The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
RETRACTED: The Chromatin-Remodeling Complex WINAC Targets a Nuclear Receptor to Promoters and Is Impaired in Williams Syndrome
Open accessAbstract
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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]
Citations
Cites
2 retracted
RETRACTED: Nuclear Receptor Function Requires a TFTC-Type Histone Acetyl Transferase Complex
Yanagisawa, J., Kitagawa, H., Yanagida, M., Wada, O., Ogawa, S., Nakagomi, M., Oishi, H., Yamamoto, Y., Nagasawa, H., McMahon, S. B., et al. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00478-1 · Cited by 157
Self-citationRetractedKitagawa, H., Yanagisawa, J., Fuse, H., Ogawa, S., Yogiashi, Y., Okuno, A., Nagasawa, H., Nakajima, T., Matsumoto, T., & Kato, S. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.11.3698-3706.2002 · Cited by 101
Self-citationRetractedDuplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
Elbashir, S. M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K., & Tuschl, T. (2001) · Nature · doi:10.1038/35078107 · Cited by 9,456
The nuclear receptor superfamily: the second decade
Mangelsdorf, D. J., Thummel, C., Beato, M., Herrlich, P., Schütz, G., Umesono, K., Blumberg, B., Kastner, P., Mark, M., Chambon, P., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90199-x · Cited by 6,964
Sequence and Characterization of a Coactivator for the Steroid Hormone Receptor Superfamily
Oñate, S. A., Tsai, S. Y., Tsai, M., & O’Malley, B. W. (1995) · Science · doi:10.1126/science.270.5240.1354 · Cited by 2,398
The coregulator exchange in transcriptional functions of nuclear receptors
Glass, C. K., & Rosenfeld, M. G. (2000) · Genes & Development · doi:10.1101/gad.14.2.121 · Cited by 2,233
Kamei, Y., Xu, L., Heinzel, T., Torchia, J., Kurokawa, R., Gloss, B., Lin, S.-C., Heyman, R. A., Rose, D. W., Glass, C. K., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81118-6 · Cited by 2,150
Cofactor Dynamics and Sufficiency in Estrogen Receptor–Regulated Transcription
Shang, Y., Hu, X., DiRenzo, J., Lazar, M. A., & Brown, M. A. (2000) · Cell · doi:10.1016/s0092-8674(00)00188-4 · Cited by 1,647
Cooperation between Complexes that Regulate Chromatin Structure and Transcription
Narlikar, G. J., Fan, H.-Y., & Kingston, R. E. (2002) · Cell · doi:10.1016/s0092-8674(02)00654-2 · Cited by 1,511
Schultz, D. C., Ayyanathan, K., Negorev, D., Maul, G. G., & Rauscher, F. J. (2002) · Genes & Development · doi:10.1101/gad.973302 · Cited by 1,313
Cited by
Sorted by citations
The biology of chromatin remodeling complexes.
Clapier, C. R., & Cairns, B. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.062706.153223 · Cited by 2,384
“Among the 28 genes lost by heterozygous deletion is the gene encoding WSTF, a transcription factor that recruits BRG1- and BRM-containing WINAC complexes to vitamin D-regulated promoters (121) and recruits hSNF2H in the WICH complex to heterochromatic replication foci (83).”
BackgroundVitamin D and Human Health: Lessons from Vitamin D Receptor Null Mice
Bouillon, R., Carmeliet, G., Verlinden, L., van Etten, E., Verstuyf, A., Luderer, H. F., Lieben, L., Mathieu, C., & Demay, M. (2008) · Endocrine Reviews · doi:10.1210/er.2008-0004 · Cited by 1,783
Nonclassic Actions of Vitamin D
Bikle, D. D. (2008) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2008-1454 · Cited by 995
“ement in its promoter to which VDR binds indirectly (12).”
