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An integrated encyclopedia of DNA elements in the human genome

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The language of covalent histone modifications

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Transposition of native chromatin for fast and sensitive epigenomic profiling of open chromatin, DNA-binding proteins and nucleosome position

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Chromatin Structure: A Repeating Unit of Histones and DNA

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A general method for the covalent labeling of fusion proteins with small molecules in vivo

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Twenty-Five Years of the Nucleosome, Fundamental Particle of the Eukaryote Chromosome

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A genomic code for nucleosome positioning

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Genome-wide Map of Nucleosome Acetylation and Methylation in Yeast

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Pioneer factor ETV2 safeguards endothelial cell specification by recruiting the repressor REST to restrict alternative lineage commitment

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Hypoxia-Inducible Factors and Burn-Associated Acute Kidney Injury—A New Paradigm?

Enescu, D. M., Parasca, S. V., Bădoiu, S. C., Miricescu, D., Totan, A., Stănescu-Spînu, I.-I., Greabu, M., & Jinga, V. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052470 · Cited by 17

CUT&RUN Profiling of the Budding Yeast Epigenome

Brahma, S., & Henikoff, S. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2257-5_9 · Cited by 15

Molecular dynamics simulations for the study of chromatin biology

Brandani, G. B., Gopi, S., Yamauchi, M., & Takada, S. (2022) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102485 · Cited by 16

Loss of the Ash2l subunit of histone H3K4 methyltransferase complexes reduces chromatin accessibility at promoters

Barsoum, M., Stenzel, A. T., Bochyńska, A., Kuo, C., Tsompanidis, A., Sayadi-Boroujeni, R., Bussmann, P., Lüscher‐Firzlaff, J., Costa, I. G., & Lüscher, B. (2022) · Scientific Reports · doi:10.1038/s41598-022-25881-0 · Cited by 15

Chromatin remodeling in tissue stem cell fate determination

Li, X., Zhu, G., & Zhao, B. T. (2024) · Cell Regeneration · doi:10.1186/s13619-024-00203-z · Cited by 16

Plasmodium blood stage development requires the chromatin remodeller Snf2L

Watzlowik, M. T., Silberhorn, E., Das, S., Singhal, R., Venugopal, K., Holzinger, S., Stokes, B. H., Schadt, E. E., Sollelis, L., Bonnell, V. A., et al. (2025) · Nature · doi:10.1038/s41586-025-08595-x · Cited by 15

Alterations in oocytes and early zygotes following oral exposure to di(2-ethylhexyl) phthalate in young adult female mice

Parra-Forero, L. Y., Veloz-Contreras, A., Vargas-Marín, S., Mojica-Villegas, M. A., Alfaro-Pedraza, E., Urióstegui-Acosta, M., & Hernández‐Ochoa, I. (2019) · Reproductive Toxicology · doi:10.1016/j.reprotox.2019.08.012 · Cited by 15

Intercalation of small molecules into DNA in chromatin is primarily controlled by superhelical constraint

Bosire, R., Nánási, P. P., Imre, L., Dienes, B., Szöőr, Á., Mázló, A., Kovács, A., Seidel, R., Vámosi, G., & Szabó, G. (2019) · PLoS ONE · doi:10.1371/journal.pone.0224936 · Cited by 15

Nucleosomes as allosteric scaffolds for genetic regulation

Takada, S., Brandani, G. B., & Tan, C. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.11.013 · Cited by 15

Loss of chromatin structural integrity is a source of stress during aging

Yu, R., McCauley, B. S., & Dang, W. (2020) · Human Genetics · doi:10.1007/s00439-019-02100-x · Cited by 16

Chromatin Organization and Function in Drosophila

Llorens‐Giralt, P., Camilleri‐Robles, C., Corominas, M., & Climent‐Cantó, P. (2021) · Cells · doi:10.3390/cells10092362 · Cited by 16

Nucleosome Positioning by an Evolutionarily Conserved Chromatin Remodeler Prevents Aberrant DNA Methylation in Neurospora

Klocko, A. D., Uesaka, M., Ormsby, T., Rountree, M. R., Wiles, E. T., Adhvaryu, K. K., Honda, S., & Selker, E. U. (2018) · Genetics · doi:10.1534/genetics.118.301711 · Cited by 15

