HDAC11 deficiency disrupts oncogene-induced hematopoiesis in myeloproliferative neoplasms
Open accessAbstract
Protein acetylation is an important contributor to cancer initiation. Histone deacetylase 6 (HDAC6) controls JAK2 translation and protein stability and has been implicated in JAK2-driven diseases best exemplified by myeloproliferative neoplasms (MPNs). By using novel classes of highly selective HDAC inhibitors and genetically deficient mouse models, we discovered that HDAC11 rather than HDAC6 is necessary for the proliferation and survival of oncogenic JAK2-driven MPN cells and patient samples. Notably, HDAC11 is variably expressed in primitive stem cells and is expressed largely upon lineage commitment. Although Hdac11is dispensable for normal homeostatic hematopoietic stem and progenitor cell differentiation based on chimeric bone marrow reconstitution, Hdac11 deficiency significantly reduced the abnormal megakaryocyte population, improved splenic architecture, reduced fibrosis, and increased survival in the MPLW515L-MPN mouse model during primary and secondary transplantation. Therefore, inhibitors of HDAC11 are an attractive therapy for treating patients with MPN. Although JAK2 inhibitor therapy provides substantial clinical benefit in MPN patients, the identification of alternative therapeutic targets is needed to reverse MPN pathogenesis and control malignant hematopoiesis. This study establishes HDAC11 as a unique type of target molecule that has therapeutic potential in MPN.
Integrity signals
Registry
Cites
Statistics
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?
Mice with Hdac11 knockout show no significant abnormalities.
“To add further mystery to HDAC11, mice Hdac11 -/-show no significant abnormalities (Huang et al., 2017;Sun et al., 2018;Yue et al., 2020).”
From HDACs and the epigenetic plasticity of cancer cells: target the complexity (2022) · cites this paper as Yue et al., 2020
In myeloproliferative neoplasms (MPN), selective HDAC11 inhibitors regulate the expression of mitotic genes, causing cell cycle arrest.
“In myeloproliferative neoplasms (MPN), selective HDAC11 inhibitors regulate the expression of mitotic genes, causing cell cycle arrest (Yue et al., 2020).”
From HDACs and the epigenetic plasticity of cancer cells: target the complexity (2022) · cites this paper as Yue et al., 2020
HDAC11 is involved in tumors of the hematopoietic system.
“HDAC11 is also involved in tumors of the hematopoietic system.”
From HDACs and the epigenetic plasticity of cancer cells: target the complexity (2022) · cites this paper as Yue et al., 2020
Cites
The Molecular Signatures Database Hallmark Gene Set Collection
Liberzon, A., Birger, C., Thorvaldsdóttir, H., Ghandi, M., Mesirov, J. P., & Tamayo, P. (2015) · Cell Systems · doi:10.1016/j.cels.2015.12.004 · Cited by 13,807 · see citing works
Evaluation of survival data and two new rank order statistics arising in its consideration.
Mantel, N. (1966) · PubMed · Cited by 7,516 · see citing works
Andromeda: A Peptide Search Engine Integrated into the MaxQuant Environment
Cox, J., Neuhauser, N., Michalski, A., Scheltema, R. A., Olsen, J. V., & Mann, M. (2011) · Journal of Proteome Research · doi:10.1021/pr101065j · Cited by 5,349 · see citing works
Skyline: an open source document editor for creating and analyzing targeted proteomics experiments
MacLean, B., Tomazela, D. M., Shulman, N., Chambers, M., Finney, G. L., Frewen, B., Kern, R., Tabb, D. L., Liebler, D. C., & MacCoss, M. J. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq054 · Cited by 4,697 · see citing works
Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040 · see citing works
A Gain-of-Function Mutation of <i>JAK2</i> in Myeloproliferative Disorders
Kralovics, R., Passamonti, F., Buser, A. S., Teo, S.-S., Tiedt, R., Passweg, J. R., Tichelli, A., Cazzola, M., & Skoda, R. C. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa051113 · Cited by 3,470 · see citing works
Levine, R. L., Wadleigh, M., Cools, J., Ebert, B. L., Wernig, G., Huntly, B. J. P., Boggon, T. J., Wlodarska, I., Clark, J. J., Moore, S., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.03.023 · Cited by 2,993 · see citing works
Self-citationHDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403 · see citing works
A double-blind, placebo-controlled trial of ruxolitinib for myelofibrosis
Verstovsek, S., Mesa, R. A., Gotlib, J., Levy, R. S., Gupta, V., DiPersio, J. F., Catalano, J. V., Deininger, M., Miller, C., Silver, R. T., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1110557 · Cited by 2,103 · see citing works
Erasers of Histone Acetylation: The Histone Deacetylase EnzymesPreprint
Seto, E., & Yoshida, M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018713 · Cited by 2,019 · see citing works
Somatic Mutations of Calreticulin in Myeloproliferative Neoplasms
Klampfl, T., Gisslinger, H., Harutyunyan, A. S., Nivarthi, H., Rumi, E., Milosevic, J. D., Them, N. C. C., Berg, T., Gisslinger, B., Pietra, D., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1311347 · Cited by 2,003 · see citing works
Xie, X., Lu, J., Kulbokas, E. J., Golub, T. R., Mootha, V., Lindblad-Toh, K., Lander, E. S., & Kellis, M. (2005) · Nature · doi:10.1038/nature03441 · Cited by 1,872 · see citing works
JAK inhibition with ruxolitinib versus best available therapy for myelofibrosis
Harrison, C., Kiladjian, J.-J., Al-Ali, H. K., Gisslinger, H., Waltzman, R., Stalbovskaya, V., McQuitty, M., Hunter, D. S., Levy, R., Knoops, L., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1110556 · Cited by 1,825 · see citing works
Histone-deacetylase inhibitors: novel drugs for the treatment of cancer
Johnstone, R. W. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd772 · Cited by 1,515 · see citing works
MPLW515L Is a Novel Somatic Activating Mutation in Myelofibrosis with Myeloid Metaplasia
Pikman, Y., Lee, B. H., Mercher, T., McDowell, E. P., Ebert, B. L., Gozo, M. C., Cuker, A. C., Wernig, G., Moore, S. A., Galinsky, I. A., et al. (2006) · PLoS Medicine · doi:10.1371/journal.pmed.0030270 · Cited by 1,445 · see citing works
Self-citationHDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor
Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153 · see citing works
Bali, P., Pranpat, M., Bradner, J., Balasis, M., Fiskus, W., Guo, F., Rocha, K., Kumaraswamy, S., Boyapalle, S., Atadja, P., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500186200 · Cited by 755 · see citing works
Gao, L., Cueto, M. A., Asselbergs, F., & Atadja, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111871200 · Cited by 744 · see citing works
HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
Zhang, Y., Li, N., Caron, C., Matthias, G., Hess, D., Khochbin, S., & Matthias, P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg115 · Cited by 740 · see citing works
In vivo destabilization of dynamic microtubules by HDAC6‐mediated deacetylation
Matsuyama, A., Shimazu, T., Sumida, Y., Saito, A., Yoshimatsu, Y., Seigneurin‐Berny, D., Osada, H., Komatsu, Y., Nishino, N., Khochbin, S., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf682 · Cited by 720 · see citing works
