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Chromatin Compaction by Human MeCP2
Open accessAbstract
MeCP2 is a transcriptional repressor that contains an N-terminal methylated DNA-binding domain, a central transcription regulation domain, and a C-terminal domain of unknown function. Whereas current models of MeCP2 function evoke localized recruitment of histone deacetylases to specific methylated regions of the genome, it is unclear whether MeCP2 requires DNA methylation to bind to chromatin or whether MeCP2 binding influences chromatin structure in the absence of other proteins. To address these issues, we have characterized the complexes formed between MeCP2 and biochemically defined nucleosomal arrays. At molar ratios near 1 MeCP2/nucleosome, unmethylated nucleosomal arrays formed both extensively condensed ellipsoidal particles and oligomeric suprastructures. Furthermore, MeCP2-mediated chromatin compaction occurred in the absence of monovalent or divalent cations, in distinct contrast to all other known chromatin-condensing proteins. Analysis of specific missense and nonsense MeCP2 mutants indicated that the ability to condense chromatin resides in region(s) of the protein other than the methylated DNA-binding domain. These data demonstrate that MeCP2 assembles novel secondary chromatin structures independent of DNA modification and suggest that the ability of MeCP2 to silence chromatin may be related in part to its effects on large-scale chromatin organization.
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“However, MeCP2 may also facilitate transcriptional activation [77], chromatin compaction [78,79] and mRNA splicing [80,81], while also interacting with a host of other regulatory proteins involved in a variety of molecular pathways [81–84].”
From Rett syndrome: a neurological disorder with metabolic components (2018) · cites this paper as [78]
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Nan, X., Ng, H.-H., Johnson, C. A., Laherty, C. D., Turner, B. M., Eisenman, R. N., & Bird, A. (1998) · Nature · doi:10.1038/30764 · Cited by 3,440
Methylated DNA and MeCP2 recruit histone deacetylase to repress transcription
Jones, P. L., Veenstra, G. J. C., Wade, P. A., Vermaak, D., Kass, S. U., Landsberger, N., Strouboulis, J., & Wolffe, A. P. (1998) · Nature Genetics · doi:10.1038/561 · Cited by 2,791
Self-citationThe DNA methyltransferases of mammals
Bestor, T. H. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.16.2395 · Cited by 2,078
Methylation-Induced Repression— Belts, Braces, and Chromatin
Bird, A. P., & Wolffe, A. P. (1999) · Cell · doi:10.1016/s0092-8674(00)81532-9 · Cited by 1,858
Lewis, J. D., Meehan, R. R., Henzel, W. J., Maurer-Fogy, I., Jeppesen, P., Klein, F., & Bird, A. (1992) · Cell · doi:10.1016/0092-8674(92)90610-o · Cited by 1,371
MeCP2 Is a Transcriptional Repressor with Abundant Binding Sites in Genomic Chromatin
Nan, X., Campoy, F. J., & Bird, A. P. (1997) · Cell · doi:10.1016/s0092-8674(00)81887-5 · Cited by 1,288
Bednář, J., Horowitz, R. A., Grigoryev, S. A., Carruthers, L. M., Hansen, J. C., Koster, A. J., & Woodcock, C. L. F. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.24.14173 · Cited by 593
Self-citationConformational Dynamics of the Chromatin Fiber in Solution: Determinants, Mechanisms, and Functions
Hansen, J. C. (2002) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.31.101101.140858 · Cited by 556
Self-citationCharacterization of MeCP2, a vertebrate DNA binding protein with affinity for methylated DNA
Meehan, R. R., Lewis, J., & Bird, A. P. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.19.5085 · Cited by 527
Corepressor-Dependent Silencing of Chromosomal Regions Encoding Neuronal Genes
Lunyak, V. V., Burgess, R., Prefontaine, G. G., Nelson, C., Sze, S.-H., Chenoweth, J., Schwartz, P., Pevzner, P. A., Glass, C., Mandel, G., et al. (2002) · Science · doi:10.1126/science.1076469 · Cited by 472
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Items 101–200 of 305
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Grigoryev, S. A., Bulynko, Y. A., & Popova, E. Y. (2006) · Chromosome Research · doi:10.1007/s10577-005-1021-6 · Cited by 58
MECP2 genomic structure and function: insights from ENCODE
Singh, J., Saxena, A., Christodoulou, J., & Ravine, D. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn591 · Cited by 60
MicroRNAs in addiction: adaptation's middlemen?
