118
Francette, A. M., Tripplehorn, S. A., & Arndt, K. M. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166979 · Cited by 104
Structure of transcribing RNA polymerase II-nucleosome complex
Farnung, L., Vos, S. M., & Cramer, P. (2018) · Nature Communications · doi:10.1038/s41467-018-07870-y · Cited by 100
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Lin, X., Qi, Y., Latham, A. P., & Zhang, B. (2021) · The Journal of Chemical Physics · doi:10.1063/5.0044150 · Cited by 93
Single-cell sequencing technology applied to epigenetics for the study of tumor heterogeneity
Hu, Y., Shen, F., Yang, X., Han, T., Long, Z., Wen, J., Huang, J., Shen, J., & Guo, Q. (2023) · Clinical Epigenetics · doi:10.1186/s13148-023-01574-x · Cited by 101
Transcription through the nucleosome
Kujirai, T., & Kurumizaka, H. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.10.007 · Cited by 107
Histone H1 binding to nucleosome arrays depends on linker DNA length and trajectory
Dombrowski, M., Engeholm, M., Dienemann, C., Dodonova, S., & Cramer, P. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00768-w · Cited by 95
The Histone H3 Lysine 4 Presenter WDR5 as an Oncogenic Protein and Novel Epigenetic Target in Cancer
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Oldfield, A., Henriques, T., Kumar, D., Burkholder, A., Cinghu, S., Paulet, D., Bennett, B. D., Yang, P., Scruggs, B. S., Lavender, C. A., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10905-7 · Cited by 94
Design, Synthesis, and Evaluation of WD-Repeat-Containing Protein 5 (WDR5) Degraders
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The nucleosome core particle remembers its position through DNA replication and RNA transcription
Schlissel, G., & Rine, J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1911943116 · Cited by 82
Ruler elements in chromatin remodelers set nucleosome array spacing and phasing
Oberbeckmann, E., Niebauer, V., Watanabe, S., Farnung, L., Moldt, M., Schmid, A., Cramer, P., Peterson, C. L., Eustermann, S., Hopfner, K., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23015-0 · Cited by 80
Multiscale footprints reveal the organization of cis-regulatory elements
Yan, H., Horlbeck, M. A., Zhang, R., Ma, S., Shrestha, R., Kartha, V. K., Duarte, F. M., Hock, C., Savage, R. E., Labade, A. S., et al. (2025) · Nature · doi:10.1038/s41586-024-08443-4 · Cited by 93
Mechanosensing dysregulation in the fibroblast: A hallmark of the aging heart
Angelini, A., Trial, J., Ortiz-Urbina, J., & Cieslik, K. A. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101150 · Cited by 79
DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network
Hammond, C. M., Bao, H., Hendriks, I. A., Carraro, M., García-Nieto, A., Liu, Y., Reverón-Gómez, N., Spanos, C., Chen, L., Rappsilber, J., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.03.041 · Cited by 79
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Structures of +1 nucleosome–bound PIC-Mediator complex
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Live-cell single particle imaging reveals the role of RNA polymerase II in histone H2A.Z eviction
Ranjan, A., Nguyen, V. Q., Liu, S., Wiśniewski, J., Kim, J. M., Tang, X., Mizuguchi, G., Elalaoui, E., Nickels, T. J., Jou, V., et al. (2020) · eLife · doi:10.7554/elife.55667 · Cited by 75
Sarkar, N. D., Patton, R. D., Doebley, A.-L., Hanratty, B. P., Kreitzman, A. J., Sarthy, J. F., Ko, M., Adil, M., Brahma, S., Meers, M. P., et al. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-22-0692 · Cited by 80
FACT is recruited to the +1 nucleosome of transcribed genes and spreads in a Chd1-dependent manner