Barbui, T., Thiele, J., Gisslinger, H., Kvasnicka, H. M., Vannucchi, A. M., Guglielmelli, P., Orazi, A., & Tefferi, A. (2018) · Blood Cancer Journal · doi:10.1038/s41408-018-0054-y · Cited by 644 · see citing works
Barbui, T., Thiele, J., Passamonti, F., Rumi, E., Boveri, E., Ruggeri, M., Rodeghiero, F., dʼAmore, E. S. G., Randi, M. L., Bertozzi, I., et al. (2011) · Journal of Clinical Oncology · doi:10.1200/jco.2010.34.5298 · Cited by 534 · see citing works
Single-cell analysis of mixed-lineage states leading to a binary cell fate choice
Olsson, A., Venkatasubramanian, M., Chaudhri, V. K., Aronow, B. J., Salomonis, N., Singh, H., & Grimes, H. L. (2016) · Nature · doi:10.1038/nature19348 · Cited by 476 · see citing works
Self-citationThe histone deacetylase HDAC11 regulates the expression of interleukin 10 and immune tolerance
Villagra, A., Cheng, F., Wang, H.-W., Suarez, I., Glozak, M., Maurin, M., Nguyen, D., Wright, K. L., Atadja, P. W., Bhalla, K., et al. (2009) · Nature Immunology · doi:10.1038/ni.1673 · Cited by 455 · see citing works
Self-citationVitamin A-Retinoic Acid Signaling Regulates Hematopoietic Stem Cell Dormancy
Cabezas-Wallscheid, N., Buettner, F., Sommerkamp, P., Klimmeck, D., Ladel, L., Thalheimer, F. B., Pastor-Flores, D., Roma, L. P., Renders, S., Zeisberger, P., et al. (2017) · Cell · doi:10.1016/j.cell.2017.04.018 · Cited by 454 · see citing works
Cervantes, F., Vannucchi, A. M., Kiladjian, J., et al. (2013) · Blood · doi:10.1182/blood-2013-02-485888 · Cited by 428 · see citing works
An Acetylation Site in the Middle Domain of Hsp90 Regulates Chaperone Function
Scroggins, B. T., Robzyk, K., Wang, D., Marcu, M. G., Tsutsumi, S., Beebe, K., Cotter, R. J., Felts, S., Toft, D., Karnitz, L., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.008 · Cited by 413 · see citing works
HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination
Boyault, C., Sadoul, K., Pabion, M., & Khochbin, S. (2007) · Oncogene · doi:10.1038/sj.onc.1210614 · Cited by 397 · see citing works
Clinical Toxicities of Histone Deacetylase Inhibitors
Subramanian, S., Bates, S. E., Wright, J. J., Espinoza-Delgado, I., & Piekarz, R. L. (2010) · Pharmaceuticals · doi:10.3390/ph3092751 · Cited by 386 · see citing works
Bac to the future: The use of bac transgenic mice for neuroscience research
Heintz, N. (2001) · Nature reviews. Neuroscience · doi:10.1038/35104049 · Cited by 333 · see citing works
Structural insights into HDAC6 tubulin deacetylation and its selective inhibition
Miyake, Y., Keusch, J. J., Wang, L., Saito, M., Hess, D., Wang, X., Melancon, B. J., Helquist, P., Gut, H., & Matthias, P. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2140 · Cited by 315 · see citing works
Verstovsek, S., Gotlib, J., Mesa, R. A., Vannucchi, A. M., Kiladjian, J.-J., Cervantes, F., Harrison, C. N., Paquette, R., Sun, W., Naim, A., et al. (2017) · Journal of Hematology & Oncology · doi:10.1186/s13045-017-0527-7 · Cited by 305 · see citing works
Warfel, N. A., & El‐Deiry, W. S. (2012) · Current Opinion in Oncology · doi:10.1097/cco.0b013e32835b639e · Cited by 287 · see citing works
Histone deacetylase inhibitor (HDACI) mechanisms of action: Emerging insights
Bose, P., Dai, Y., & Grant, S. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.04.004 · Cited by 282 · see citing works
Acetylation site specificities of lysine deacetylase inhibitors in human cells
Schölz, C., Weinert, B. T., Wagner, S., Beli, P., Miyake, Y., Qi, J., Jensen, L. J., Streicher, W. W., McCarthy, A. R., Westwood, N. J., et al. (2015) · Nature Biotechnology · doi:10.1038/nbt.3130 · Cited by 271 · see citing works