Li, M. D., & van der Vaart, A. D. (2011) · Molecular Psychiatry · doi:10.1038/mp.2011.58 · Cited by 57
Mechanisms of Disease: neurogenetics of MeCP2 deficiency
Francke, U. (2006) · Nature Clinical Practice Neurology · doi:10.1038/ncpneuro0148 · Cited by 56
Ishibashi, T., Thambirajah, A. A., & Ausió, J. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.03.005 · Cited by 55
The role of genetics in the establishment and maintenance of the epigenome
Huidobro, C., Fernández, A. F., & Fraga, M. F. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1296-2 · Cited by 55
Brain-Derived Neurotrophic Factor and Rett Syndrome
Katz, D. M. (2014) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-45106-5_18 · Cited by 53
Organization of interphase chromatin
Horowitz-Scherer, R. A., & Woodcock, C. L. F. (2005) · Chromosoma · doi:10.1007/s00412-005-0035-3 · Cited by 52
Self-citationLudwig, A. K., Zhang, P., & Cardoso, M. C. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00115 · Cited by 56
DNA damage repair and transcription
Bowen, N. J., Palmer, M. B., & Wade, P. A. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4177-x · Cited by 53
Self-citationRett syndrome and the urge of novel approaches to study MeCP2 functions and mechanisms of action
Bedogni, F., Rossi, R. L., Galli, F., Cobolli Gigli, C., Gandaglia, A., Kilstrup-Nielsen, C., & Landsberger, N. (2014) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2014.01.011 · Cited by 51
Casas-Delucchi, C. S., Becker, A., Bolius, J. J., & Cardoso, M. C. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks784 · Cited by 51
The role of CTCF in regulating nuclear organization
Williams, A., & Flavell, R. A. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20080066 · Cited by 50
Proteins That Read DNA Methylation
Shimbo, T., & Wade, P. A. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-43624-1_13 · Cited by 54
Self-citationSwitching between Epigenetic States at Pericentromeric Heterochromatin
Déjardin, J. (2015) · Trends in Genetics · doi:10.1016/j.tig.2015.09.003 · Cited by 47
Merging Data from Genetic and Epigenetic Approaches to Better Understand Autistic Spectrum Disorder
Grayson, D. R., & Guidotti, A. (2015) · Epigenomics · doi:10.2217/epi.15.92 · Cited by 51
MeCP2 and Chromatin Compartmentalization
Schmidt, A., Zhang, H., & Cardoso, M. C. (2020) · Cells · doi:10.3390/cells9040878 · Cited by 51
Springhetti, E. M., Istomina, N. E., Whisstock, J. C., Tv, N., Woodcock, C. L. F., & Grigoryev, S. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307635200 · Cited by 49
Self-citationErb, T. M., Schneider, C., Mucko, S. E., Sanfilippo, J. S., Lowry, N., Desai, M. N., Mangoubi, R., Leuba, S. H., & Sammak, P. J. (2011) · Stem Cells and Development · doi:10.1089/scd.2010.0281 · Cited by 48
Role of Mecp2 in Experience-Dependent Epigenetic Programming
Zimmermann, C. A., Hoffmann, A., Raabe, F. J., & Spengler, D. (2015) · Genes · doi:10.3390/genes6010060 · Cited by 51
Ausió, J. (2016) · Clinical Epigenetics · doi:10.1186/s13148-016-0214-5 · Cited by 49
Keeping fingers crossed: heterochromatin spreading through interdigitation of nucleosome arrays
Grigoryev, S. A. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00258-3 · Cited by 48
MeCP2 in Rett syndrome: transcriptional repressor or chromatin architectural protein?
