RETRACTED: The Chromatin-Remodeling Complex WINAC Targets a Nuclear Receptor to Promoters and Is Impaired in Williams Syndrome
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We identified a human multiprotein complex (WINAC) that directly interacts with the vitamin D receptor (VDR) through the Williams syndrome transcription factor (WSTF). WINAC has ATP-dependent chromatin-remodeling activity and contains both SWI/SNF components and DNA replication-related factors. The latter might explain a WINAC requirement for normal S phase progression. WINAC mediates the recruitment of unliganded VDR to VDR target sites in promoters, while subsequent binding of coregulators requires ligand binding. This recruitment order exemplifies that an interaction of a sequence-specific regulator with a chromatin-remodeling complex can organize nucleosomal arrays at specific local sites in order to make promoters accessible for coregulators. Furthermore, overexpression of WSTF could restore the impaired recruitment of VDR to vitamin D regulated promoters in fibroblasts from Williams syndrome patients. This suggests that WINAC dysfunction contributes to Williams syndrome, which could therefore be considered, at least in part, a chromatin-remodeling factor disease.
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Baz1b was chosen as the best candidate for MommeD10 because it contains a bromodomain and has been shown to form chromatin remodeling complexes and associate with replication foci and promoters.
“The linked interval for MommeD10 contains 52 genes and Baz1b was chosen as the best candidate because it contains a bromodomain (a domain commonly associated with chromatin remodelers) and has recently been shown to form at least two chromatin remodeling complexes and associate with replication foci and promoters [23-25].”
From A genome-wide screen for modifiers of transgene variegation identifies genes with critical roles in development (2008) · cites this paper as [24]
Baz1b is expressed in the mouse embryo from around 9.5 dpc and at 11.5 dpc in limb buds, tail and brain.
“It has previously been shown that Baz1b is expressed in the mouse embryo from around 9.5 dpc and whole mount in situ at 11.5 dpc showed expression in limb buds, tail and brain [24].”
From A genome-wide screen for modifiers of transgene variegation identifies genes with critical roles in development (2008) · cites this paper as [24]
Both MommeD5 and MommeD10 genes encode proteins involved in histone modification and chromatin remodeling.
“This is consistent with the fact that both genes encode proteins involved in histone modification and chromatin remodeling [21,23-25,30-33].”
From A genome-wide screen for modifiers of transgene variegation identifies genes with critical roles in development (2008) · cites this paper as [24]
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“28 ), Williams syndrome transcription factor (WSTF) in the chromatin-remodeling complex WINA”
BackgroundHypercalcemia in children and adolescents
Lietman, S. A., Germain‐Lee, E. L., & Levine, M. A. (2010) · Current Opinion in Pediatrics · doi:10.1097/mop.0b013e32833b7c23 · Cited by 136 · see citing works
“A common finding is increased sensitivity to vitamin D, which appears to be due to decreased ability of ligandbound vitamin D receptor (VDR) to mediate transrepression of the 25(OH)D3-1a-hydroxylase gene, CYP27B1.”
InfluentialBouillon, R. (2010) · Elsevier eBooks · doi:10.1016/b978-1-4160-5583-9.00058-7 · Cited by 135 · see citing works
Paredes, R., Arriagada, G., Cruzat, F., Villagra, A., Olate, J., Zaidi, K., van Wijnen, A. J., Lian, J. B., Stein, G. S., Stein, J. L., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.20.8847-8861.2004 · Cited by 135 · see citing works
SS18 Together with Animal-Specific Factors Defines Human BAF-Type SWI/SNF Complexes
Middeljans, E., Wan, X., Jansen, P. W., Sharma, V., Stunnenberg, H. G., & Logie, C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033834 · Cited by 133 · see citing works
Transrepressive Function of TLX Requires the Histone Demethylase LSD1
Yokoyama, A., Takezawa, S., Schüle, R., Kitagawa, H., & Kato, S. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02030-07 · Cited by 132 · see citing works
“The first group comprises ATP-dependent chromatin-remodeling complexes (such as the SWI/SNF complex), which reorganize nucleosomal arrays and potentiate the promoter accessibility of NRs (6, 18 , 23, 33).”
