The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
Overcoming retinoic acid-resistance of mammary carcinomas by diverting retinoic acid from PPARβ/δ to RAR
Open accessAbstract
Retinoic acid (RA) displays potent anticarcinogenic activities that are mediated by the nuclear retinoic acid receptors (RARs). However, use of RA in oncology is limited by RA resistance acquired during carcinogenesis. Moreover, in some cancers, RA facilitates rather than inhibits growth. A clue to this paradoxical behavior was recently suggested by the findings that RA also activates PPARβ/δ, a receptor involved in mitogenic and anti-apoptotic activities. The observations that partitioning of RA between its two receptors is regulated by two intracellular lipid-binding proteins—CRABP-II, which targets RA to RAR, and FABP5, which delivers it to PPARβ/δ—further suggest that RA resistance may stem from the deregulation of the binding proteins, resulting in activation of PPARβ/δ rather than RAR. Here, we show that, in the RA-resistant mouse model of breast cancer MMTV-neu , RA indeed activates the nonclassical RA receptor PPARβ/δ. This behavior was traced to an aberrantly high intratumor FABP5/CRABP-II ratio. Decreasing this ratio in mammary tissue diverted RA from PPARβ/δ to RAR and suppressed tumor growth. The data demonstrate the existence of a mechanism that underlies RA resistance in tumors, indicate that CRABP-II functions as a tumor suppressor, and suggest that the inhibition of FABP5 may comprise a therapeutic strategy for overcoming RA resistance in some tumors.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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
“Most interestingly, RA binding activates the nuclear translocation of FABP5, which then delivers the ligand to the PPAR  / ␦ subtype (but not to the other PPARs) (21)(22)(23).”
From Vitamin A and retinoid signaling: genomic and nongenomic effects (2013) · cites this paper as [22]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Studies of the HER-2/ neu Proto-Oncogene in Human Breast and Ovarian Cancer
Slamon, D. J., Godolphin, W. J., Jones, L. A., Holt, J. A., Wong, S., Keith, D. E., Levin, W. J., Stuart, S. G., Udove, J. A., Ullrich, A., et al. (1989) · Science · doi:10.1126/science.2470152 · Cited by 6,817
Effects of a combination of beta carotene and vitamin A on lung cancer and cardiovascular disease
Omenn, G. S., Goodman, G. E., Thornquist, M. D., Balmes, J., Cullen, M. R., Glass, A., Keogh, J. P., Meyskens, F. L., Valanis, B., Williams, J. H., et al. (1996) · New England Journal of Medicine · doi:10.1056/nejm199605023341802 · Cited by 3,638
An inhibitor of Bcl-2 family proteins induces regression of solid tumours
Oltersdorf, T., Elmore, S. W., Shoemaker, A. R., Armstrong, R. C., Augeri, D. J., Belli, B., Bruncko, M., Deckwerth, T. L., Dinges, J., Hajduk, P. J., et al. (2005) · Nature · doi:10.1038/nature03579 · Cited by 3,407
Guy, C. T., Webster, M. A., Schaller, M. D., Parsons, T. J., Cardiff, R. D., & Muller, W. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.22.10578 · Cited by 1,193
Amplification of a Novel v- erb B-Related Gene in a Human Mammary Carcinoma
King, C. R., Kraus, M. H., & Aaronson, S. A. (1985) · Science · doi:10.1126/science.2992089 · Cited by 1,054
Treatment of diabetes and atherosclerosis by inhibiting fatty-acid-binding protein aP2
Furuhashi, M., Tuncman, G., Görgün, C. Z., Makowski, L., Atsumi, G., Vaillancourt, E., Kono, K., Babaev, V. R., Fazio, S., Linton, M. F., et al. (2007) · Nature · doi:10.1038/nature05844 · Cited by 730