Chadwick, L. H., & Wade, P. A. (2007) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2007.02.003 · Cited by 46
Self-citationIntracellular manipulation of chromatin using magnetic nanoparticles
Kanger, J. S., Subramaniam, V., & DRIEL, R. V. (2008) · Chromosome Research · doi:10.1007/s10577-008-1239-1 · Cited by 47
Sulforaphane modulates telomerase activity via epigenetic regulation in prostate cancer cell lines
Abbas, A., Hall, J. A., Patterson, W. L., Ho, E., Hsu, A., Al‐Mulla, F., & Georgel, P. T. (2015) · Biochemistry and Cell Biology · doi:10.1139/bcb-2015-0038 · Cited by 46
Self-citationCohen, S., Zhou, Z., & Greenberg, M. E. (2008) · Science · doi:10.1126/science.1159146 · Cited by 48
McGowan, S., Buckle, A. M., Irving, J. A., Ong, P. C., Bashtannyk-Puhalovich, T. A., Kan, W., Henderson, K. N., Bulynko, Y. A., Popova, E. Y., Smith, A. I., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601201 · Cited by 46
Zhang, H., Romero, H., Schmidt, A., Gagova, K., Qin, W., Bertulat, B., Lehmkuhl, A., Milden, M., Eck, M., Meckel, T., et al. (2022) · Nucleus · doi:10.1080/19491034.2021.2024691 · Cited by 44
Mild Overexpression of Mecp2 in Mice Causes a Higher Susceptibility toward Seizures
Bodda, C., Tantra, M., Mollajew, R., Arunachalam, J. P., Laccone, F. A., Can, K., Rosenberger, A., Mironov, S. L., Ehrenreich, H., & Mannan, A. U. (2013) · American Journal Of Pathology · doi:10.1016/j.ajpath.2013.03.019 · Cited by 44
Griffiths, R., & Whitehouse, A. (2007) · Journal of Virology · doi:10.1128/jvi.02171-06 · Cited by 43
Thatcher, K. N., & LaSalle, J. M. (2006) · Epigenetics · doi:10.4161/epi.1.1.2339 · Cited by 45
McBryant, S. J., Krause, C., Woodcock, C. L. F., & Hansen, J. C. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01389-07 · Cited by 44
Self-citationThe Molecular Functions of MeCP2 in Rett Syndrome Pathology
Sharifi, O., & Yasui, D. H. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.624290 · Cited by 49
Fibrogenic Activity of MECP2 Is Regulated by Phosphorylation in Hepatic Stellate Cells
Morán‐Salvador, E., Macia, M. G., Sivaharan, A., Sabater, L., Zaki, M. Y. W., Oakley, F., Knox, A., Page, A., Luli, S., Mann, J., et al. (2019) · Gastroenterology · doi:10.1053/j.gastro.2019.07.029 · Cited by 43
The contribution of epigenetics to understanding genetic factors in autism
Hall, L., & Kelley, E. A. (2013) · Autism · doi:10.1177/1362361313503501 · Cited by 48
Dissecting MECP2 function in the central nervous system
Kishi, N., & Macklis, J. D. (2005) · Journal of Child Neurology · doi:10.1177/08830738050200082501 · Cited by 42
Babbio, F., Castiglioni, I., Cassina, C., Gariboldi, M. B., Pistore, C., Magnani, E., Badaracco, G., Monti, E., & Bonapace, I. M. (2012) · BMC Cell Biology · doi:10.1186/1471-2121-13-19 · Cited by 40
Role of metabolic programming in the pathogenesis of β-cell failure in postnatal life
Simmons, R. A. (2007) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-007-9045-1 · Cited by 43
Direct Homo- and Hetero-Interactions of MeCP2 and MBD2
Becker, A., Allmann, L., Hofstätter, M., Casà, V., Weber, P., Lehmkuhl, A., Herce, H. D., & Cardoso, M. C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053730 · Cited by 42
Genomic insights into MeCP2 function: A role for the maintenance of chromatin architecture
Connolly, D. R., & Zhou, Z. (2019) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2019.07.002 · Cited by 40
Bertulat, B., Bonis, M. L. D., Ragione, F. D., Lehmkuhl, A., Milden, M., Storm, C., Jost, K. L., Scala, S., Hendrich, B., D’Esposito, M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047848 · Cited by 36
Epigenetic Factors that Control Pericentric Heterochromatin Organization in Mammals
Fioriniello, S., Marano, D., Fiorillo, F., D’Esposito, M., & Ragione, F. D. (2020) · Genes · doi:10.3390/genes11060595 · Cited by 39