BackgroundSelf-citationBAF57 Governs Androgen Receptor Action and Androgen-Dependent Proliferation through SWI/SNF
Link, K. A., Burd, C. J., Williams, E., Marshall, T. W., Rosson, G. B., Henry, E. C., Weissman, B. E., & Knudsen, K. E. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.6.2200-2215.2005 · Cited by 131 · see citing works
“Several classes of chromatin remodeling complexes have been described, including WINAC, NuRD, ISWI, and SWI/SNF (4, 39 , 46, 70, 72).”
MethodAshe, A., Morgan, D. K., Whitelaw, N. C., Bruxner, T. J., Vickaryous, N. K., Cox, L. L., Butterfield, N. C., Wicking, C., Blewitt, M. E., Wilkins, S. J., et al. (2008) · Genome Biology · doi:10.1186/gb-2008-9-12-r182 · Cited by 117 · see citing works
“The linked interval for MommeD10 contains 52 genes and Baz1b was chosen as the best candidate because it contains a bromodomain (a domain commonly associated with chromatin remodelers) and has recently been shown to form at least two chromatin remodeling complexes and associate with replication foci and promoters [23-…”
Belandia, B., & Parker, M. G. (2003) · Cell · doi:10.1016/s0092-8674(03)00599-3 · Cited by 117 · see citing works
“Additional complexes continue to be discovered, including a novel ATP-dependent remodeling complex, termed WINAC, described recently by Kato and coworkers in Cell to play a role in vitamin D action (Kitagawa et al., 2003).”
Kim, M. S., Fujiki, R., Murayama, A., Kitagawa, H., Yamaoka, K., Yamamoto, Y., Mihara, M., Takeyama, K.-I., & Kato, S. (2006) · Molecular Endocrinology · doi:10.1210/me.2006-0231 · Cited by 114 · see citing works
“Luciferase assays were performed as described (31).”
Self-citationLinking the ubiquitin–proteasome pathway to chromatin remodeling/modification by nuclear receptors
Kinyamu, H. K., Chen, J., & Archer, T. (2005) · Journal of Molecular Endocrinology · doi:10.1677/jme.1.01680 · Cited by 112 · see citing works
“Conversely, it is known that the FACT complex associates with chromatin remodeling complexes found in the VDR complex WINAC, which also contains SWI/SNF and is required for NR function (Kitagawa et al. 2003).”
Mutations of RAI1, a PHD-containing protein, in nondeletion patients with Smith-Magenis syndrome
Bi, W., Saifi, G. M., Shaw, C. J., Walz, K., Fonseca, P., Wilson, M., Potocki, L., & Lupski, J. R. (2004) · Human Genetics · doi:10.1007/s00439-004-1187-6 · Cited by 110 · see citing works
“Many PHD-containing proteins regulate transcription by forming a multi-component chromatin-remodeling complex (Aasland et al. 1995; Kitagawa et al. 2003).”
In vitro nuclear interactome of the HIV-1 Tat protein
Gautier, V., Gu, L., O'Donoghue, N. M., Pennington, S. R., Sheehy, N., & Hall, W. W. (2009) · Retrovirology · doi:10.1186/1742-4690-6-47 · Cited by 108 · see citing works
Fujiki, R., Kim, M., Sasaki, Y., Yoshimura, K., Kitagawa, H., & Kato, S. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600853 · Cited by 109 · see citing works
“Although WSTF was previously shown to be involved in 1a(OH)ase gene regulation (Kitagawa et al, 2003; Kato et al, 2004), the function of WSTF, with respect to ligand- induced VDR/VDIR transrepression, remained unclear.”
BackgroundMethodResultInfluentialSelf-citationRetractedAndrogen receptor functions in male and female physiology
Μatsumoto, T., Shiina, H., Kawano, H., Sato, T., & Kato, S. (2008) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2008.03.023 · Cited by 107 · see citing works
Self-citationNuclear receptor coregulators merge transcriptional coregulation with epigenetic regulation
Kato, S., Yokoyama, A., & Fujiki, R. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.01.001 · Cited by 103 · see citing works
Self-citationAdvances in chromatin remodeling and human disease
Cho, K. S., Elizondo, L. I., & Boerkoel, C. F. (2004) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2004.04.015 · Cited by 100 · see citing works
“The transcription factor encoded by BAZ1B (bromodomain adjacent to zinc finger domain, 1B), a gene deleted in Williams syndrome, recruits BRG1 and BRM with their associated chromatin-remodeling factors to vitamin D regulated promoters (Figure 1i) [14 ,16,17].”