Establishment and Maintenance of Chromatin Architecture Are Promoted Independently of Transcription by the Histone Chaperone FACT and H3-K56 Acetylation in Saccharomyces cerevisiae

McCullough, L. L., Pham, T. H., Parnell, T. J., Connell, Z., Chandrasekharan, M. B., Stillman, D. J., & Formosa, T. (2019) · Genetics · doi:10.1534/genetics.118.301853 · Cited by 15

Histone exchange is associated with activator function at transcribed promoters and with repression at histone loci

Kassem, S., Ferrari, P., Hughes, A. L., Soudet, J., Rando, O. J., & Strubin, M. (2020) · Science Advances · doi:10.1126/sciadv.abb0333 · Cited by 15

Structures of H2A.Z-associated human chromatin remodelers SRCAP and TIP60 reveal divergent mechanisms of chromatin engagementPreprint

Park, G., Patel, A. B., Wu, C., & Louder, R. K. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.30.605802 · Cited by 16

Pioneer factors and their in vitro identification methods

Yu, X., & Buck, M. J. (2020) · Molecular Genetics and Genomics · doi:10.1007/s00438-020-01675-9 · Cited by 14

Autism-associated CHD8 keeps proliferation of human neural progenitors in check by lengthening the G1 phase of the cell cycle

Coakley-Youngs, E., Shorter, S. A., Ranatunga, M., Richardson, S., Getti, G., & Fivaz, M. L. (2022) · Biology Open · doi:10.1242/bio.058941 · Cited by 15

Molecular mechanism of parental H3/H4 recycling at a replication fork

Nagae, F., Murayama, Y., & Terakawa, T. (2024) · Nature Communications · doi:10.1038/s41467-024-53187-4 · Cited by 14

A droplet microfluidic platform for efficient enzymatic chromatin digestion enables robust determination of nucleosome positioning

Xu, Y. F., Lee, J., Li, Z., Wang, L., Ördög, T., & Bailey, R. C. (2018) · Lab on a Chip · doi:10.1039/c8lc00599k · Cited by 15

Proteasome inhibition creates a chromatin landscape favorable to RNA Pol II processivity

Kinyamu, H. K., Bennett, B. D., Bushel, P. R., & Archer, T. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011174 · Cited by 15

Immunity onset alters plant chromatin and utilizes EDA16 to regulate oxidative homeostasis

Pardal, A. J., Piquerez, S. J. M., Domínguez‐Ferreras, A., Frungillo, L., Mastorakis, E., Reilly, E., Latrasse, D., Concia, L., Ibanez, S. G., Spoel, S. H., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009572 · Cited by 14

The Latest Twists in Chromatin Remodeling

Blossey, R., & Schießel, H. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2017.12.008 · Cited by 14

Engineered Chromatin Remodeling Proteins for Precise Nucleosome Positioning

Donovan, D. A., Crandall, J. G., Banks, O. G., Jensvold, Z. D., Truong, V. N., Dinwiddie, D., McKnight, L. E., & McKnight, J. N. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.10.046 · Cited by 13

The Accidental Ally: Nucleosome Barriers Can Accelerate Cohesin-Mediated Loop Formation in Chromatin

Maji, A., Padinhateeri, R., & Mitra, M. K. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.10.014 · Cited by 14

Gene expression levels modulate germline mutation rates through the compound effects of transcription-coupled repair and damage

Xia, B., & Yanai, I. (2021) · Human Genetics · doi:10.1007/s00439-021-02355-3 · Cited by 14

Establishment and Maintenance of Open Ribosomal RNA Gene Chromatin States in Eukaryotes

Schächner, C., Merkl, P., Pilsl, M., Schwank, K., Hergert, K., Kruse, S., Milkereit, P., Tschochner, H., & Griesenbeck, J. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2501-9_2 · Cited by 13

Emerging functions of chromatin modifications in auxin biosynthesis in response to environmental alterations

Do, B. H., Vu, P. T. B., Tran, G., & Nguyen, N. H. (2018) · Plant Growth Regulation · doi:10.1007/s10725-018-0453-x · Cited by 14