Haussler, M. R., Jurutka, P. W., Mizwicki, M. T., & Norman, A. W. (2011) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2011.05.010 · Cited by 713
Dioxin receptor is a ligand-dependent E3 ubiquitin ligase
Ohtake, F., Baba, A., Takada, I., Okada, M., Iwasaki, K., Miki, H., Takahashi, S., Kouzmenko, A., Nohara, K., Chiba, T., et al. (2007) · Nature · doi:10.1038/nature05683 · Cited by 585
Self-citationThe SWI/SNF complex and cancer
Reisman, D., Glaros, S., & Thompson, E. A. (2009) · Oncogene · doi:10.1038/onc.2009.4 · Cited by 567
Fukuda, T., Yamagata, K., Fujiyama, S., Μatsumoto, T., Koshida, I., Yoshimura, K., Mihara, M., Naitou, M., Endoh, H., Nakamura, T., et al. (2007) · Nature Cell Biology · doi:10.1038/ncb1577 · Cited by 452
Self-citationRetractedTakada, I., Mihara, M., Suzawa, M., Ohtake, F., Kobayashi, S., Igarashi, M., Youn, M., Takeyama, K.-I., Nakamura, T., Mezaki, Y., et al. (2007) · Nature Cell Biology · doi:10.1038/ncb1647 · Cited by 424
“We therefore biochemically purified NLK-containing complexes from nuclear extracts of KCl-treated HeLa cells expressing Flag-tagged NLK by two-step purificatio”
Self-citationRetractedThe PHD finger, a nuclear protein-interaction domain
Bienz, M. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.11.001 · Cited by 420
Epigenetics and cardiovascular disease
Ordovás, J. M., & Smith, C. E. (2010) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2010.104 · Cited by 413
Premature ovarian failure in androgen receptor-deficient mice
Shiina, H., Μatsumoto, T., Sato, T., Igarashi, K., Miyamoto, J., Takemasa, S., Sakari, M., Takada, I., Nakamura, T., METZGER, D., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506736102 · Cited by 332
Self-citationGlcNAcylation of histone H2B facilitates its monoubiquitination
Fujiki, R., Hashiba, W., Sekine, H., Yokoyama, A., Chikanishi, T., Ito, S., Imai, Y., Kim, J., He, H. H., Igarashi, K., et al. (2011) · Nature · doi:10.1038/nature10656 · Cited by 340
Self-citationInteraction of the Glucocorticoid Receptor with the Chromatin Landscape
John, S., Sabo, P. J., Johnson, T. A., Sung, M., Biddie, S. C., Lightman, S. L., Voss, T. C., Davis, S. R., Meltzer, P. S., Stamatoyannopoulos, J. A., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.02.010 · Cited by 319
“The peroxisomal proliferator activated receptor has been shown to interact with a member of the CHD remodeling family (Surapureddi et al., 2006), and the vitamin D receptor utilizes the WINAC complex (Kitagawa et al., 2003).”
BackgroundNuclear Receptor Coregulators and Human Disease
Lonard, D. M., Lanz, R. B., & O’Malley, B. W. (2007) · Endocrine Reviews · doi:10.1210/er.2007-0012 · Cited by 318
Hormones and Disorders of Mineral Metabolism
Bringhurst, F. R., Demay, M. B., & Kronenberg, H. M. (2011) · Elsevier eBooks · doi:10.1016/b978-1-4377-0324-5.00028-6 · Cited by 297
Khundmiri, S. J., Murray, R. D., & Lederer, E. D. (2016) · Comprehensive physiology · doi:10.1002/cphy.c140071 · Cited by 376
The BRG1 transcriptional coregulator
Trotter, K. W., & Archer, T. (2008) · Nuclear Receptor Signaling · doi:10.1621/nrs.06004 · Cited by 287
Complex Role of the Vitamin D Receptor and Its Ligand in Adipogenesis in 3T3-L1 Cells
Blumberg, J. M., Tzameli, I., Astapova, I. I., Lam, F. S., Flier, J. S., & Hollenberg, A. N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510343200 · Cited by 250
Wnt/β-Catenin and Estrogen Signaling Converge in Vivo
Kouzmenko, A., Takeyama, K., Ito, S., Furutani, T., Sawatsubashi, S., Maki, A., Suzuki, E., Kawasaki, Y., Akiyama, T., Tabata, T., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400331200 · Cited by 214
Self-citationPoot, R. A., Bozhenok, L., van den Berg, D. L. C., Steffensen, S., Ferreira, F., Grimaldi, M., Gilbert, N., Ferreira, J. A., & Varga‐Weisz, P. (2004) · Nature Cell Biology · doi:10.1038/ncb1196 · Cited by 203
“Depletion of the WSTF protein has been implicated as the cause for the hypocalcaemia observed in individuals with Williams-Beuren syndrome through its role in Vitamin D receptor-mediated gene regulatio”
RETRACTED: 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. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.08.017 · Cited by 197
“Additional cell lines included mouse kidney proximal tubule-derived MCT cell lines and the human breast cancer-derived MCF-7 cell line (Kitagawa et al., 2003; Ohtake et al., 2007).”
Self-citationRetractedWilliams-Beuren syndrome: a challenge for genotype-phenotype correlations
Tassabehji, M. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg299 · Cited by 192
“May be involved in chromatin-dependent regulation of transcription (41)”
Percipalle, P., Fomproix, N., Cavellán, E., Voit, R., Reimer, G., Krüger, T., Thyberg, J., Scheer, U., Grummt, I., & Östlund Farrants, A. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400657 · Cited by 171
Of mice and men: molecular genetics of congenital heart disease
Andersen, T. A., Troelsen, K. D. L. L., & Larsen, L. A. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1430-1 · Cited by 173
GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis
Fujiki, R., Chikanishi, T., Hashiba, W., Ito, H., Takada, I., Roeder, R. G., Kitagawa, H., & Kato, S. (2009) · Nature · doi:10.1038/nature07954 · Cited by 171
Self-citationRetractedSox9 and p300 Cooperatively Regulate Chromatin-mediated Transcription
Furumatsu, T., Tsuda, M., Yoshida, K., Taniguchi, N., Ito, T., Hashimoto, M., Ito, T., & Asahara, H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502409200 · Cited by 168
Self-citationChromatin Remodeling in Cardiovascular Development and Physiology
Han, P., Hang, C. T., Yang, J., & Chang, C. (2011) · Circulation Research · doi:10.1161/circresaha.110.224287 · Cited by 168
A histone chaperone, DEK, transcriptionally coactivates a nuclear receptorPreprint
Sawatsubashi, S., Murata, T., Lim, J., Fujiki, R., Ito, S., Suzuki, E., Tanabe, M., Zhao, Y., Kimura, S., Fujiyama, S., et al. (2009) · Genes & Development · doi:10.1101/gad.1857410 · Cited by 157
Self-citationATP-dependent nucleosome remodelling: factors and functions
Eberharter, A., & Becker, P. B. (2004) · Journal of Cell Science · doi:10.1242/jcs.01175 · Cited by 163
“Depending on the isolation procedure, variants of a basic BAF (Brg1-associated factors) complex with additional subunits are observed (Kitagawa et al., 2003; Sif et al., 2001; Underhill et al., 2000; Xu et al., 2004).”
