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The histone deacetylase inhibitor valproic acid selectively induces proteasomal degradation of HDAC2
Open accessAbstract
Histone-modifying enzymes play essential roles in physiological and aberrant gene regulation. Since histone deacetylases (HDACs) are promising targets of cancer therapy, it is important to understand the mechanisms of HDAC regulation. Selective modulators of HDAC isoenzymes could serve as efficient and well-tolerated drugs. We show that HDAC2 undergoes basal turnover by the ubiquitin-proteasome pathway. Valproic acid (VPA), in addition to selectively inhibiting the catalytic activity of class I HDACs, induces proteasomal degradation of HDAC2, in contrast to other inhibitors such as trichostatin A (TSA). Basal and VPA-induced HDAC2 turnover critically depend on the E2 ubiquitin conjugase Ubc8 and the E3 ubiquitin ligase RLIM. Ubc8 gene expression is induced by both VPA and TSA, whereas only TSA simultaneously reduces RLIM protein levels and therefore fails to induce HDAC2 degradation. Thus, poly-ubiquitination and proteasomal degradation provide an isoenzyme-selective mechanism for downregulation of HDAC2.
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“Inhibition of histone deacetylase (HDAC) increases acetylation of H4 and disrupts the interaction between the locus and RNA polymerase II, leading to the suppression of PU.1 transcription in murine microglia [35, 36].”
From Transcriptional and Epigenetic Regulation of Microglia in Health and Disease (2019) · cites this paper as [36]
In the citing paper
“Valproic acid treatment, which selectively inhibits the catalytic activity of class I HDACs and induces proteasomal degradation of HDAC2, of primary adult human microglia reduces phagocytic capacity and expression of PU.1 and CD45, suggesting the its regulation of microglial phagocytosis via epigenetic mechanism [36-38].”
From Transcriptional and Epigenetic Regulation of Microglia in Health and Disease (2019) · cites this paper as [36]
In the citing paper
“Acetylation of histone H4 on the promoter and intron-1 region of the PU.1 locus are tightly regulated for allowing the interaction between the locus and RNA polymerase II.”
From Transcriptional and Epigenetic Regulation of Microglia in Health and Disease (2019) · cites this paper as [36]
In the citing paper
“suggesting the its regulation of microglial phagocytosis via epigenetic mechanism [36-38].”
From Transcriptional and Epigenetic Regulation of Microglia in Health and Disease (2019) · cites this paper as [36]
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Cites
The language of covalent histone modifications
Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679
The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction
Glickman, M. H., & Ciechanover, A. J. (2002) · Physiological Reviews · doi:10.1152/physrev.00027.2001 · Cited by 4,296
The polycomb group protein EZH2 is involved in progression of prostate cancer
Varambally, S., Dhanasekaran, S. M., Zhou, M., Barrette, T. R., Kumar-Sinha, C., Sanda, M. G., Ghosh, D., Pienta, K. J., Sewalt, R. G. A. B., Otte, A. P., et al. (2002) · Nature · doi:10.1038/nature01075 · Cited by 2,717
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
Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells
Göttlicher, M., Minucci, S., Zhu, P., Krämer, O. H., Schimpf, A., Giavara, S., Sleeman, J. P., Coco, F. L., Nervi, C., Pelicci, P. G., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.24.6969 · Cited by 1,930
Phiel, C. J., Zhang, F., Huang, E. Y., Guenther, M. G., Lazar, M. A., & Klein, P. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101287200 · Cited by 1,758
SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
Carrano, A. C., Eytan, E., Hershko, A., & Pagano, M. (1999) · Nature Cell Biology · doi:10.1038/12013 · Cited by 1,544