Schug, T. T., Berry, D. C., Shaw, N. S., Travis, S. N., & Noy, N. (2007) · Cell · doi:10.1016/j.cell.2007.02.050 · Cited by 680
Self-citationTan, N.-S., Shaw, N. S., Vinckenbosch, N., Liu, P., Yasmin, R., Desvergne, B., Wahli, W., & Noy, N. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.14.5114-5127.2002 · Cited by 499
Self-citationCardiff, R. D., Anver, M. R., Gusterson, B. A., Hennighausen, L. G., Jensen, R. A., Merino, M. J., Rehm, S., Russo, J., Tavassoli, F. A., Wakefield, L. M., et al. (2000) · Oncogene · doi:10.1038/sj.onc.1203277 · Cited by 491
Kersten, S., Mandard, S., Tan, N. S., Escher, P., Metzger, D., Chambon, P., Gonzalez, F. J., Desvergne, B., & Wahli, W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004029200 · Cited by 489
Cited by
Sorted by citations
Field, C. S., Baixauli, F., Kyle, R. L., Puleston, D. J., Cameron, A. M., Sanin, D. E., Hippen, K. L., Loschi, M. L., Thangavelu, G., Corrado, M., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.11.021 · Cited by 443
Vitamin A and retinoid signaling: genomic and nongenomic effects
Al Tanoury, Z., Piskunov, A., & Rochette-Egly, C. (2013) · Journal of Lipid Research · doi:10.1194/jlr.r030833 · Cited by 408
Itoh, Y., Ishikawa, M., Naito, M., & Hashimoto, Y. (2010) · Journal of the American Chemical Society · doi:10.1021/ja100691p · Cited by 404
Tissue-specific Functions in the Fatty Acid-binding Protein Family
Storch, J., & THUMSER, A. E. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.135210 · Cited by 363
Berry, D. C., & Noy, N. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01742-08 · Cited by 345
Self-citationGenomic Antagonism between Retinoic Acid and Estrogen Signaling in Breast Cancer
Hua, S., Kittler, R., & White, K. P. (2009) · Cell · doi:10.1016/j.cell.2009.04.043 · Cited by 301
Aldehyde Dehydrogenases: Not Just Markers, but Functional Regulators of Stem Cells
Vassalli, G. (2019) · Stem Cells International · doi:10.1155/2019/3904645 · Cited by 296
Structural and functional analysis of fatty acid-binding proteins
Storch, J., & McDermott, L. (2008) · Journal of Lipid Research · doi:10.1194/jlr.r800084-jlr200 · Cited by 297
Retinoic acid signaling and neuronal differentiation
Janesick, A., Wu, S. C., & Blumberg, B. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1815-9 · Cited by 295
PROTACs: great opportunities for academia and industry (an update from 2020 to 2021)
He, M., Cao, C., Ni, Z., Liu, Y., Song, P., Hao, S., He, Y., Sun, X., & Rao, Y. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00999-9 · Cited by 283
Napoli, J. L. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.01.004 · Cited by 262
Dynamic and combinatorial control of gene expression by nuclear retinoic acid receptors (RARs)
Rochette‐Egly, C., & Germain, P. (2009) · Nuclear Receptor Signaling · doi:10.1621/nrs.07005 · Cited by 263
Bowen, N. J., Walker, L. D., Matyunina, L. V., Logani, S., Totten, K. A., Benigno, B. B., & McDonald, J. F. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-71 · Cited by 241
Aldehyde dehydrogenases and cancer stem cells
Xu, X., Chai, S., Wang, P., Zhang, C., Yang, Y., Yang, Y., & Wang, K. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.08.018 · Cited by 209
Between Death and Survival: Retinoic Acid in Regulation of Apoptosis
Noy, N. (2010) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155509 · Cited by 192