Nut1/Hos1 and Sas2/Rpd3 control the H3 acetylation of two different sets of osmotic stress-induced genes

Pérez-Martínez, M. E., Benet, M., Alepuz, P. M., & Tordera, V. (2019) · Epigenetics · doi:10.1080/15592294.2019.1664229 · Cited by 13

Reduced USP22 Expression Impairs Mitotic Removal of H2B Monoubiquitination, Alters Chromatin Compaction and Induces Chromosome Instability That May Promote Oncogenesis

Jeusset, L. M., Guppy, B. J., Lichtensztejn, Z., McDonald, D., & McManus, K. J. (2021) · Cancers · doi:10.3390/cancers13051043 · Cited by 13

Nucleosome remodeling at origins of global genome–nucleotide excision repair occurs at the boundaries of higher-order chromatin structurePreprint

van Eijk, P., Nandi, S. P., Yu, S., Bennett, M., Leadbitter, M., Teng, Y., & Reed, S. H. (2018) · Genome Research · doi:10.1101/gr.237198.118 · Cited by 13

In vivo DNA methylation editing in zebrafish

Liang, F., Dong, Z., Ye, J., Hu, W., Bhandari, R. K., Mai, K., & Wang, X. (2023) · Epigenetics · doi:10.1080/15592294.2023.2192326 · Cited by 14

Deciphering principles of nucleosome interactions and impact of cancer-associated mutations from comprehensive interaction network analysis

Wang, X., Zhang, H., Guo, W., Jiang, L., Zhao, Y., & Peng, Y. (2024) · Briefings in Bioinformatics · doi:10.1093/bib/bbad532 · Cited by 12

The Use of Mononucleosome Immunoprecipitation for Analysis of Combinatorial Histone Post-translational Modifications and Purification of Nucleosome-Interacting Proteins

Khan, K. A., Ng, M. K., & Cheung, P. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00331 · Cited by 12

Effective dynamics of nucleosome configurations at the yeast PHO5 promoter

Wolff, M. R., Schmid, A., Korber, P., & Gerland, U. (2021) · eLife · doi:10.7554/elife.58394 · Cited by 12

Transcriptome analysis reveals gene expression changes of the basidiomycetous yeast Apiotrichum mycotoxinivorans in response to ochratoxin A exposure

Yang, Z.-K., Huang, X., & Peng, L. (2022) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2022.114146 · Cited by 12

Exploring the Link between Nucleosome Occupancy and DNA Methylation

Lövkvist, C., Sneppen, K., & Haerter, J. O. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2017.00232 · Cited by 12

Aptamer functionalized magnetic graphene oxide nanocomposites for highly selective capture of histones

Chen, Y., Jiang, B., Hu, Y., Deng, N., Zhao, B., Li, X., Liang, Z., Zhang, L., & Zhang, Y. (2019) · Electrophoresis · doi:10.1002/elps.201900061 · Cited by 12

The yeast genome is globally accessible in living cells

Prajapati, H. K., Eriksson, P. R., Elizalde, P., Coey, C. T., Xu, Z., & Clark, D. J. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01318-2 · Cited by 11

Histone-Net: a multi-paradigm computational framework for histone occupancy and modification prediction

Asim, M. N., Ibrahim, M. A., Malik, M. I., Razzak, I., Dengel, A. R., & Ahmed, S. (2022) · Complex & Intelligent Systems · doi:10.1007/s40747-022-00802-w · Cited by 11

The Saccharomyces cerevisiae Yta7 ATPase hexamer contains a unique bromodomain tier that functions in nucleosome disassembly

Wang, F., Feng, X., He, Q., Li, H. L., & Li, H. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102852 · Cited by 11

Investigating Nucleosome Accessibility for MNase, FeII Peplomycin, and Duocarmycin B2 by Using Capillary Electrophoresis

Zou, T., Kizaki, S., & Sugiyama, H. (2018) · ChemBioChem · doi:10.1002/cbic.201700643 · Cited by 11

Regulation of Gene Expression and Replication Initiation by Non‐Coding Transcription: A Model Based on Reshaping Nucleosome‐Depleted Regions