Bi, W., Ohyama, T., Nakamura, H., Yan, J., Visvanathan, J., Justice, M. J., & Lupski, J. R. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi085 · Cited by 97 · see citing works
“The PHD domain has been suggested to be a protein–protein interaction domain, and many PHD-containing proteins regulate transcription through a multicomponent chromatin remodeling complex (25,26).”
The HARE-HTH and associated domains
Aravind, L., & Iyer, L. M. (2012) · Cell Cycle · doi:10.4161/cc.11.1.18475 · Cited by 96 · see citing works
Dong, X., Lutz, W. H., Schroeder, T. M., Bachman, L. A., Westendorf, J. J., Kumar, R., & Griffin, M. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506516102 · Cited by 94 · see citing works
Smad3 activates the Sox9-dependent transcription on chromatin
Furumatsu, T., Ozaki, T., & Asahara, H. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.10.032 · Cited by 93 · see citing works
“…authors have reported that p300 plays a critical role for the activation of cAMP response element-binding protein-, MyoD-, p53-, or vitamin D receptor-dependent transcription on reconstituted chromatin (Asahara et al., 2001; Dilworth et al., 2004; Espinosa, & Emerson, 2001; Kitagawa et al., 2003).”
Functional diversity of ISWI complexes
Dirscherl, S., & Krebs, J. E. (2004) · Biochemistry and Cell Biology · doi:10.1139/o04-044 · Cited by 92 · see citing works
Nuclear Receptor Mediated Gene Regulation through Chromatin Remodeling and Histone Modifications
Kishimoto, M., Fujiki, R., Takezawa, S., Sasaki, Y., Nakamura, T., Yamaoka, K., Kitagawa, H., & Kato, S. (2006) · Endocrine Journal · doi:10.1507/endocrj.53.157 · Cited by 90 · see citing works
“tile aberrant vitamin D metabolism, including hypercalcemia [79].”
Self-citationJurutka, P. W., Thompson, P. D., Whitfield, G. K., Eichhorst, K. R., Hall, N., Dominguez, C. E., Hsieh, J., Haussler, C. A., & Haussler, M. R. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20359 · Cited by 86 · see citing works
Nuclear receptors and chromatin remodeling machinery
Trotter, K. W., & Archer, T. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2006.12.015 · Cited by 85 · see citing works
“In addition, SWI/SNF subunits have also been shown to interact with DNA replication factors such as CAF-1 and TOPO II within the Williams syndrome transcription factor (WSTF) complex, including WINAC (WSTF-Including Nucleosome Assembly Complex) (Kitagawa et al., 2003) (Fig.”
Coactivation of the N-terminal Transactivation of Mineralocorticoid Receptor by Ubc9
Yokota, K., Shibata, H., Kurihara, I., Kobayashi, S., Suda, N., Murai‐Takeda, A., Saito, I., Kitagawa, H., Kato, S., Saruta, T., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607741200 · Cited by 85 · see citing works
Self-citationRETRACTED: 1α,25(OH)2D3-induced DNA methylation suppresses the human CYP27B1 gene
Kim, M. S., Fujiki, R., Kitagawa, H., & Kato, S. (2007) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2006.12.014 · Cited by 83 · see citing works
Self-citationRetractedCuesta, I., Zaret, K. S., & Santisteban, P. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00758-07 · Cited by 79 · see citing works
“To study the molecular mechanism of TPO gene activation by FoxE1 in vivo, we sought to mimic the process in vitro with the TPO promoter sequence inserted into a phased nucleosome array (8, 28, 49, 50).”