Self-citationWagner, K., & Wagner, N. (2009) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2009.12.001 · Cited by 198
Retinoic Acid Upregulates Preadipocyte Genes to Block Adipogenesis and Suppress Diet-Induced Obesity
Berry, D. C., DeSantis, D., Soltanian, H. T., Croniger, C. M., & Noy, N. (2012) · Diabetes · doi:10.2337/db11-1620 · Cited by 180
Self-citationAssociation of FABP5 Expression With Poor Survival in Triple-Negative Breast Cancer
Liu, R., Graham, K., Glubrecht, D. D., Germain, D. R., Mackey, J. R., & Godbout, R. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2010.11.075 · Cited by 163
Fatty Acid Signaling Mechanisms in Neural Cells: Fatty Acid Receptors
Falomir‐Lockhart, L. J., Cavazzutti, G. F., Giménez, E., & Toscani, A. M. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00162 · Cited by 164
Physiological functions of peroxisome proliferator-activated receptor β
Neels, J. G., & Grimaldi, P. A. (2014) · Physiological Reviews · doi:10.1152/physrev.00027.2013 · Cited by 161
Diverse roles of fatty acid binding proteins (FABPs) in development and pathogenesis of cancers
Amiri, M., Yousefnia, S., Forootan, F. S., Peymani, M., Ghaedi, K., & Nasr‐Esfahani, M. H. (2018) · Gene · doi:10.1016/j.gene.2018.07.035 · Cited by 150
Retinoids and breast cancer: From basic studies to the clinic and back again
Garattini, E., Bolis, M., Garattini, S. K., Fratelli, M., Centritto, F., Paroni, G., Gianni’, M., Zanetti, A., Pagani, A., Fisher, J. N., et al. (2014) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2014.01.001 · Cited by 135
Armstrong, E. H., Goswami, D., Griffin, P. R., Noy, N., & Ortlund, E. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.514646 · Cited by 135
Self-citationGuaita‐Esteruelas, S., Gumà, J., Masana, L., & Borràs, J. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.02.002 · Cited by 135
Marcato, P., Dean, C. A., Liu, R., Coyle, K. M., Bydoun, M., Wallace, M., Clements, D. R., Turner, C., Mathenge, E. G., Gujar, S. A., et al. (2014) · Molecular Oncology · doi:10.1016/j.molonc.2014.07.010 · Cited by 142
Role of fatty acid binding proteins (FABPs) in cancer development and progression
McKillop, I. H., Girardi, C. A., & Thompson, K. J. (2019) · Cellular Signalling · doi:10.1016/j.cellsig.2019.06.001 · Cited by 132
Yu, S., Levi, L., Siegel, R. E., & Noy, N. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.410381 · Cited by 116
Self-citationLevi, L., Wang, Z., Doud, M. K., Hazen, S. L., & Noy, N. (2015) · Nature Communications · doi:10.1038/ncomms9794 · Cited by 113
Self-citationLevi, L., Lobo, G. P., Doud, M. K., Lintig, J. V., Seachrist, D. D., Tochtrop, G. P., & Noy, N. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-0384 · Cited by 109
Self-citationKannan-Thulasiraman, P., Seachrist, D. D., Mahabeleshwar, G. H., Jain, M. K., & Noy, N. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.099770 · Cited by 100
Self-citationEpigenetic Silencing of CRABP2 and MX1 in Head and Neck Tumors
Calmon, M. F., Rodrigues, R. V., Kaneto, C. M., de Moura, R. P., da Silva, S. D., Mota, L. D. C., Pinheiro, D. G., Torres, C., de Carvalho, A. F., Cury, P. M., et al. (2009) · Neoplasia · doi:10.1593/neo.91110 · Cited by 99
Han, S. J., & O’Malley, B. W. (2014) · Human Reproduction Update · doi:10.1093/humupd/dmu002 · Cited by 98
Peters, J. M., & Gonzalez, F. J. (2009) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2009.06.002 · Cited by 99
Functions of Intracellular Retinoid Binding-Proteins