Soudet, J., & Stutz, F. (2019) · BioEssays · doi:10.1002/bies.201900043 · Cited by 12

The importance of DNA sequence for nucleosome positioning in transcriptional regulation

Sahrhage, M., Paul, N. B., Beißbarth, T., & Haubrock, M. (2024) · Life Science Alliance · doi:10.26508/lsa.202302380 · Cited by 10

Molecular models of bidirectional promoter regulation

Nemsick, S., & Hansen, A. S. (2024) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102865 · Cited by 11

Always on the Move: Overview on Chromatin Dynamics within Nuclear Processes

de Fenffe, C. M. D., Govers, J., & Mattiroli, F. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00114 · Cited by 10

FACT weakens the nucleosomal barrier to transcription and preserves its integrity by forming a hexasome-like intermediate

Burgos‐Bravo, F., Tong, A., Li, C., Díaz-Celis, C., Kaplan, C. D., LeRoy, G., Reinberg, D., & Bustamante, C. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.05.002 · Cited by 11

Chromatin architecture mapping by multiplex proximity tagging

Delamarre, A., Bailey, B. M., Yavid, J., Koche, R. P., Mohibullah, N., & Whitehouse, I. (2024) · Molecular Cell · doi:10.1016/j.molcel.2025.06.018 · Cited by 10

Molecular mechanisms and functions of protein acetylation in sepsis and sepsis-associated organ dysfunction

Xu, Y.-F., Yang, N., Hao, P.-H., Wen, R., & Zhang, T. (2025) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-025-00773-z · Cited by 10

GeneBits: ultra-sensitive tumour-informed ctDNA monitoring of treatment response and relapse in cancer patients

Broche, J., Kelemen, O., Aishwarya, S., Schütz, L., Muyas, F., Forschner, A., Schroeder, C., & Ossowski, S. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-06993-3 · Cited by 10

SAGA mediates transcription from the TATA-like element independently of Taf1p/TFIID but dependent on core promoter structures in Saccharomyces cerevisiae

Watanabe, K., & Kokubo, T. (2017) · PLoS ONE · doi:10.1371/journal.pone.0188435 · Cited by 10

Complex context relationships between DNA methylation and accessibility, histone marks, and hTERT gene expression in acute promyelocytic leukemia cells: perspectives for all‐trans retinoic acid in cancer therapy

Garsuault, D., Bouyer, C., Nguyen, É., Kandhari, R., Prochazkova‐Carlotti, M., Chevret, E., Forgez, P., & Ségal‐Bendirdjian, E. (2020) · Molecular Oncology · doi:10.1002/1878-0261.12681 · Cited by 10

The roles of transcription, chromatin organisation and chromosomal processes in holocentromere establishment and maintenance

Wang, Y., Wu, L., & Yuen, K. W. Y. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.01.004 · Cited by 10

The AtMYB44 promoter is accessible to signals that induce different chromatin modifications for gene transcription

Nguyen, N. H., & Cheong, J. (2018) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2018.06.030 · Cited by 10

Interplay between the transcription preinitiation complex and the +1 nucleosome

Chen, X., & Xu, Y. (2024) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2023.12.001 · Cited by 9

The Role of Epigenetic Mechanisms in the Pathogenesis of Hepatitis C Infection

Żychowska, J., Ćmil, M., Skórka, P., Olejnik-Wojciechowska, J., Plewa, P., Bakinowska, E., Kiełbowski, K., & Pawlik, A. (2024) · Biomolecules · doi:10.3390/biom14080986 · Cited by 9

Nuclear warfare: pathogen manipulation of the nuclear pore complex and nuclear functions

Steiert, B. P., & Weber, M. M. (2025) · mBio · doi:10.1128/mbio.01940-24 · Cited by 9

AlphaFold-guided structural analyses of nucleosome binding proteins

Yang, X., Zhu, H., Shi, L., Song, T., Gong, W., He, S., Shan, S., Xu, C., & Zhou, Z. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf735 · Cited by 9

Replication-Independent Histone Turnover Underlines the Epigenetic Homeostasis in Adult Heart