Nuclear Receptor Repression Mediated by a Complex Containing SMRT, mSin3A, and Histone Deacetylase
Nagy, L., Kao, H.-Y., Chakravarti, D., Lin, R. J., Hassig, C. A., Ayer, D. E., Schreiber, S. L., & Evans, R. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80218-4 · Cited by 1,230
Protein regulation by monoubiquitin
Hicke, L. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056583 · Cited by 1,227
A complex containing N-CoR, mSln3 and histone deacetylase mediates transcriptional repression
Heinzel, T., Lavinsky, R. M., Mullen, T.-M., Söderström, M., Laherty, C. D., Torchia, J., Yang, W., Brard, G., Ngo, S. D., Davie, J., et al. (1997) · Nature · doi:10.1038/387043a0 · Cited by 1,210
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Wolters, J. E. J., Breda, S. G. J. V., Grossmann, J., Fortes, C., Caiment, F., & Kleinjans, J. C. S. (2018) · Toxicology Letters · doi:10.1016/j.toxlet.2018.02.026 · Cited by 25
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Lu, Y. C., & Yang, S. (2009) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.219.17 · Cited by 25
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Madugula, K., Mulherkar, R., Khan, Z. K., Chigbu, D. I., Patel, D., Harhaj, E. W., & Jain, P. (2019) · Oncotarget · doi:10.18632/oncotarget.26763 · Cited by 26
George, S., Kadam, S. D., Irving, N. D., Markowitz, G. J., Raja, S., Kwan, A., Tu, Y., Chen, H., Rohde, C. A., Smith, D. R., et al. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00123 · Cited by 25
Phase I trial of ATRA-IV and depakote in patients with advanced solid tumor malignancies
David, K. A., Mongan, N. P., Smith, C. P., Gudas, L. J., & Nanus, D. M. (2010) · Cancer Biology & Therapy · doi:10.4161/cbt.9.9.11436 · Cited by 24
Histone Deacetylase Inhibitor: Antineoplastic Agent and Radiation Modulator
Konsoula, Z., Velena, A., Lee, R., Dritschilo, A., & Jung, M. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-0254-1_14 · Cited by 24
Brody, L., Sahuri-Arisoylu, M., Parkinson, J. R. C., Parkes, H. G., So, P., Hajji, N., Thomas, E. L., Frost, G. S., Miller, A. D., & Bell, J. D. (2017) · International Journal of Nanomedicine · doi:10.2147/ijn.s135968 · Cited by 24
Escelsior, A., Sterlini, B., Murri, M. B., Valente, P., Amerio, A., di Brozolo, M. R., da Silva, B. P., & Amore, M. (2020) · Psychiatric Genetics · doi:10.1097/ypg.0000000000000249 · Cited by 25
Kim (2009) · International Journal of Oncology · doi:10.3892/ijo_00000262 · Cited by 23
Histone deacetylase‑2: A potential regulator and therapeutic target in liver disease (Review)
Liu, Y.-R., Wang, J., Huang, Z., Chen, R.-N., Cao, X., Zhu, D., Yu, H., Wang, X., Zhou, H.-Y., Xia, Q., et al. (2021) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2021.4964 · Cited by 23
Jeon, S. J., Kim, J., Kim, K. C., Han, S. M., Go, H. S., Seo, J. E., Choi, C. S., Ryu, J. H., Shin, C. Y., & Song, M. (2013) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-013-0014-9 · Cited by 23
HDAC inhibitor valproic acid upregulates CAR in vitro and in vivo
Segura-Pacheco, B. A., Avalos, B., Rangel‐López, E., Velázquez, D. M., & Cabrera, G. (2007) · Genetic Vaccines and Therapy · doi:10.1186/1479-0556-5-10 · Cited by 23
Fractal Characterization of Chromatin Decompaction in Live Cells
Yi, J., Stypula‐Cyrus, Y., Blaha, C. S., Roy, H. K., & Backman, V. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.10.014 · Cited by 23
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Navarrete-Modesto, V., Orozco-Suárez, S. A., Feria-Romero, I. A., & Rocha, L. (2018) · Epilepsy Research · doi:10.1016/j.eplepsyres.2018.11.006 · Cited by 23
Shirsath, N., Rathos, M. J., Chaudhari, U., Sivaramakrishnan, H., & Joshi, K. S. (2013) · Lung Cancer · doi:10.1016/j.lungcan.2013.08.010 · Cited by 23