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Singh, R., Bassett, E. A., Chakravarti, A., & Parthun, M. R. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky768 · Cited by 69
Single-molecule long-read sequencing reveals the chromatin basis of gene expressionPreprint
Wang, Y., Wang, A., Liu, Z., Thurman, A. L., Powers, L. S., Zou, M., Zhao, Y., Hefel, A., Li, Y., Zabner, J., et al. (2019) · Genome Research · doi:10.1101/gr.251116.119 · Cited by 68
KDM5B demethylates H3K4 to recruit XRCC1 and promote chemoresistance
Xu, W., Zhou, B., Zhao, X., Zhu, L., Xu, J., Jiang, Z., Chen, D., Wei, Q., Han, M., Feng, L., et al. (2018) · International Journal of Biological Sciences · doi:10.7150/ijbs.25881 · Cited by 67
Targeting Chromatin Remodeling for Cancer Therapy
Kaur, J., Daoud, A., & Eblen, S. T. (2019) · Current Molecular Pharmacology · doi:10.2174/1874467212666190215112915 · Cited by 69
Sentinels of chromatin: chromodomain helicase DNA-binding proteins in development and diseasePreprint
Alendar, A., & Berns, A. J. M. (2021) · Genes & Development · doi:10.1101/gad.348897.121 · Cited by 69
Kim, J. M., Visanpattanasin, P., Jou, V., Liu, S., Tang, X., Zheng, Q., Li, K. Y., Snedeker, J. C., Lavis, L. D., Lionnet, T., et al. (2021) · eLife · doi:10.7554/elife.69387 · Cited by 64
Shared genetic and epigenetic changes link aging and cancer
Zabransky, D. J., Jaffee, E. M., & Weeraratna, A. T. (2022) · Trends in Cell Biology · doi:10.1016/j.tcb.2022.01.004 · Cited by 67
Shen, J., Chen, M., Lee, D., Law, C., Wei, L., Tsang, F. H., Chin, D. W., Cheng, C. L., Lee, J. M., Ng, I. O., et al. (2019) · Gut · doi:10.1136/gutjnl-2019-318668 · Cited by 64
Transcription-coupled repair of DNA–protein cross-links depends on CSA and CSB
Carnie, C. J., Acampora, A. C., Bader, A. S., Erdenebat, C., Zhao, S., Bitensky, E. M., van den Heuvel, D., Parnas, A., Gupta, V., D’Alessandro, G., et al. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01391-1 · Cited by 61
Structure of transcribing RNA polymerase II-nucleosome complex
Farnung, L., Vos, S. M., & Cramer, P. (2018) · Worldwide Protein Data Bank · doi:10.2210/pdb6i84/pdb · Cited by 61
Genome information processing by the INO80 chromatin remodeler positions nucleosomes
Oberbeckmann, E., Krietenstein, N., Niebauer, V., Wang, Y., Schall, K., Moldt, M., Straub, T., Rohs, R., Hopfner, K., Korber, P., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23016-z · Cited by 60
Regulation of neuronal connectivity in the mammalian brain by chromatin remodeling
Goodman, J. V., & Bonni, A. (2019) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2019.04.010 · Cited by 64
Challal, D., Barucco, M., Kubik, S., Feuerbach, F., Candelli, T., Geoffroy, H., Benaksas, C., Shore, D., & Libri, D. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.11.037 · Cited by 60
Clarkson, C. T., Deeks, E. A., Samarista, R., Mamayusupova, H., Zhurkin, V. B., & Teif, V. B. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz908 · Cited by 63
DNA mechanics and its biological impact
Basu, A., Bobrovnikov, D. G., & Ha, T. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166861 · Cited by 61
Structure of a backtracked hexasomal intermediate of nucleosome transcription
Farnung, L., Ochmann, M., Garg, G., Vos, S. M., & Cramer, P. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.06.027 · Cited by 59
Structural transition of the nucleosome during chromatin remodeling and transcription
Kobayashi, W., & Kurumizaka, H. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.07.011 · Cited by 58
Pharmacological targeting of the cancer epigenome
Mabe, N. W., Perry, J. A., Malone, C. F., & Stegmaier, K. (2024) · Nature Cancer · doi:10.1038/s43018-024-00777-2 · Cited by 61