Structure-specific binding of MeCP2 to four-way junction DNA through its methyl CpG-binding domain
Galvão, T. C. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki971 · Cited by 39
Angrisano, T., Lembo, F., Peluso, S., Keller, S., Chiariotti, L., & Pero, R. (2012) · Medical Microbiology and Immunology · doi:10.1007/s00430-011-0227-9 · Cited by 38
Nucleosome Interactions and Stability in an Ordered Nucleosome Array Model System
Blacketer, M. J., Feely, S. J., & Shogren‐Knaak, M. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.140061 · Cited by 37
Poly(ADP-ribosyl)ation of Methyl CpG Binding Domain Protein 2 Regulates Chromatin Structure
Becker, A., Zhang, P., Allmann, L., Meilinger, D., Bertulat, B., Eck, D., Hofstaetter, M., Bartolomei, G., Hottiger, M. O., Schreiber, V., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.698357 · Cited by 37
To the 30-nm chromatin fiber and beyond
Adkins, N. L., Watts, M., & Georgel, P. T. (2003) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2003.09.013 · Cited by 39
Self-citationKucukkal, T. G., Yang, Y., Chapman, S. C., Cao, W., & Alexov, E. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15069670 · Cited by 40
Mok, R. S. F., Zhang, W., Sheikh, T. I., Pradeepan, K. S., Fernandes, I. R., DeJong, L. C., Benigno, G., Hildebrandt, M. R., Mufteev, M., Rodrigues, D. C., et al. (2022) · Translational Psychiatry · doi:10.1038/s41398-022-02216-1 · Cited by 35
Three-dimensional genome organization in interphase and its relation to genome function
Götze, S., Langerak, J. M., & DRIEL, R. V. (2007) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2007.08.007 · Cited by 35
Exploring the complexity of MECP2 function in Rett syndrome
Liu, Y., Whitfield, T. W., Bell, G. W., Guo, R., Flamier, A., Young, R. A., & Jaenisch, R. (2025) · Nature reviews. Neuroscience · doi:10.1038/s41583-025-00926-1 · Cited by 39
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Koch, C., & Strätling, W. H. (2004) · Biochemistry · doi:10.1021/bi0359271 · Cited by 35
Claveria‐Gimeno, R., Lanuza, P. M., Morales-Chueca, I., Jorge-Torres, O. C., Vega, S., Abián, O., Esteller, M., & Velázquez‐Campoy, A. (2017) · Scientific Reports · doi:10.1038/srep41635 · Cited by 32
Kaipananickal, H., Bayles, R., Ciccotosto, G. D., Maxwell, S., Cappai, R., Pelka, G. J., Tam, P., Christodoulou, J., & El‐Osta, A. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.4675-09.2010 · Cited by 31
Cell type–specific 3D-genome organization and transcription regulation in the brain
Liu, S., Wang, C. Y., Zheng, P., Jia, B. B., Zemke, N. R., Ren, P., Park, H. L., Ren, B., & Zhuang, X. (2025) · Science Advances · doi:10.1126/sciadv.adv2067 · Cited by 34
Hansen, J. C., Wexler, B. B., Rogers, D. J., Hite, K. C., Panchenko, T., Ajith, S., & Black, B. E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.234609 · Cited by 30
Self-citationBergo, A., Strollo, M., Gai, M., Barbiero, I., Stefanelli, G., Sertic, S., Gigli, C. C., Cunto, F. D., Kilstrup‐Nielsen, C., & Landsberger, N. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.608125 · Cited by 29
Yaqinuddin, A., Abbas, F., Naqvi, S. Z., Bashir, M. U., Qazi, R., & Qureshi, S. A. (2008) · Bioscience Reports · doi:10.1042/bsr20080032 · Cited by 26
Impaired in vivo binding of MeCP2 to chromatin in the absence of its DNA methyl-binding domain
Stuss, D. P., Cheema, M., Ng, M. K., de Paz, A. M., Williamson, B., Missiaen, K. K., Cosman, J. D., McPhee, D., Esteller, M., Hendzel, M. J., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt213 · Cited by 27
Grayson, T., Murphy, T. V., & Sandow, S. L. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.02.022 · Cited by 25