Li, Y., Ai, S., Yu, X., Li, C., Li, X., Yue, Y., Wei, Y., Li, C., & He, A. (2019) · Circulation Research · doi:10.1161/circresaha.118.314366 · Cited by 9

Epigenetic processes in Alzheimer's disease

Castanho, I., & Lunnon, K. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813796-3.00008-0 · Cited by 10

Chromatin remodelers as active Brownian dimers

Blossey, R., & Schießel, H. (2019) · Journal of Physics A Mathematical and Theoretical · doi:10.1088/1751-8121/aafea0 · Cited by 9

The coupled effect of nucleosome organization on gene transcription level and transcriptional plasticity

Chen, J., Li, E., & Lai, J. (2017) · Nucleus · doi:10.1080/19491034.2017.1402152 · Cited by 9

Nucleosome Dynamics Derived at the Single-Molecule Level Bridges Its Structures and Functions

Chen, P., Li, G., & Li, W. (2024) · JACS Au · doi:10.1021/jacsau.3c00658 · Cited by 8

Antisense-mediated repression of SAGA-dependent genes involves the HIR histone chaperone

Soudet, J., Beyrouthy, N., Pastucha, A., Maffioletti, A., Menéndez, D., Bakir, Z., & Stutz, F. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac264 · Cited by 8

Different elongation factors distinctly modulate RNA polymerase II transcription in Arabidopsis

Obermeyer, S., Schrettenbrunner, L., Stöckl, R., Schwartz, U., & Grasser, K. D. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad825 · Cited by 8

Structural and dynamic studies of chromatin by solid-state NMR spectroscopy

Jaroniec, C. P. (2024) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2024.102921 · Cited by 9

Deregulated levels of RUVBL1 induce transcription-dependent replication stress

Hristova, R. H., Stoynov, S., Tsaneva, I. R., & Gospodinov, A. G. (2020) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2020.105839 · Cited by 8

Alterations in chromatin at antigen receptor loci define lineage progression during B lymphopoiesis

Lion, M., Muhire, B. M., Namiki, Y., Tolstorukov, M. Y., & Oettinger, M. A. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1914923117 · Cited by 8

Nucleosome Assembly and Disassembly in vitro Are Governed by Chemical Kinetic Principles

Zhao, H., Guo, M., Zhang, F., Shao, X., Liu, G., Xing, Y., Zhao, X., Luo, L., & Cai, L. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.762571 · Cited by 8

Genome-wide identification of accessible chromatin regions in bumblebee by ATAC-seq

Zhao, X., Su, L., Xu, W., Schaack, S., & Sun, C. (2020) · Scientific Data · doi:10.1038/s41597-020-00713-w · Cited by 8

CODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate the histone supply

Jeong, T.-K., Frater, R. C. M., Yoon, J., Groth, A., & Song, J.-J. (2025) · Nature Communications · doi:10.1038/s41467-025-56976-7 · Cited by 8

Biotin Induces Inactive Chromosome X Reactivation and Corrects Physiopathological Alterations in Beta-Propeller-Protein-Associated Neurodegeneration

Reche-López, D., Romero-González, A., Álvarez-Córdoba, M., Suárez-Carrillo, A., Cilleros-Holgado, P., Piñero-Pérez, R., Gómez-Fernández, D., Romero-Domínguez, J. M., López-Cabrera, A., González-Granero, S., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26031315 · Cited by 7

Rate-limiting enzymes in nucleotide metabolism synchronize nucleotide biosynthesis and chromatin formation

Srivastava, S., Samaniego‐Castruita, D., Srivastava, S., Khurana, S., Rehman, J., Shukla, V., Ben‐Sahra, I., & Foltz, D. R. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.11.009 · Cited by 7

How ATP-Dependent Chromatin Remodeling Complexes Regulate Vertebrate Embryonic Development

Wang, H., Anwaier, G., 白生宾, Liao, L., Wang, Y., & Li, S. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27020835 · Cited by 7

Chromatin Dynamics: Chromatin Remodeler, Epigenetic Modification and Diseases

Cui, G., Dong, Q., Gai, K., & Qi, S. (2023) · IntechOpen eBooks · doi:10.5772/intechopen.108385 · Cited by 7