Napoli, J. L. (2016) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-024-0945-1_2 · Cited by 95
All-trans-Retinoic Acid Ameliorates Hepatic Steatosis in Mice by a Novel Transcriptional Cascade
Kim, S. C., Kim, C., Axe, D., Cook, A., Lee, M., Li, T., Smallwood, N. D., Chiang, J. Y. L., Hardwick, J. P., Moore, D. D., et al. (2013) · Hepatology · doi:10.1002/hep.26699 · Cited by 91
Targeting the retinoic acid signaling pathway as a modern precision therapy against cancers
Lavudi, K., Nuguri, S. M., Olverson, Z. A., Dhanabalan, A. K., Patnaik, S., & Kokkanti, R. R. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1254612 · Cited by 90
Development of target protein-selective degradation inducer for protein knockdown
Itoh, Y., Ishikawa, M., Kitaguchi, R., Sato, S., Naito, M., & Hashimoto, Y. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.03.057 · Cited by 87
Campos, B., Centner, F.-S., Bermejo, J. L., Ali, R., Dorsch, K., Wan, F., Felsberg, J., Ahmadi, R., Grabe, N., Reifenberger, G., et al. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.01.051 · Cited by 86
Involvement of Fatty Acid Binding Protein 5 and PPAR β / δ in Prostate Cancer Cell Growth
Morgan, E., Kannan-Thulasiraman, P., & Noy, N. (2010) · PPAR Research · doi:10.1155/2010/234629 · Cited by 85
Self-citationIntegrative and Systemic Approaches for Evaluating PPARβ/δ (PPARD) Function
Attianese, G. M. P. G., & Desvergne, B. (2015) · Nuclear Receptor Signaling · doi:10.1621/nrs.13001 · Cited by 88
A Comprehensive Nuclear Receptor Network for Breast Cancer Cells
Kittler, R., Zhou, J. H. S., Hua, S., Ma, L., Liu, Y., Pendleton, E., Cheng, C., Gerstein, M., & White, K. P. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.01.004 · Cited by 81
Establishing the Role of PPARβ/δ in Carcinogenesis
Peters, J. M., Gonzalez, F. J., & Müller, R. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.09.004 · Cited by 81
Ohata, T., Yokoo, H., Kamiyama, T., Fukai, M., Aiyama, T., Hatanaka, Y., Hatanaka, K. C., Wakayama, K., Orimo, T., Kakisaka, T., et al. (2017) · Cancer Medicine · doi:10.1002/cam4.1020 · Cited by 78
Xia, J. L., Li, S., Liu, S., & Zhang, L. (2023) · MedComm · doi:10.1002/mco2.195 · Cited by 80
Altered retinoid uptake and action contributes to cell survival in endometriosis
Pavone, M. E., Reierstad, S., Sun, H., Milad, M., Bulun, S. E., & Cheng, Y.-H. (2010) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2010-0459 · Cited by 74
Transcriptional control of physiological and pathological processes by the nuclear receptor PPARβ/δ
Tan, N. S., Vázquez‐Carrera, M., Montagner, A., Sng, M. K., Guillou, H., & Wahli, W. (2016) · Progress in Lipid Research · doi:10.1016/j.plipres.2016.09.001 · Cited by 75
Retinoic Acids in the Treatment of Most Lethal Solid Cancers
Costantini, L., Molinari, R., Farinon, B., & Merendino, N. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9020360 · Cited by 74
Liu, R., Garcia, E., Glubrecht, D. D., Poon, H. Y., Mackey, J. R., & Godbout, R. (2015) · Molecular Cancer · doi:10.1186/s12943-015-0380-7 · Cited by 72
Curcumin restores sensitivity to retinoic acid in triple negative breast cancer cells
Thulasiraman, P., McAndrews, D. J., & Mohiuddin, I. Q. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-724 · Cited by 69
Liu, R., Graham, K., Glubrecht, D. D., Lai, R. L., Mackey, J. R., & Godbout, R. (2012) · The Journal of Pathology · doi:10.1002/path.4001 · Cited by 69
Molecular Determinants of Retinoic Acid Sensitivity in Pancreatic Cancer