Vannucchi, A. M., Kantarjian, H. M., Kiladjian, J.-J., Gotlib, J., Cervantes, F., Mesa, R. A., Sarlis, N. J., Peng, W., Sandor, V., Gopalakrishna, P., et al. (2015) · Haematologica · doi:10.3324/haematol.2014.119545 · Cited by 260 · see citing works
Histone deacetylase inhibitors: Signalling towards p21cip1/waf1
Ocker, M., & Schneider‐Stock, R. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.03.001 · Cited by 252 · see citing works
Rambaldi, A., Dellacasa, C. M., Finazzi, G., Carobbio, A., Ferrari, M. L., Guglielmelli, P., Gattoni, E., Salmoiraghi, S., Finazzi, M. C., Tollo, S. D., et al. (2010) · British Journal of Haematology · doi:10.1111/j.1365-2141.2010.08266.x · Cited by 244 · see citing works
Active maintenance of mHDA2/mHDAC6 histone-deacetylase in the cytoplasm
Verdel, A., Curtet, S., Brocard, M.-P., Rousseaux, S., Lemercier, C., Yoshida, M., & Khochbin, S. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00542-x · Cited by 224 · see citing works
Regulation of CD133 by HDAC6 Promotes β-Catenin Signaling to Suppress Cancer Cell Differentiation
Mak, A. B., Nixon, A. M. L., Kittanakom, S., Stewart, J. M., Chen, G. I., Ćurak, J., Gingras, A., Mazitschek, R., Neel, B. G., Štagljar, I., et al. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.09.016 · Cited by 183 · see citing works
Wang, Y., Fiskus, W. C., Chong, D. G., Buckley, K. M., Natarajan, K., Rao, R., Joshi, A., Balusu, R., Koul, S., Chen, J., et al. (2009) · Blood · doi:10.1182/blood-2009-05-222133 · Cited by 177 · see citing works
Self-citationMyeloproliferative neoplasms: A decade of discoveries and treatment advances
Tefferi, A. (2015) · American Journal of Hematology · doi:10.1002/ajh.24221 · Cited by 176 · see citing works
Histone deacetylase 11 is a fatty-acid deacylase
Kutil, Z., Novakova, Z., Meleshin, M., Mikesova, J., Schutkowski, M., & Barinka, C. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.7b00942 · Cited by 174 · see citing works
Murphy, P. J. M., Morishima, Y., Kovacs, J. J., Yao, T.-P., & Pratt, W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506997200 · Cited by 167 · see citing works
Molecular Pathways: Molecular Basis for Sensitivity and Resistance to JAK Kinase Inhibitors
Meyer, S. C., & Levine, R. L. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-0279 · Cited by 164 · see citing works
Self-citationThépot, S., Itzykson, R., Seegers, V., Raffoux, E., Quesnel, B., Chaït, Y., Sorin, L., Dreyfus, F., Cluzeau, T., Delaunay, J., et al. (2010) · Blood · doi:10.1182/blood-2010-03-274811 · Cited by 156 · see citing works
Targeting megakaryocytic-induced fibrosis in myeloproliferative neoplasms by AURKA inhibition
Wen, Q. J., Yang, Q., Goldenson, B., Malinge, S., Lasho, T. L., Schneider, R. K., Breyfogle, L. J., Schultz, R. F., Gilles, L., Koppikar, P., et al. (2015) · Nature Medicine · doi:10.1038/nm.3995 · Cited by 149 · see citing works
Self-citationHistone deacetylase inhibitors in hematological malignancies and solid tumors
Chun, P. (2015) · Archives of Pharmacal Research · doi:10.1007/s12272-015-0571-1 · Cited by 147 · see citing works
Drugging the HDAC6–HSP90 interplay in malignant cells
Krämer, O. H., Mahboobi, S., & Sellmer, A. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.08.001 · Cited by 133 · see citing works
Risk factors for leukemic transformation in patients with primary myelofibrosis
Huang, J., Li, C., Mesa, R. A., et al. (2008) · Cancer · doi:10.1002/cncr.23505 · Cited by 126 · see citing works
Programming and regulation of metabolic homeostasis by HDAC11
Sun, L., Marin de Evsikova, C., Bian, K., Achille, A., Telles, E., Pei, H., & Seto, E. (2018) · EBioMedicine · doi:10.1016/j.ebiom.2018.06.025 · Cited by 125 · see citing works