Poly(dA:dT) Tracts Differentially Modulate Nucleosome Remodeling Activity of RSC and ISW1a Complexes, Exerting Tract Orientation-Dependent and -Independent Effects

Amigo, R., Raiqueo, F., Tarifeño-Saldivia, E., Farkas, C., & Gutiérrez, J. L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015245 · Cited by 7

Histone 3.3-related chromatinopathy: missense variants throughout H3-3A and H3-3B cause a range of functional consequences across species

Bryant, L. M., Sangree, A. K., Clark, K., & Bhoj, E. J. K. (2023) · Human Genetics · doi:10.1007/s00439-023-02536-2 · Cited by 7

Gold labelling of a green fluorescent protein (GFP)-tag inside cells using recombinant nanobodies conjugated to 2.4 nm thiolate-coated gold nanoparticles

Groysbeck, N., Donzeau, M., Stoessel, A., Haeberlé, A., Ory, S., Spehner, D., Schultz, P., Ersen, O., Bahri, M., Ihiawakrim, D., et al. (2021) · Nanoscale Advances · doi:10.1039/d1na00256b · Cited by 7

Loop-seq: A high-throughput technique to measure the mesoscale mechanical properties of DNA

Basu, A. (2021) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2021.08.011 · Cited by 7

Advancing towards a global mammalian gene regulation model through single-cell analysis and synthetic biology

Tycko, J., Van, M. V., Elowitz, M. B., & Bintu, L. (2017) · Current Opinion in Biomedical Engineering · doi:10.1016/j.cobme.2017.10.011 · Cited by 7

Chemical map-based prediction of nucleosome positioning using the Bioconductor package nuCpos

Kato, H., Shimizu, M., & Urano, T. (2021) · BMC Bioinformatics · doi:10.1186/s12859-021-04240-2 · Cited by 7

Inference of tumor cell-specific transcription factor binding from cell-free DNA enables tumor subtype prediction and early detection of cancerPreprint

Ulz, P., Perakis, S., Zhou, Q., Moser, T., Belic, J., Lazzeri, I., Wölfler, A., Zebisch, A., Gerger, A., Pristauz, G., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/456681 · Cited by 7

Intrinsically Disordered Regions Define Unique Protein Interaction Networks in CHD Family Remodelers

Tabar, M. S., Parsania, C., Giardina, C., Feng, Y., Wong, A. C. H., Metierre, C., Nagarajah, R., Dhungel, B. P., Rasko, J. E. J., & Bailey, C. G. (2025) · The FASEB Journal · doi:10.1096/fj.202402808rr · Cited by 7

Expression of LINE-1 elements is required for preimplantation development and totipotency

Ma, R., Xiao, N., & Liu, N. (2025) · Genes & Diseases · doi:10.1016/j.gendis.2025.101555 · Cited by 7

Roles of histone chaperone Nap1 and histone acetylation in regulating phase-separation of nucleosome arrays

Gao, J., Li, H., Tan, S., Zhou, R., & Lee, T.-H. (2025) · Nature Communications · doi:10.1038/s41467-025-65701-3 · Cited by 7

Conserved HSFA1-dependent chromatin dynamics drive heat stress responses in plants

Yen, M.-J., Lin, K., Thalimaraw, L., Yang, H.-R., Boonyaves, K., Cheng, C.-Y., & Wu, T. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116714 · Cited by 6

Recognition and remodelling of nucleosomes and hexasomes by the human INO80 complex

Aggarwal, P., Sharma, M., Woike, S., Kunert, F., Brem, A., Moldt, M., & Hopfner, K. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag138 · Cited by 6

Molecular perspectives in hypertrophic heart disease: An epigenetic approach from chromatin modification

Lizcano, F., & Bustamante, L. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1070338 · Cited by 6

The Role of Epigenetic Modifier Mutations in Peripheral T-Cell Lymphomas

Țigu, A. B., & Bancos, A. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45110563 · Cited by 6

Assessing DNA methylation of ATG 5 and MAP1LC3Av1 gene in oral squamous cell carcinoma and oral leukoplakia- a cross sectional study