Genetics and epigenetics of arrhythmia and heart failure
Duygu, B., Poels, E. M., & Martins, P. A. D. C. (2013) · Frontiers in Genetics · doi:10.3389/fgene.2013.00219 · Cited by 79 · see citing works
Igarashi, M., Yogiashi, Y., Mihara, M., Takada, I., Kitagawa, H., & Kato, S. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00813-07 · Cited by 79 · see citing works
Self-citationRetractedModifying chromatin to permit steroid hormone receptor-dependent transcription
Kinyamu, H. K., & Archer, T. (2003) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2003.09.015 · Cited by 78 · see citing works
Chen, J., Kinyamu, H. K., & Archer, T. (2005) · Molecular Endocrinology · doi:10.1210/me.2005-0192 · Cited by 76 · see citing works
Selective Regulation of Vitamin D Receptor-Responsive Genes by TFIIH
Drané, P., Compe, E., Catez, P., Chymkowitch, P., & Egly, J.-M. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.007 · Cited by 75 · see citing works
The Use of Mouse Models to Study EpigeneticsPreprint
Blewitt, M., & Whitelaw, E. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a017939 · Cited by 73 · see citing works
“Baz1b is a mammalian bromodomain-containing protein, which is part of two different chromatin-remodeling complexes (WINAC SWI/SNF and WICH ISWI-containing) bound at promoters and replication foci (Bozhenok et al. 2002; Kitagawa et al. 2003).”
BackgroundAnimal models of Williams syndrome
Osborne, L. R. (2010) · American Journal of Medical Genetics Part C Seminars in Medical Genetics · doi:10.1002/ajmg.c.30257 · Cited by 72 · see citing works
“Interestingly, the WINAC protein complex has also been shown to interact directly with the vitamin D receptor (VDR) where it mediates VDR recruitment and binding to target sites in the promoters of genes regulated by VDR, including key enzymes regulating vitamin D biosynthesis and catabolism [Kitagawa et al., 2003].”
BackgroundTerhune, S. S., Moorman, N. J., Cristea, I. M., Savaryn, J. P., Cuevas-Bennett, C., Rout, M. P., Chait, B. T., & Shenk, T. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1000965 · Cited by 70 · see citing works
Maturation of MicroRNA Is Hormonally Regulated by a Nuclear Receptor
Yamagata, K., Fujiyama, S., Ito, S., Ueda, T., Murata, T., Naitou, M., Takeyama, K., Minami, Y., O’Malley, B. W., & Kato, S. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.011 · Cited by 71 · see citing works
Self-citationRetractedKimura, S., Μatsumoto, T., Matsuyama, R., Shiina, H., Sato, T., Takeyama, K., & Kato, S. (2007) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2007.04.002 · Cited by 70 · see citing works
Self-citationHonjo, Y., Sasaki, S., Kobayashi, Y., Misawa, H., & Nakamura, H. (2006) · Journal of Endocrinology · doi:10.1677/joe.1.06105 · Cited by 69 · see citing works
“On the other hand, VDR has been recently reported to associate with the Williams syndrome transcription factor (WSTF) that has ATP-dependent chromatin-remodeling activity (Kitagawa et al. 2003).”
Role of Steroid Hormone Coregulators in Health and Disease
Thakur, M. K., & Paramanik, V. (2009) · Hormone Research in Paediatrics · doi:10.1159/000201107 · Cited by 68 · see citing works
“VDR interacts directly with a human multi-protein WINAC through the William syndrome transcription factor which contains both SWI/SNF components and DNA replication-related factors and exhibits ATP-dependent chromatin remodeling activity [”
BackgroundTakigawa, Y., Hata, K., Muramatsu, S., Amano, K., Ono, K., Wakabayashi, M., Matsuda, A., Takada, K., Nishimura, R., & Yoneda, T. (2010) · Journal of Cell Science · doi:10.1242/jcs.071373 · Cited by 68 · see citing works
“…a large molecular complex that regulates several processes of gene expression including chromatin remodeling, histone modification, transcription and splicing of the target genes during chondrogenesis (Maniatis and Reed, 2002; Carrozza et al., 2003; Kitagawa et al., 2003; Kameoka et al., 2004).”