Sahakian, E., Powers, J. J., Chen, J., Deng, S., Cheng, F., Graeter, A. I., Woods, D. M., Rock-Klotz, J. A., Sodré, A. L., Youn, J., et al. (2014) · Molecular Immunology · doi:10.1016/j.molimm.2014.08.002 · Cited by 120 · see citing works
Self-citationHDAC11 plays an essential role in regulating OX40 ligand expression in Hodgkin lymphoma
Buglio, D., Khaskhely, N. M., Voo, K. S., Martínez-Valdez, H., Liu, Y., & Younes, A. (2011) · Blood · doi:10.1182/blood-2010-08-303701 · Cited by 119 · see citing works
HDAC11 is a novel drug target in carcinomas
Deubzer, H. E., Schier, M. C., Oehme, I., Lodrini, M., Haendler, B., Sommer, A., & Witt, O. (2013) · International Journal of Cancer · doi:10.1002/ijc.27876 · Cited by 112 · see citing works
HDAC11 is a regulator of diverse immune functions
Yanginlar, C., & Logie, C. (2017) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2017.12.002 · Cited by 106 · see citing works
HDAC6 Deacetylates Ku70 and Regulates Ku70-Bax Binding in Neuroblastoma
Subramanian, C., Jarzembowski, J. A., Opipari, A. W., Castle, V. P., & Kwok, R. P. S. (2011) · Neoplasia · doi:10.1593/neo.11558 · Cited by 105 · see citing works
Evrot, E., Ebel, N., Romanet, V., Röelli, C., Andraos, R., Qian, Z., Dölemeyer, A., Dammassa, E., Sterker, D., Cozens, R. M., et al. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-0905 · Cited by 83 · see citing works
HDAC6 deacetylates p53 at lysines 381/382 and differentially coordinates p53-induced apoptosis
Ryu, H.-W., Shin, D.-H., Lee, D. H., Choi, J., Han, G., Lee, K. Y., & Kwon, S. H. (2017) · Cancer Letters · doi:10.1016/j.canlet.2017.01.033 · Cited by 82 · see citing works
Bonicelli, G., Abdulkarim, K., Mounier, M., et al. (2012) · British Journal of Haematology · doi:10.1111/bjh.12117 · Cited by 81 · see citing works
HSP90 Inhibitors for Cancer Therapy and Overcoming Drug Resistance
Jhaveri, K. L., & Modi, S. (2012) · Advances in pharmacology · doi:10.1016/b978-0-12-397927-8.00015-4 · Cited by 77 · see citing works
Efficacy and safety of ruxolitinib in the treatment of patients with myelofibrosis
Yi, C. A., Tam, C. S. L., & Verstovšek, S. (2015) · Future Oncology · doi:10.2217/fon.14.272 · Cited by 77 · see citing works
Mascarenhas, J. O., Lü, M., Li, T., et al. (2013) · British Journal of Haematology · doi:10.1111/bjh.12220 · Cited by 75 · see citing works
Therapy with the histone deacetylase inhibitor pracinostat for patients with myelofibrosis
Quintás‐Cardama, A., Kantarjian, H. M., Estrov, Z. E., et al. (2012) · Leukemia Research · doi:10.1016/j.leukres.2012.03.003 · Cited by 75 · see citing works
Woods, D. M., Woan, K. V., Cheng, F., Sodré, A. L., Wang, D., Wu, Y., Wang, Z., Chen, J., Powers, J., Pinilla-Ibarz, J., et al. (2017) · Blood · doi:10.1182/blood-2016-08-731505 · Cited by 74 · see citing works
DeAngelo, D. J., Mesa, R. A., Fiskus, W. C., Tefferi, A., Paley, C. S., Wadleigh, M., Ritchie, E. K., Snyder, D., Begna, K. H., Ganguly, S., et al. (2013) · British Journal of Haematology · doi:10.1111/bjh.12384 · Cited by 73 · see citing works
Essential role for histone deacetylase 11 (HDAC11) in neutrophil biology
Sahakian, E., Chen, J., Powers, J. J., Chen, X., Maharaj, K. K., Deng, S., Achille, A. N., Lienlaf, M., Wang, H., Cheng, F., et al. (2017) · Journal of Leukocyte Biology · doi:10.1189/jlb.1a0415-176rrr · Cited by 68 · see citing works
Self-citationNeuroblastoma cells depend on HDAC11 for mitotic cell cycle progression and survival