Histone chaperone FACT FAcilitates Chromatin Transcription: mechanistic and structural insights
Zhou, K., Liu, Y., & Luger, K. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.05.019 · Cited by 58
Resetting the Yeast Epigenome with Human Nucleosomes
Truong, D. M., & Boeke, J. D. (2017) · Cell · doi:10.1016/j.cell.2017.10.043 · Cited by 62
Chromatin remodelers couple inchworm motion with twist-defect formation to slide nucleosomal DNA
Brandani, G. B., & Takada, S. (2018) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1006512 · Cited by 55
Structural visualization of key steps in nucleosome reorganization by human FACT
Mayanagi, K., Saikusa, K., Miyazaki, N., Akashi, S., Iwasaki, K., Nishimura, Y., Morikawa, K., & Tsunaka, Y. (2019) · Scientific Reports · doi:10.1038/s41598-019-46617-7 · Cited by 57
Unravelling the role of epigenetics in reproductive adaptations to early-life environment
Bar-Sadeh, B., Rudnizky, S., Pnueli, L., Bentley, G. R., Stöger, R. J., Kaplan, A., & Melamed, P. (2020) · Nature Reviews Endocrinology · doi:10.1038/s41574-020-0370-8 · Cited by 61
Investigating the Dynamics of Destabilized Nucleosomes Using Methyl-TROSY NMR
Kitevski-LeBlanc, J. L., Yuwen, T., Dyer, P. N., Rudolph, J., Luger, K., & Kay, L. E. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b00931 · Cited by 56
Arora, I., & Tollefsbol, T. O. (2020) · Methods · doi:10.1016/j.ymeth.2020.09.008 · Cited by 56
Current and Emerging Methods for the Synthesis of Single-Stranded DNA
Hao, M., Qiao, J., & Qi, H. (2020) · Genes · doi:10.3390/genes11020116 · Cited by 55
PARP1 exhibits enhanced association and catalytic efficiency with γH2A.X-nucleosome
Sharma, D., Falco, L. D., Padavattan, S., Rao, C., Shochat, S. G., Liu, C., & Davey, C. A. (2019) · Nature Communications · doi:10.1038/s41467-019-13641-0 · Cited by 55
The chromatin remodeling enzyme Chd4 regulates genome architecture in the mouse brain
Goodman, J. V., Yamada, T., Yang, Y., Kong, L., Wu, D. Y., Zhao, G., Gabel, H. W., & Bonni, A. (2020) · Nature Communications · doi:10.1038/s41467-020-17065-z · Cited by 57
Gruszka, D. T., Xie, S., Kimurâ, H., & Yardimci, H. (2020) · Science Advances · doi:10.1126/sciadv.abc0330 · Cited by 52
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Abril-Garrido, J., Dienemann, C., Grabbe, F., Velychko, T., Lidschreiber, M., Wang, H., & Cramer, P. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.04.011 · Cited by 48
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Metadata
- Authors
- Lai, W. K. M., & Pugh, B. F.
- Affiliations
- Pennsylvania State University (US)
- Corresponding author
- Pugh, B. Franklin
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2017-05-24
- Volume
- 18
- Issue
- 9
- Pages
- 548-562
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- PMC
- PMC5831138
- OpenAlex
- W2618569629
- Cited by
- 495
- References
- 178
- Citations by year
- 2026: 36 · 2025: 54 · 2024: 55 · 2023: 46 · 2022: 54 · 2021: 63 · 2020: 61 · 2019: 66 · 2018: 53 · 2017: 7
- FWCI
- 4.81
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM059055)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- nucleosome dynamics, nucleosome positioning, nucleosome occupancy, chromatin structure, histone modifications, histone composition, chromatin remodeling, gene transcription, DNA replication, DNA repair, polymerase
- MeSH terms
- Animals, Chromatin, DNA Repair, DNA Replication, Gene Expression Regulation, Humans, Nucleosomes, Protein Processing, Post-Translational, Transcription, Genetic, Histone Code
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