Actin complexes in the cell nucleus: new stones in an old field
Castaño, E., Philimonenko, V. V., Kahle, M., Fukalová, J., Kalendová, A., Yildirim, S., Dzijak, R., Dingová, H., & Hozák, P. (2010) · Histochemistry and Cell Biology · doi:10.1007/s00418-010-0701-2 · Cited by 67 · see citing works
Khundmiri, S. J., Murray, R. D., & Lederer, E. D. (2016) · Comprehensive physiology · doi:10.1002/j.2040-4603.2016.tb00690.x · Cited by 66 · see citing works
“The essential requirement for this interaction has been demonstrated in vitro in knockdown experiments as well as in the skin fibroblasts of Williams Syndrome patients (49,177,338,339,354,355).”
Barnett, C., & Krebs, J. E. (2011) · Biochemistry and Cell Biology · doi:10.1139/o10-114 · Cited by 65 · see citing works
“This may reveal important differences in the tissues where the WICH and WINAC complexes assemble and highlights the potential for unique roles for these two WSTF-containing remodeling complexes during development (Kitagawa et al. 2003).”
InfluentialLi, J., Ma, M., & Wang, Z. (2007) · Environmental Toxicology and Chemistry · doi:10.1897/07-054.1 · Cited by 62 · see citing works
Vintermist, A., Böhm, S., Sadeghifar, F., Louvet, É., Mansén, A., Percipalle, P., & Farrants, A. Ö. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019184 · Cited by 61 · see citing works
Maki, A., Sawatsubashi, S., Ito, S., Shirode, Y., Suzuki, E., Zhao, Y., Yamagata, K., Kouzmenko, A., Takeyama, K., & Kato, S. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.05.156 · Cited by 61 · see citing works
Self-citationSplicing potentiation by growth factor signals via estrogen receptor phosphorylation
Masuhiro, Y., Mezaki, Y., Sakari, M., Takeyama, K., Yoshida, T., Inoue, K., Yanagisawa, J., Hanazawa, S., O’Malley, B. W., & Kato, S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503197102 · Cited by 61 · see citing works
Self-citationGriffin, M. D., Dong, X., & Kumar, R. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.01.034 · Cited by 61 · see citing works
Spermatogenesis‐specific association of SMCY and MSH5
Akimoto, C., Kitagawa, H., Μatsumoto, T., & Kato, S. (2008) · Genes to Cells · doi:10.1111/j.1365-2443.2008.01193.x · Cited by 60 · see citing works
Self-citationInvestigation and management of hypercalcaemia in children
Davies, J. H., & Shaw, N. J. (2012) · Archives of Disease in Childhood · doi:10.1136/archdischild-2011-301284 · Cited by 60 · see citing works
Kahata, K., Hayashi, M., Asaka, M., Hellman, U., Kitagawa, H., Yanagisawa, J., Kato, S., Imamura, T., & Miyazono, K. (2004) · Genes to Cells · doi:10.1111/j.1365-2443.2004.00706.x · Cited by 60 · see citing works
“Nuclear extract from MCF-7 cell was prepared as previously described (Kitagawa et al. 2003).”
Self-citationOma, Y., & Harata, M. (2011) · Nucleus · doi:10.4161/nucl.2.1.14510 · Cited by 58 · see citing works
Kitagawa, H., Ray, W. J., Glantschnig, H., Nantermet, P. V., Yu, Y., Leu, C., Harada, S.-I., Kato, S., & Freedman, L. P. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00409-07 · Cited by 57 · see citing works
“As a reference plasmid to normalize transfection efficiency, 2 ng pRL-CMV plasmid (Promega) was cotransfected in all experiments ( 28 , 58).”
MethodInfluentialSelf-citationRetractedYoshimura, K., Kitagawa, H., Fujiki, R., Tanabe, M., Takezawa, S., Takada, I., Yamaoka, I., Yonezawa, M., Kondo, T., Furutani, Y., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901184106 · Cited by 56 · see citing works
“Although WSTF was indispensable for proper in vitro function of transcriptional activators specific for cardiovascular development like other BAF components (12, 30), WSTF / embryos did not exhibit the same abnormalities seen in the embryos deficient in either BAF components (10, 21) or Fig.”