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Zhang, T., Meng, J., Liu, X., Zhang, X., Peng, X., Cheng, Z., & Zhang, F. (2017) · Oncotarget · doi:10.18632/oncotarget.22176 · Cited by 28
Zalosnik, M. I., Fabio, M. C., Bertoldi, M. L., Castañares, C., & Degano, A. L. (2021) · Scientific Reports · doi:10.1038/s41598-021-90517-8 · Cited by 24
MeCP2 and transcriptional control of eukaryotic gene expression
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Thambirajah, A. A., Eubanks, J. H., & Ausió, J. (2009) · BioEssays · doi:10.1002/bies.200800220 · Cited by 24
Neier, K. E., Grant, T. E., Palmer, R. L., Chappell, D., Hakam, S. M., Yasui, K. M., Rolston, M., Settles, M. L., Hunter, S. S., Madany, A. M., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02915-3 · Cited by 26
Sheikh, T. I., Harripaul, R., Ayub, M., & Vincent, J. B. (2018) · Human Mutation · doi:10.1002/humu.23409 · Cited by 24
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Cusack, S. M., Rohn, T. T., Medeck, R. J., Irwin, K. M., Brown, R. J., Mercer, L. M., & Oxford, J. T. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.05.035 · Cited by 23
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Chua, G. N. L., Watters, J. W., Olinares, P. D. B., Begum, M., Vostal, L. E., Luo, J. A., Chait, B. T., & Liu, S. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01373-9 · Cited by 25
Extending MeCP2 interactome: canonical nucleosomal histones interact with MeCP2
Ortega-Alarcón, D., Claveria‐Gimeno, R., Vega, S., Kalani, L., Jorge-Torres, O. C., Esteller, M., Ausió, J., Abián, O., & Velázquez‐Campoy, A. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae051 · Cited by 22
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Brero, A., Leonhardt, H., & Cardoso, M. C. (2006) · Springer eBooks · doi:10.1007/3-540-31390-7_2 · Cited by 24
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Zemach, A., Gaspan, O., & Grafi, G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706221200 · Cited by 22
Jost, K. L., Rottach, A., Milden, M., Bertulat, B., Becker, A., Wolf, P., Sandoval, J., Petazzi, P., Huertas, D., Esteller, M., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026499 · Cited by 23
Duncan, J. R. (2012) · ISRN Neurology · doi:10.5402/2012/972607 · Cited by 22
Marshall, K. L., Wang, J., Ji, T., & Rivera, R. M. (2018) · Animal Reproduction · doi:10.21451/1984-3143-ar2018-0087 · Cited by 21
Plasma membrane and brain dysfunction of the old: Do we age from our membranes?
Martín, M. G., & Dotti, C. G. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.1031007 · Cited by 24
Effect of DNA Groove Binder Distamycin A upon Chromatin Structure
Majumder, P., & Dasgupta, D. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026486 · Cited by 21
Hypermethylated LTR retrotransposon exhibits enhancer activity
Hu, T., Zhu, X., Pi, W., Yu, M., Shi, H., & Tuan, D. Y. H. (2017) · Epigenetics · doi:10.1080/15592294.2017.1289300 · Cited by 21
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LaSalle, J. M., Hogart, A., & Thatcher, K. N. (2005) · International review of neurobiology · doi:10.1016/s0074-7742(05)71006-0 · Cited by 21
Yakabe, S., Soejima, H., Yatsuki, H., Tominaga, H., Wei, Z., Higashimoto, K., Joh, K., Kudo, S., Miyazaki, K., & Mukai, T. (2008) · Genes & Genetic Systems · doi:10.1266/ggs.83.199 · Cited by 21
Shiraishi, M., Sekiguchi, A., Oates, A., Terry, M. J., Miyamoto, Y., & Sekiya, T. (2004) · Analytical Biochemistry · doi:10.1016/j.ab.2004.02.024 · Cited by 22
Cohesin Interaction with Centromeric Minichromosomes Shows a Multi-Complex Rod-Shaped Structure
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High Levels of MeCP2 Depress MHC Class I Expression in Neuronal Cells
Miralvès, J., Magdeleine, E., Kaddoum, L., Brun, H., Peries, S., & Joly, E. (2007) · PLoS ONE · doi:10.1371/journal.pone.0001354 · Cited by 19