Gupta, S., Pramanik, D., Mukherjee, R., Campbell, N. R., Elumalai, S., de Wilde, R. F., Hong, S., Goggins, M., Jesus‐Acosta, A. D., Laheru, D. A., et al. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-2165 · Cited by 68
Molecular subtypes of urothelial carcinoma are defined by specific gene regulatory systems
Eriksson, P., Aine, M., Veerla, S., Liedberg, F., Sjödahl, G., & Höglund, M. (2015) · BMC Medical Genomics · doi:10.1186/s12920-015-0101-5 · Cited by 67
Dobrotkova, V., Chlapek, P., Mazánek, P., Štěrba, J., & Veselská, R. (2018) · BMC Cancer · doi:10.1186/s12885-018-4966-5 · Cited by 67
Peroxisome Proliferator-Activated Receptors and the Hallmarks of Cancer
Wagner, N., & Wagner, K. (2022) · Cells · doi:10.3390/cells11152432 · Cited by 69
Specific non-genetic IAP-based protein erasers (SNIPERs) as a potential therapeutic strategy
Ma, Z., Yu, J. H., Yu, Y., & Liang, D. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113247 · Cited by 63
Bhat‐Nakshatri, P., Goswami, C. P., Badve, S., Sledge, G. W., & Nakshatri, H. (2013) · Scientific Reports · doi:10.1038/srep02530 · Cited by 65
Yu, D. C. W., Liang, X., Lipsky, S., Karaaslan, Ç., Kozakewich, H. P., Hotamışlıgil, G. S., Bischoff, J. E., & Çataltepe, S. (2015) · Angiogenesis · doi:10.1007/s10456-015-9491-4 · Cited by 62
Enzymatic Metabolism of Vitamin A in Developing Vertebrate Embryos
Metzler, M. A., & Sandell, L. J. (2016) · Nutrients · doi:10.3390/nu8120812 · Cited by 65
Peters, J. M., Foreman, J. E., & Gonzalez, F. J. (2011) · Cancer and Metastasis Reviews · doi:10.1007/s10555-011-9320-1 · Cited by 64
Yao, P., Morales, J. L., Zhu, B., Kang, B.-H., Gonzalez, F. J., & Peters, J. M. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-13-0836 · Cited by 61
Lv, Q., Wang, G., Zhang, Y., Han, X., Li, H., Le, W., Zhang, M., Ma, C., Wang, P., & Ding, Q. (2019) · International Journal of Oncology · doi:10.3892/ijo.2019.4721 · Cited by 61
Majumdar, A., Petrescu, A. D., Xiong, Y., & Noy, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.293464 · Cited by 60
Self-citationTerao, M., Kurosaki, M., Barzago, M. M., Fratelli, M., Bagnati, R., Bastone, A., Giudice, C., Scanziani, E., Mancuso, A., Tiveron, C., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01385-08 · Cited by 60
Montagner, A., Delgado, M. B., Tallichet-Blanc, C., Chan, J. S. K., Sng, M. K., Mottaz, H., Degueurce, G., Lippi, Y., Moret, C., Baruchet, M., et al. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201302666 · Cited by 60
Apaya, M. K., Hsiao, P., Yang, Y., & Shyur, L. (2020) · Cancers · doi:10.3390/cancers12010199 · Cited by 60
Pavone, M. E., Dyson, M., Reirstad, S., Pearson, E., Ishikawa, H., Cheng, Y. H., & Bulun, S. E. (2011) · Human Reproduction · doi:10.1093/humrep/der172 · Cited by 56
Repression of Cellular Retinoic Acid-binding Protein II during Adipocyte Differentiation
Berry, D. C., Soltanian, H. T., & Noy, N. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.110635 · Cited by 55
Self-citationVreeland, A. C., Yu, S., Levi, L., Rossetto, D. D. B., & Noy, N. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00281-14 · Cited by 54
Self-citationLiu, R., Li, S., Garcia, E., Glubrecht, D. D., Poon, H. Y., Easaw, J. C., & Godbout, R. (2016) · Glia · doi:10.1002/glia.22976 · Cited by 55
The Role of PPARs in Breast Cancer
Zhao, B., Xin, Z., Ren, P., & Wu, H. (2022) · Cells · doi:10.3390/cells12010130 · Cited by 53
Cellular Retinoic Acid-binding Protein 2 Inhibits Tumor Growth by Two Distinct Mechanisms