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Elizalde, C., Fernández‐Rueda, J., Salcedo, J. M., Dorronsoro, A., Ferrin, I., Jakobsson, E., & Trigueros, C. (2012) · Stem Cells and Development · doi:10.1089/scd.2011.0698 · Cited by 23
Wang, Y., Zhang, J., Wu, L., Liu, W., Wei, G., Gong, X., Liu, Y., Ma, Z., Ma, F., Thiery, J. P., et al. (2018) · Breast Cancer Research · doi:10.1186/s13058-018-1018-7 · Cited by 22
A combined approach for the study of histone deacetylase inhibitors
Činčárová, L., Lochmanová, G., Nováková, K., Šultesová, P., Konečná, H., Fajkusová, L., Fajkus, J., & Zdráhal, Z. (2012) · Molecular BioSystems · doi:10.1039/c2mb25136a · Cited by 22
Takizawa, D., Kakizaki, S., Horiguchi, N., Tojima, H., Yamazaki, Y., Ichikawa, T., Sato, K., & Mori, M. (2010) · Drug Metabolism and Disposition · doi:10.1124/dmd.110.032854 · Cited by 22
Bator, E., Latusz, J., Radaszkiewicz, A., Wędzony, K., & Maćkowiak, M. (2015) · Pharmacological Reports · doi:10.1016/j.pharep.2015.04.004 · Cited by 22
Gao, D., Xia, Q., Lv, J., & Zhang, H. (2007) · International Journal of Urology · doi:10.1111/j.1442-2042.2007.01823.x · Cited by 22
Song, H., Tao, L., Chen, C., Pan, L., Hao, J., Ni, Y., Li, D., Li, B., & Shi, G. (2015) · PubMed Central · Cited by 22
Lerche, C. M., Philipsen, P. A., Sehested, M., & Wulf, H. C. (2008) · Experimental Dermatology · doi:10.1111/j.1600-0625.2008.00733.x · Cited by 22
Ouyang, D., Ji, Y., Saltis, M., Xu, L., Zhang, Y.-T., Zha, Q., Cai, J., & He, X. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.06.016 · Cited by 21
Molecular regulation of brain metabolism underlying circadian epilepsy
Chan, F., & Liu, J. S.-H. (2021) · Epilepsia · doi:10.1111/epi.16796 · Cited by 21
Dodurga, Y., Gündoğdu, G., Tekin, V., Koc, T., Şatıroğlu-Tufan, N. L., Bağcı, G., & Küçükatay, V. (2014) · Molecular Biology Reports · doi:10.1007/s11033-014-3330-3 · Cited by 21
Epigenetic modulation by inorganic metal complexes
Leung, C., Liu, L., Leung, K., & Ma, D. (2016) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2016.03.014 · Cited by 21
Jamal, I., Kumar, V., Vatsa, N., Shekhar, S., Singh, B. K., Sharma, A., & Jana, N. R. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.05.010 · Cited by 22
Chowdhury, S. K., Liu, W., Zi, M., Li, Y., Wang, S., Tsui, H., Prehar, S., Castro, S. J., Zhang, H., Ji, Y. I., et al. (2016) · Circulation · doi:10.1161/circulationaha.116.022941 · Cited by 21
Rlim-Dependent and -Independent Pathways for X Chromosome Inactivation in Female ESCs
Wang, F., McCannell, K. N., Bošković, A., Zhu, X., Shin, J., Yu, J., Gallant, J., Byron, M., Lawrence, J. B., Zhu, L. J., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.12.004 · Cited by 21
Zhou, J. J., Cho, J. S., Han, H., Blitz, I. L., Wang, W., & Cho, K. W. Y. (2023) · eLife · doi:10.7554/elife.79380 · Cited by 20
Hui, H., Zhang, X., Li, H., Liu, X., Shen, L., Zhu, Y., Xu, J., Guo, Q., & Lu, N. (2016) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-016-2160-1 · Cited by 20
Arnason, T., Pisclevich, M. G., Dash, M. D., Davies, G. F., & Harkness, T. A. A. (2005) · Eukaryotic Cell · doi:10.1128/ec.4.1.134-146.2005 · Cited by 20
Zhang, S., Tang, Z., Qing, B., Tang, R., Duan, Q., Ding, S., & Deng, D. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.172745 · Cited by 19
Chromatin Acetylation Status in the Manifestation of Neurodegenerative Diseases
Boutillier, A., Rouaux, C., Panteleeva, I., & Loeffler, J. (2007) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/1-4020-5466-1_12 · Cited by 19
Genome-Wide Screening for Genes Associated with Valproic Acid Sensitivity in Fission Yeast
Zhang, L., Ma, N., Liu, Q., & Ma, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068738 · Cited by 20
Drugs and Epigenetic Molecular Functions. A Pharmacological Data Scientometric Analysis
Kringel, D., Malkusch, S., & Lötsch, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147250 · Cited by 19
Chromatin Structure and Drug Resistance in Candida spp.