InfluentialSelf-citationRetractedChromatin remodelling and transcription: be-WICHed by nuclear myosin 1
Percipalle, P., & Farrants, A. Ö. (2006) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.03.001 · Cited by 56 · see citing works
Li, J., Ma, M., & Wang, Z. (2007) · Toxicology Letters · doi:10.1016/j.toxlet.2007.11.006 · Cited by 54 · see citing works
“This assay ased on the mechanism that most of the activities of hormones re mediated through their receptors, which reside in the cell and egulate the transcription of target genes in a ligand-dependent anner (Kitagawa et al., 2003).”
MethodYenamandra, S. P., Hellman, U., Kempkes, B., Darekar, S. D., Petermann, S., Sculley, T. B., Klein, G., & Kashuba, E. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0441-4 · Cited by 53 · see citing works
Inaba, Y., Yamamoto, K., Yoshimoto, N., Matsunawa, M., Uno, S., Yamada, S., & Makishima, M. (2007) · Molecular Pharmacology · doi:10.1124/mol.106.032318 · Cited by 52 · see citing works
Nuclear hormone receptor degradation and gene transcription: An update
Ismail, A., & Nawaz, Z. (2005) · IUBMB Life · doi:10.1080/15216540500147163 · Cited by 52 · see citing works
PPAR- γ Signaling Crosstalk in Mesenchymal Stem Cells
Takada, I., Kouzmenko, A., & Kato, S. (2010) · PPAR Research · doi:10.1155/2010/341671 · Cited by 51 · see citing works
Self-citationSugimoto, N., Yugawa, T., Iizuka, M., Kiyono, T., & Fujita, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.256123 · Cited by 50 · see citing works
Function of nuclear sex hormone receptors in gene regulation
Kato, S., Sato, T., Watanabe, T., Takemasa, S., Masuhiro, Y., Ohtake, F., & Μatsumoto, T. (2005) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-005-0102-8 · Cited by 50 · see citing works
“While histone modification due to HAT/HDAC activity in NR coregulator complexes in co-operation with chromatin remodeling complexes explains, at least in part, the mechanism of NR-mediated transcriptional control [10, 18], the molecular link between NR-mediated gene regulation and cell cycle control remains elusive.”
BackgroundSelf-citationDaigo, K., Kawamura, T., Ohta, Y., Ohashi, R., Katayose, S., Tanaka, T., Aburatani, H., Naito, M., Kodama, T., Ihara, S., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.154732 · Cited by 49 · see citing works
- Authors
- Kitagawa, H., Fujiki, R., Yoshimura, K., Mezaki, Y., Uematsu, Y., Matsui, D., Ogawa, S., Unno, K., Okubo, M., Tokita, A., Nakagawa, T., Ito, T., Ishimi, Y., Nagasawa, H., Matsumoto, T., Yanagisawa, J., & Kato, S.
- Affiliations
- Institute for Quantitative Biosciences, The University of Tokyo (JP)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2003-06
- Volume
- 113
- Issue
- 7
- Pages
- 905-917
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2150721910
- Cited by
- 268
- References
- 45
- Citations by year
- 2024: 3 · 2023: 3 · 2022: 2 · 2021: 3 · 2020: 2 · 2019: 2 · 2018: 6 · 2017: 2 · 2016: 5 · 2015: 5 · 2014: 7 · 2013: 13 · 2012: 12
- FWCI
- 9.01
- Type
- journal article
- Language
- en
- Status
- Retracted
- Update notices
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Life Sciences › Neuroscience › Developmental Neuroscience › Williams Syndrome Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- chromatin remodeling complexes, Williams syndrome, vitamin D receptor, SWI/SNF complex, promoter accessibility, coregulators, nucleosome organization, S phase progression
- MeSH terms
- Animals, Binding Sites, Cell Nucleus, Chromatin, DNA Replication, Eukaryotic Cells, Fetus, Gene Expression Regulation, Genes, Regulator, Humans, Nuclear Proteins, Nucleosomes, Promoter Regions, Genetic, Transcription Factors, Transcriptional Activation, S Phase, Protein Structure, Tertiary, Receptors, Calcitriol, Williams Syndrome, Active Transport, Cell Nucleus, Macromolecular Substances, Multiprotein Complexes, Mice
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