Vreeland, A. C., Levi, L., Zhang, W., Berry, D. C., & Noy, N. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.604041 · Cited by 48
Self-citationNuclear and extranuclear effects of vitamin A
Iskakova, M., Karbyshev, M. S., Piskunov, A., & Rochette‐Egly, C. (2015) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-2014-0522 · Cited by 47
Physiological and pathological implications of retinoid action in the endometrium
Jiang, Y., Chen, L., Taylor, R. N., Li, C., & Zhou, X. (2018) · Journal of Endocrinology · doi:10.1530/joe-17-0544 · Cited by 52
Kruppel-like factor 2 suppresses mammary carcinoma growth by regulating retinoic acid signaling
Zhang, W., Levi, L., Banerjee, P., Jain, M. K., & Noy, N. (2015) · Oncotarget · doi:10.18632/oncotarget.5767 · Cited by 42
Self-citationCRABP‐II methylation: A critical determinant of retinoic acid resistance of medulloblastoma cells
Yuan-Shan, F., Wang, Q. Q., Ma, J., Yang, X., Wu, M., Zhang, K., Kong, Q., Chen, X.-Y., Sun, Y., Chen, N., et al. (2011) · Molecular Oncology · doi:10.1016/j.molonc.2011.11.004 · Cited by 41
Noy, N. (2013) · Adipocyte · doi:10.4161/adip.23489 · Cited by 40
Self-citationGuaita‐Esteruelas, S., Saavedra-García, P., Bosquet, A., Borràs, J., Girona, J., Amiliano, K., Rodríguez-Balada, M., Heras, M., Masana, L., & Gumà, J. (2017) · The Oncologist · doi:10.1634/theoncologist.2016-0483 · Cited by 41
Chemical Protein Degradation Approach and its Application to Epigenetic Targets
Itoh, Y. (2018) · The Chemical Record · doi:10.1002/tcr.201800032 · Cited by 41
Wu, G., Xu, Y., Wang, Q., Li, J., Li, L., Han, C., & Xia, Q. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.172637 · Cited by 39
Analysis of Common and Specific Mechanisms of Liver Function Affected by Nitrotoluene Compounds
Deng, Y., Meyer, S. A., Guan, X., Escalon, B. L., Ai, J., Wilbanks, M. S., Welti, R., García‐Reyero, N., & Perkins, E. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0014662 · Cited by 40
Coyle, K. M., Maxwell, S. P., Thomas, M. L., & Marcato, P. (2017) · Scientific Reports · doi:10.1038/s41598-017-16687-6 · Cited by 38
Disparate roles of retinoid acid signaling molecules in kidney disease
Chen, A., Liu, Y., Lu, Y., Lee, K., & He, C. (2021) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00045.2021 · Cited by 38
Alessandri, J., Extier, A., Al-Gubory, K. H., Goustard, B., Baudry, C., LePoupon, C., Lavialle, M., & Guesnet, P. (2010) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2010.07.005 · Cited by 40
Lipid-sensors, enigmatic-orphan and orphan nuclear receptors as therapeutic targets in breast-cancer
Garattini, E., Bolis, M., Gianni’, M., Paroni, G., Fratelli, M., & Terao, M. (2016) · Oncotarget · doi:10.18632/oncotarget.7410 · Cited by 36
Pavel, P., Leman, G., Hermann, M., Ploner, C., Eichmann, T. O., Minzaghi, D., Radner, F. P. W., Frari, B. D., Gruber, R. W., & Dubrac, S. (2021) · JID Innovations · doi:10.1016/j.xjidi.2021.100033 · Cited by 35
Nuclear and Extra-Nuclear Effects of Retinoid Acid Receptors: How They Are Interconnected
Piskunov, A., Tanoury, Z. A., & Rochette‐Egly, C. (2014) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-017-9050-5_6 · Cited by 38
Yang, Q., Wang, R., Xiao, W., Sun, F., Yuan, H., & Pan, Q. (2016) · PLoS ONE · doi:10.1371/journal.pone.0148381 · Cited by 34
CRABP1 in Non-Canonical Activities of Retinoic Acid in Health and Diseases
Nhieu, J., Lin, Y., & Wei, L. (2022) · Nutrients · doi:10.3390/nu14071528 · Cited by 34