O’Kane, C. J., Weild, R., & Hyland, E. M. (2020) · Journal of Fungi · doi:10.3390/jof6030121 · Cited by 19
Aminpour, M., Miranda, W. E., Wacker, S., Noskov, S., Houghton, M., Tyrrell, D. L., & Tuszyński, J. A. (2021) · BMC Pharmacology and Toxicology · doi:10.1186/s40360-021-00519-5 · Cited by 17
Blaauboer, A., van Koetsveld, P. M., Mustafa, D. A. M., Dumas, J., Dogan, F., van Zwienen, S., van Eijck, C. H. J., & Hofland, L. J. (2022) · Biomedicines · doi:10.3390/biomedicines10030517 · Cited by 17
Fatty acids and epigenetics in health and diseases
Chung, M.-Y., & Kim, B. H. (2024) · Food Science and Biotechnology · doi:10.1007/s10068-024-01664-3 · Cited by 21
Role of Histone Deacetylase Inhibitors in the Treatment of Lymphomas and Multiple Myeloma
Zain, J. M. (2012) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2012.01.006 · Cited by 17
Walters, B. J., & Zovkic, I. B. (2015) · Neuroscience · doi:10.1016/j.neuroscience.2015.05.005 · Cited by 19
Deficient spermiogenesis in mice lacking Rlim
Wang, F., Gervasi, M. G., Bošković, A., Sun, F., Rinaldi, V. D., Yu, J., Wallingford, M. C., Tourzani, D. A., Mager, J., Zhu, L. J., et al. (2021) · eLife · doi:10.7554/elife.63556 · Cited by 18
Toronjo‐Urquiza, L., Acosta‐Martin, A. E., James, D. C., Nagy, T., & Falconer, R. J. (2020) · Biotechnology Progress · doi:10.1002/btpr.2980 · Cited by 18
Effects of histone deacetylase inhibitor valproic acid on skeletal myocyte development
Li, Q., Foote, M., & Chen, J. (2014) · Scientific Reports · doi:10.1038/srep07207 · Cited by 17
Pekary, A. E., Stevens, S. A., & Sattin, A. (2006) · Peptides · doi:10.1016/j.peptides.2006.07.014 · Cited by 17
Kiweler, N., Schwarz, H., Nguyen, A., Matschos, S., Mullins, C. S., Piée‐Staffa, A., Brachetti, C., Roos, W. P., Schneider, G., Linnebacher, M., et al. (2022) · Cell Biology and Toxicology · doi:10.1007/s10565-022-09731-3 · Cited by 16
Combined therapy of colon carcinomas with an oncolytic adenovirus and valproic acid
Bressy, C., Majhen, D., Raddi, N., Jdey, W., Cornilleau, G., Zig, L., Guirouilh‐Barbat, J., López, B. S., Bawa, O., Opolon, P., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.22107 · Cited by 16
Duan, H., Wang, C., Zhou, K., Wang, T., Li, Y., Qiu, D., Li, Q., Zhang, Y., & Hua, Y. (2016) · Placenta · doi:10.1016/j.placenta.2016.11.011 · Cited by 16
Histone deacetylase inhibitors differentially regulate c‑Myc expression in retinoblastoma cells
Yu, N. H., Chen, P., Wang, Q., Liang, M., Qiu, J., Zhou, P., Yang, M., Yang, P., Wu, Y., Han, X., et al. (2019) · Oncology Letters · doi:10.3892/ol.2019.11111 · Cited by 16
Moreno‐Torres, M., Guzmán, C., Petrov, P., & Jover, R. (2022) · Nutrients · doi:10.3390/nu14132673 · Cited by 15
The epigenetic regulation of Dicer and microRNA biogenesis by Panobinostat
Hoffend, N. C., Magner, W. J., & Tomasi, T. B. (2016) · Epigenetics · doi:10.1080/15592294.2016.1267886 · Cited by 15
Vega‐García, N., Malatesta, R., Estella, C., Pérez‐Jaume, S., Esperanza‐Cebollada, E., Torrebadell, M., Català, A., Gassiot, S., Berrueco, R., Ruiz‐Llobet, A., et al. (2018) · British Journal of Haematology · doi:10.1111/bjh.15436 · Cited by 15
Trichostatin A promotes GLI1 degradation and P21 expression in multiple myeloma cells
Geng, Y., Liu, J., Xie, Y., Jiang, H., Zuo, K., Li, T., & Liu, Z. (2018) · Cancer Management and Research · doi:10.2147/cmar.s167330 · Cited by 15