The WSTF-SNF2h Chromatin Remodeling Complex Interacts with Several Nuclear Proteins in Transcription
Cavellán, E., Asp, P., Percipalle, P., & Farrants, A. Ö. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600233200 · Cited by 156
Murayama, A., Kim, M. S., Yanagisawa, J., Takeyama, K.-I., & Kato, S. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600157 · Cited by 153
“ChIP analyses were performed using the ChIP assay kit (Upstate Biotechnology), as described previously (Kitagawa et al, 2003).”
InfluentialSelf-citationRetractedCopy number variants at Williams–Beuren syndrome 7q11.23 region
Merla, G., Brunetti‐Pierri, N., Micale, L., & Fusco, C. (2010) · Human Genetics · doi:10.1007/s00439-010-0827-2 · Cited by 159
“Experimental data suggest that BAZ1B regulates the expression of enzymes involved in both synthesis and catabolism of vitamin D (Kitagawa et al. 2003).”
BackgroundInfluentialMechanisms for ATP-dependent chromatin remodelling: farewell to the tuna-can octamer?
Flaus, A., & Owen‐Hughes, T. (2004) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2004.01.007 · Cited by 152
Jurutka, P. W., Bartik, L., Whitfield, G. K., Mathern, D. R., Barthel, T. K., Gurevich, M., Hsieh, J., Kaczmarska, M. J., Haussler, C. A., & Haussler, M. R. (2007) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.07s216 · Cited by 148
“2A and 2C): step 3, factors capable of histone acetylation (HATs), such as SRC-1,(37) CBP/p300, or pCAF, or of ATP-dependent chromatin remodeling, such as the mammalian homologs of SWI/SNF(38); step 4, TATA binding protein associated factors (TAFs, especially TAFs 28, 55, and 135(39,40)); step 5, basal transcription f…”
BackgroundMolecular switching of osteoblastogenesis versus adipogenesis: implications for targeted therapies
Takada, I., Kouzmenko, A., & Kato, S. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728220902915310 · Cited by 147
“NLK-containing protein complexes were biochemically purified from nuclear extracts of KCl-treated HeLa cells expressing FLAG-tagged NLK [73,74] and a distinct NLK-nuclear protein complex with a molecular weight of 400-500 kDa was isolated and analyzed [75].”
Self-citationTakada, I., Suzawa, M., Matsumoto, K., & Kato, S. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1402.034 · Cited by 144
Self-citationStructural insights into human KAP1 PHD finger–bromodomain and its role in gene silencing
Zeng, L., Yap, K. L., Ivanov, A. V., Wang, X., Mujtaba, S., Plotnikova, O. V., Rauscher, F. J., & Zhou, M. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1416 · Cited by 136
“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
“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
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
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 139
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 130
“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
“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
“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
“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
“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
“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 109
“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 111
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
“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
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 109
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 102
“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 100
“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 95
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
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
“…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
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 91
“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
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
“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 90
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
Self-citationRetractedCuesta, I., Zaret, K. S., & Santisteban, P. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00758-07 · Cited by 80
“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 82
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
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 79
Chen, J., Kinyamu, H. K., & Archer, T. (2005) · Molecular Endocrinology · doi:10.1210/me.2005-0192 · Cited by 76
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
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 74
“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
“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].”
BackgroundMaturation 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
Self-citationRetractedTerhune, 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
Kimura, 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
Self-citationHonjo, Y., Sasaki, S., Kobayashi, Y., Misawa, H., & Nakamura, H. (2006) · Journal of Endocrinology · doi:10.1677/joe.1.06105 · Cited by 69
“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 70
“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
“…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 70
Khundmiri, S. J., Murray, R. D., & Lederer, E. D. (2016) · Comprehensive physiology · doi:10.1002/j.2040-4603.2016.tb00690.x · Cited by 66
“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
“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
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 64
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
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
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
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 62
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
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
“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
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
“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
“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
Li, J., Ma, M., & Wang, Z. (2007) · Toxicology Letters · doi:10.1016/j.toxlet.2007.11.006 · Cited by 54
“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
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
Nuclear hormone receptor degradation and gene transcription: An update
Ismail, A., & Nawaz, Z. (2005) · IUBMB Life · doi:10.1080/15216540500147163 · Cited by 58
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
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
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
“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
Metadata
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