Fernando, W., Cruickshank, B. M., Arun, R. P., MacLean, M. R., Cahill, H. F., Morales-Quintanilla, F., Dean, C. A., Wasson, M. D., Dahn, M. L., Coyle, K. M., et al. (2024) · Oncogene · doi:10.1038/s41388-024-03156-4 · Cited by 32
Conserva, M. R., Anelli, L., Zagaria, A., Specchia, G., & Albano, F. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20122921 · Cited by 31
17q12-21 – The pursuit of targeted therapy in breast cancer
Glynn, R. W., Miller, N., & Kerin, M. J. (2010) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2009.12.007 · Cited by 31
Montagner, A., Wahli, W., & Tan, N. S. (2015) · European Journal of Dermatology · doi:10.1684/ejd.2014.2505 · Cited by 30
Liu, R., & Godbout, R. (2020) · Cancers · doi:10.3390/cancers12123823 · Cited by 29
RNA-binding protein HuR regulates nuclear import of protein
Zhang, W., Vreeland, A. C., & Noy, N. (2016) · Journal of Cell Science · doi:10.1242/jcs.192096 · Cited by 28
Self-citationFischer-Huchzermeyer, S., Dombrowski, A., Wilke, G., Stahn, V., Streubel, A., Mautner, V. F., & Harder, A. (2017) · PLoS ONE · doi:10.1371/journal.pone.0187700 · Cited by 28
DNA Methylation Predicts the Response of Triple-Negative Breast Cancers to All-Trans Retinoic Acid
Coyle, K. M., Dean, C. A., Thomas, M. L., Vidovic, D., Giacomantonio, C. A., Helyer, L. K., & Marcato, P. (2018) · Cancers · doi:10.3390/cancers10110397 · Cited by 27
Redox regulation by carotenoids: Evidence and conflicts for their application in cancer
Russo, G. L., Moccia, S., Russo, M., & Spagnuolo, C. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114838 · Cited by 27
Chen, X., Peng, R., Peng, D., Liu, D., & Li, R. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05506-y · Cited by 26
Schultze, E., Buss, J. H., Coradini, K., Begnini, K. R., Guterres, S. S., Collares, T. V., Beck, R. C. R., Pohlmann, A. R., & Seixas, F. K. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.10.020 · Cited by 26
Chen, N., Li, Y., Wu, M., Liu, Z., Fu, Y., Kong, Q., Chen, X., Li, H., & Liu, J. (2011) · Experimental Dermatology · doi:10.1111/j.1600-0625.2011.01392.x · Cited by 25
Metadata
- Authors
- Schug, T. T., Berry, D. C., Toshkov, I. A., Cheng, L., Nikitin, A. Y., & Noy, N.
- Affiliations
- Cornell University (US)
- Case Western Reserve University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2008-05-27
- Volume
- 105
- Issue
- 21
- Pages
- 7546-7551
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2396692
- OpenAlex
- W2093995222
- Cited by
- 172
- References
- 45
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 9 · 2023: 5 · 2022: 7 · 2021: 10 · 2020: 8 · 2019: 9 · 2018: 10 · 2017: 12 · 2016: 12 · 2015: 15 · 2014: 15 · 2013: 10 · 2012: 7
- FWCI
- 5.35
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (CA107013)
- National Cancer Institute (R01CA096823, R01 CA 96823, R01CA107013, T32CA009682)
- National Center for Research Resources (CA96823, K26RR017595)
- Institute of Genetics
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Keywords
- retinoic acid resistance, PPARδ, retinoic acid receptor, breast cancer, FABP5, CRABP2, lipid-binding proteins, tumor suppressor, retinoic acid signaling, breast cancer treatment
- MeSH terms
- Animals, Antineoplastic Agents, Carcinoma, Disease Models, Animal, Mice, Transgenic, Neoplasm Proteins, Transcription, Genetic, Tretinoin, Mammary Neoplasms, Animal, Receptors, Retinoic Acid, Drug Resistance, Neoplasm, Cell Line, Tumor, PPAR delta, PPAR-beta, Fatty Acid-Binding Proteins, 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