Rlim/Rnf12, Rex1, and X Chromosome Inactivation
Wang, F., & Bach, I. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00258 · Cited by 15
Leung, C. S., Rosenzweig, S. J., Yoon, B., Marinelli, N. A., Hollingsworth, E. W., Maguire, A. M., Cowen, M. H., Schmidt, M., Imitola, J., Uzun, E. D. G., et al. (2023) · Human Molecular Genetics · doi:10.1093/hmg/ddad002 · Cited by 16
Caspase-3 and Caspase-6 cleave STAT1 in leukemic cells
Licht, V., Noack, K., Schlott, B., Förster, M., Schlenker, Y., Licht, A., Krämer, O. H., & Heinzel, T. (2014) · Oncotarget · doi:10.18632/oncotarget.1911 · Cited by 15
Bhattacharya, S., Reddy, D., Ingle, A., Khade, B., & Gupta, S. (2016) · Experimental Biology and Medicine · doi:10.1177/1535370216649262 · Cited by 15
HDAC inhibition is associated to valproic acid induction of early megakaryocytic markers
Vulcano, F., Ciccarelli, C., Mattia, G., Marampon, F., Macioce, G., Milazzo, L., Pascuccio, M., ZANI, B. M., Giampaolo, A., & Hassan, H. J. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.01.017 · Cited by 15
Ravillah, D., Mohammed, A., Li, Q., Brewer, M. F., Zhang, Y., Biddick, L., Steele, V. E., & Rao, C. V. (2013) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.113.208645 · Cited by 14
Al-Griw, M. A., Alshibani, Z. O., Alghazeer, R. O., Elhensheri, M., Tabagh, R. M., Eskandrani, A. A., Alansari, W. S., Habibulla, M. M., & Shamlan, G. H. (2022) · Scientific Reports · doi:10.1038/s41598-022-12937-4 · Cited by 14
Histone deacetylase inhibitor trichostatin A affects porcine oocyte maturation in vitro
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Correa-Basurto, A. M., Romero‐Castro, A., Correa‐Basurto, J., Rodríguez, M. H., Soriano-Ursua, M. A., García‐Machorro, J., Tolentino-López, L. E., Rosales‐Hernández, M. C., & Mendieta‐Wejebe, J. E. (2018) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2018.09.010 · Cited by 14
E3 ligase RCHY1 negatively regulates HDAC2
Choi, M., Choi, Y. M., An, I., Bae, S., Jung, J. H., & An, S. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.10.049 · Cited by 14
Ren, W.-B., Xia, X., Huang, J., Guo, W., Che, Y., Huang, T.-H., & Lei, L. (2019) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b1800211 · Cited by 13
Nguyen, A., Dzulko, M., Murr, J., Yun, Y., Schneider, G., & Krämer, O. (2021) · Cells · doi:10.3390/cells10102520 · Cited by 10
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Aoyama, K., Yamaguchi, N., Yuki, R., Morii, M., Kubota, S., Hirata, K., Abe, K., Honda, T., Kuga, T., Hashimoto, Y., et al. (2015) · Cell Biology International · doi:10.1002/cbin.10413 · Cited by 14
Lü, P., Yan, M., He, L., Li, J., Ji, Y., & Ji, J. (2018) · International Journal of Biological Sciences · doi:10.7150/ijbs.28642 · Cited by 13
Doering, L., Khatri, R., Petry, S. F., Sauer, H., Howaldt, H., & Linn, T. (2019) · Stem Cell Research & Therapy · doi:10.1186/s13287-019-1330-x · Cited by 13
青华, Aono, J., Findeisen, H. M., Jones, K. L., Heywood, E. B., & Bruemmer, D. (2015) · Journal of Cellular Physiology · doi:10.1002/jcp.25226 · Cited by 13
Kavaliauskaitė, D., Stakišaitis, D., Martinkutė, J., Šlekienė, L., Kazlauskas, A., Balnytė, I., Lesauskaitė, V., & Valančiūtė, A. (2017) · BioMed Research International · doi:10.1155/2017/6326053 · Cited by 13