Raja, N., Ganesan, A., Lakshmi, K. C., & Aniyan, Y. (2024) · Journal of Oral Biology and Craniofacial Research · doi:10.1016/j.jobcr.2024.07.001 · Cited by 6

Targeting DNA junction sites by bis-intercalators induces topological changes with potent antitumor effects

Huang, S.-C., Chen, C.-W., Satange, R., Hsieh, C., Chang, C.-C., Wang, S.-C., Peng, C.-L., Chen, T., Chiang, M., Horng, Y., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae643 · Cited by 6

Nanoscale Characterization of Interaction of Nucleosomes with H1 Linker Histone

Rafa, A. Y., Filliaux, S., & Lyubchenko, Y. L. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms26010303 · Cited by 6

Inositide-Dependent Nuclear Signalling in Health and Disease

Follo, M. Y., Ratti, S., Manzoli, L., Ramazzotti, G., Faenza, I., Fiume, R., Mongiorgi, S., Suh, P. G., McCubrey, J. A., & Cocco, L. (2019) · Handbook of experimental pharmacology · doi:10.1007/164_2019_321 · Cited by 6

Mass Spectrometry-Based Proteomics: Analyses Related to Drug-Resistance and Disease Biomarkers

Agostini, M., Traldi, P., & Hamdan, M. H. (2023) · Medicina · doi:10.3390/medicina59101722 · Cited by 6

Job Opening for Nucleosome Mechanic: Flexibility Required

Pitman, M., Melters, D. P., & Dalal, Y. (2020) · Cells · doi:10.3390/cells9030580 · Cited by 6

GlcNAc is a mast-cell chromatin-remodeling oncometabolite that promotes systemic mastocytosis aggressiveness

Agopian, J., Costa, Q. D., Nguyen, Q. V., Scorrano, G., Kousteridou, P., Yuan, M., Chelbi, R., Goubard, A., Castellano, R., Maurizio, J., et al. (2021) · Blood · doi:10.1182/blood.2020008948 · Cited by 6

Introducing the PARCH Scale for Quantifying the Hydropathy of Nucleic Acids and Nucleic Acid–Protein Complexes

Mandal, R., Ji, J.-J., Sheridan, C. N., Baur, A., Noel, A. C., & Nangia, S. (2025) · Langmuir · doi:10.1021/acs.langmuir.5c01051 · Cited by 5

Disruption of histone acetylation homeostasis reveals multilayered chromatin regulation for transcriptional resiliency

Venu, V., Small, E. M., Roth, C., Adikari, S., Vlot, A. H. C., Sullivan, K. A., Abeyratne, C. R., Jacobson, D., Starkenburg, S. R., Sanbonmatsu, K. Y., et al. (2025) · Epigenetics & Chromatin · doi:10.1186/s13072-025-00631-4 · Cited by 6

Transcriptional patterns and histone modification signatures reveal dehydration memory behaviour in seedlings of Gossypium hirsutum

He, S., Zhang, P., Wang, Y., Zheng, R., Li, Y., Cheng, H. S., Lv, D., Sun, Y., & Miao, C. (2024) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2024.105663 · Cited by 5

Nonequilibrium switching of segmental states can influence compaction of chromatin

Sahoo, S., Kadam, S., Padinhateeri, R., & Kumar, P. B. S. (2024) · Soft Matter · doi:10.1039/d4sm00274a · Cited by 5

Always on the Move: Overview on Chromatin Dynamics within Nuclear Processes

de Fenffe, C. M. D., Govers, J., & Mattiroli, F. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00114 · Cited by 10

Nucleosome Structure and Function

Chodaparambil, J. V., Edayathumangalam, R. S., Bao, Y., Park, Y., & Luger, K. (2006) · Springer eBooks · doi:10.1007/3-540-37633-x_2 · Cited by 24

Rules and regulation in the primary structure of chromatin

Rando, O. J., & Ahmad, K. (2007) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2007.04.006 · Cited by 119

Mechanisms of Nucleosome Dynamics In VivoPreprint

Henikoff, S. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026666 · Cited by 27

Dynamic nucleosomes

Luger, K. (2006) · Chromosome Research · doi:10.1007/s10577-005-1026-1 · Cited by 172