Sharma, K., Singh, J., & Pillai, P. P. (2018) · Journal of Molecular Neuroscience · doi:10.1007/s12031-018-1112-4 · Cited by 18
Proteins in DNA methylation and their role in neural stem cell proliferation and differentiation
Sun, J., Yang, J., Miao, X., Loh, H. H., Pei, D., & Zheng, H. (2021) · Cell Regeneration · doi:10.1186/s13619-020-00070-4 · Cited by 19
Kifayathullah, L. A., Arunachalam, J. P., Bodda, C., Agbemenyah, H. Y., Laccone, F. A., & Mannan, A. U. (2010) · Cytogenetic and Genome Research · doi:10.1159/000315906 · Cited by 18
Alternative splicing variants and DNA methylation status of BDNF in inbred chicken lines
Yu, Y., Zhang, H., Byerly, M. S., Bacon, L. D., Porter, T. E., Liu, G. E., & Song, J. (2009) · Brain Research · doi:10.1016/j.brainres.2009.01.071 · Cited by 18
MBD4-Mediated Glycosylase Activity on a Chromatin Template Is Enhanced by Acetylation
Ishibashi, T., So, K., Cupples, C. G., & Ausió, J. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00588-08 · Cited by 18
MeCP2: the chromatin connection and beyond
Zlatanova, J. S. (2005) · Biochemistry and Cell Biology · doi:10.1139/o05-048 · Cited by 18
Hassan‐Zadeh, V., Rugg‐Gunn, P. J., & Bazett‐Jones, D. P. (2017) · Chromosoma · doi:10.1007/s00412-017-0625-x · Cited by 17
D'Annessa, I., Gandaglia, A., Brivio, E., Stefanelli, G., Frasca, A., Landsberger, N., & Di Marino, D. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.02.005 · Cited by 18
Functional assessment of MeCP2 in Rett syndrome and cancers of breast, colon, and prostate
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Ortega-Alarcón, D., Claveria‐Gimeno, R., Vega, S., Jorge-Torres, O. C., Esteller, M., Abián, O., & Velázquez‐Campoy, A. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.01.206 · Cited by 15
Liu, H., Li, H., Guo, L., Li, Z., Li, M., Jiang, W., Liu, X., McNutt, M. A., & Li, G. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.0908543 · Cited by 15
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Campos, M., Churchman, S. M., Santos-Rebouças, C. B., Ponchel, F., & Pimentel, M. M. G. (2009) · Journal of Molecular Neuroscience · doi:10.1007/s12031-009-9296-2 · Cited by 14
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Metadata
- Authors
- Georgel, P. T., Horowitz-Scherer, R. A., Adkins, N., Woodcock, C. L., Wade, P. A., & Hansen, J. C.
- Affiliations
- The University of Texas at San Antonio Health Science Center (US)
- University of Massachusetts Amherst (US)
- Marshall University (US)
- Emory University (US)
- Corresponding author
- Wade, Paul A.
- Hansen, Jeffrey C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-08
- Volume
- 278
- Issue
- 34
- Pages
- 32181-32188
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2042269850
- Cited by
- 305
- References
- 39
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 5 · 2023: 6 · 2022: 11 · 2021: 11 · 2020: 7 · 2019: 7 · 2018: 10 · 2017: 14 · 2016: 16 · 2015: 18 · 2014: 14 · 2013: 20 · 2012: 14
- FWCI
- 5.99
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Collection of Biostatistics Research Archive (COBRA) (submittedVersion)
- Funders
- National Institutes of Health (5k22hd001238-02, 5r01gm043786-11)
- National Institute of General Medical Sciences (GM 45916, GM43786)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (5K22HD01238)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Keywords
- MeCP2, chromatin condensation, nucleosome arrays, chromatin silencing, transcriptional repression, chromatin organization
- MeSH terms
- Chromatin, Chromosomal Proteins, Non-Histone, DNA-Binding Proteins, Humans, Recombinant Proteins, Repressor Proteins, Protein Structure, Secondary, DNA Methylation, Methyl-CpG-Binding Protein 2
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