Stakišaitis, D., Kapočius, L., Valančiūtė, A., Balnytė, I., Tamošuitis, T., Vaitkevičius, A., Sužiedėlis, K., Urbonienė, D., Tatarūnas, V., Kilimaitė, E., et al. (2022) · Biomedicines · doi:10.3390/biomedicines10050962 · Cited by 12
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Deleu, S., Menu, E., Valckenborgh, E. V., Camp, B. V., Fraczek, J., Broek, I. V., Rogiers, V., & Vanderkerken, K. (2009) · Hematology Reports · doi:10.4081/hr.2009.e9 · Cited by 12
Royce, S. G., Ververis, K., & Karagiannis, T. C. (2012) · PubMed · Cited by 12
Borriello, A., Naviglio, S., Bencivenga, D., Caldarelli, I., Tramontano, A., Speranza, M. C., Stampone, E., Sapio, L., Negri, A., Oliva, A., et al. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/2481865 · Cited by 12
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Wang, F., Zhao, K., Yu, S., Xu, A., Han, W., & Mei, Y. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004524 · Cited by 12
Subramanian, V. S., Teafatiller, T., Moradi, H., & Marchant, J. S. (2021) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2021.108838 · Cited by 12
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Park, J., Terranova-Barberio, M., Zhong, A. Y., Thomas, S., & Münster, P. N. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805388-1.00040-7 · Cited by 12
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Kaneko, M., Ishihara, K., Takahashi, A., Hong, J., Hirasawa, N., Zee, O., & Ohuchi, K. (2007) · International Archives of Allergy and Immunology · doi:10.1159/000101401 · Cited by 12
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NovaliA, Z., & van Rossen, T. M. (2016) · Medicinal Chemistry · doi:10.4172/2161-0444.1000384 · Cited by 13
Grimi, A., Bono, B., Lazzarin, S. M., Marcheselli, S., Pessina, F., & Riva, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168953 · Cited by 13
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Metadata
- Authors
- Krämer, O. H., Zhu, P., Ostendorff, H. P., Golebiewski, M., Tiefenbach, J., Peters, M. A., Brill, B., Groner, B., Bach, I., Heinzel, T., & Göttlicher, M.
- Affiliations
- Georg Speyer Haus (DE)
- Universität Hamburg (DE)
- Corresponding author
- Heinzel, Thorsten
- Göttlicher, Martin
- Venue
- The EMBO Journal
- Published
- 2003-07-01
- Volume
- 22
- Issue
- 13
- Pages
- 3411-3420
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC165640
- OpenAlex
- W2106775330
- Cited by
- 523
- References
- 41
- Citations by year
- 2026: 5 · 2025: 8 · 2024: 14 · 2023: 13 · 2022: 25 · 2021: 16 · 2020: 19 · 2019: 20 · 2018: 27 · 2017: 26 · 2016: 30 · 2015: 19 · 2014: 27 · 2013: 33 · 2012: 29
- FWCI
- 8.96
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- mediaTUM – the media and publications repository of the Technical University Munich (Technical University Munich) (submittedVersion)
- Site cant be reached (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- valproic acid, HDAC2, histone deacetylase inhibitors, proteasomal degradation, ubiquitin-proteasome system, RLIM, polyubiquitination, trichostatin A, class I HDACs, protein turnover
- MeSH terms
- Animals, Base Sequence, Cells, Cultured, Cysteine Endopeptidases, Enzyme Inhibitors, Female, Hydrolysis, Hydroxamic Acids, Multienzyme Complexes, Valproic Acid, DNA Primers, Ubiquitin, Proteasome Endopeptidase Complex, Mice, Histone Deacetylase Inhibitors
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