Thole, T. M., Lodrini, M., Fabian, J., Wuenschel, J., Pfeil, S., Hielscher, T., Kopp-Schneider, A., Heinicke, U., Fulda, S., Witt, O., et al. (2017) · Cell Death & Disease · doi:10.1038/cddis.2017.49 · Cited by 67 · see citing works
Martin, M. W., Lee, J. Y., Lancia, D. R., Ng, P. Y., Han, B., Thomason, J. R., Lynes, M. S., Marshall, C. G., Conti, C., Collis, A. J., et al. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.05.021 · Cited by 63 · see citing works
Self-citationSkov, V., Larsen, T. S., Thomassen, M., Riley, C. H., Jensen, M. K., Bjerrum, O. W., Kruse, T. A., & Hasselbalch, H. C. (2011) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2011.597905 · Cited by 57 · see citing works
Myeloproliferative neoplasms: From JAK2 mutations discovery to JAK2 inhibitor therapies
Passamonti, F., Maffioli, M., Caramazza, D., & Cazzola, M. (2011) · Oncotarget · doi:10.18632/oncotarget.281 · Cited by 56 · see citing works
McGahon, A. J., Brown, D. G., Martin, S. J., Amarante-Mendes, G. P., Cotter, T. G., Cohen, G. M., & Green, D. R. (1997) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400213 · Cited by 51 · see citing works
Efficacy of ALK5 inhibition in myelofibrosis
Yue, L., Bartenstein, M., Zhao, W., Ho, W., Han, Y., Murdun, C., Mailloux, A. W., Zhang, L., Wang, X., Budhathoki, A., et al. (2017) · JCI Insight · doi:10.1172/jci.insight.90932 · Cited by 51 · see citing works
Self-citationGenetic determinants of response and survival in momelotinib-treated patients with myelofibrosis
Pardanani, A. D., Abdelrahman, R. A., Finke, C. M., Lasho, T. L., Begna, K. H., Al‐Kali, A., Hogan, W. J., Litzow, M. R., Hanson, C. A., Ketterling, R. P., et al. (2014) · Leukemia · doi:10.1038/leu.2014.306 · Cited by 46 · see citing works
LNK mutations and myeloproliferative disorders
McMullin, M. F., & Cario, H. (2015) · American Journal of Hematology · doi:10.1002/ajh.24259 · Cited by 44 · see citing works
Hrgović, I., Doll, M., Kleemann, J., Wang, X., Zöller, N. N., Pinter, A., Kippenberger, S., Kaufmann, R., & Meißner, M. (2016) · BMC Cancer · doi:10.1186/s12885-016-2807-y · Cited by 44 · see citing works
Sensitivity and resistance of JAK2 inhibitors to myeloproliferative neoplasms
Bhagwat, N., Levine, R. L., & Koppikar, P. (2013) · International Journal of Hematology · doi:10.1007/s12185-013-1353-5 · Cited by 43 · see citing works
Self-citationMazzacurati, L., Lambert, Q. T., Pradhan, A. R., Griner, L. N., Huszar, D., & Reuther, G. W. (2015) · Oncotarget · doi:10.18632/oncotarget.5653 · Cited by 40 · see citing works
Self-citationTherapy for myeloproliferative neoplasms: when, which agent, and how?
Geyer, H. L., & Mesa, R. A. (2014) · Hematology · doi:10.1182/asheducation-2014.1.277 · Cited by 36 · see citing works
Cardiac hypertrophy associated with myeloproliferative neoplasms in JAK2V617F transgenic mice
Shi, K., Zhao, W., Chen, Y., et al. (2014) · Journal of Hematology & Oncology · doi:10.1186/1756-8722-7-25 · Cited by 30 · see citing works
Wakahashi, K., Minagawa, K., Kawano, Y., Kawano, H., Suzuki, T., Ishii, S., Sada, A., Asada, N., Sato, M. M., Kato, S., et al. (2019) · Blood · doi:10.1182/blood-2018-09-876615 · Cited by 30 · see citing works
Sun, X., Xie, Y., Sun, X., et al. (2019) · Bioscience Reports · doi:10.1042/bsr20181916 · Cited by 29 · see citing works
Andersen, C. L., Mortensen, N. B., Klausen, T., et al. (2014) · Haematologica · doi:10.3324/haematol.2013.096669 · Cited by 28 · see citing works
Histone deacetylase 11 as a key regulator of metabolism and obesity
Bhaskara, S. (2018) · EBioMedicine · doi:10.1016/j.ebiom.2018.08.008 · Cited by 28 · see citing works
Beyond JAK inhibitor therapy in myelofibrosis
Odenike, O. M. (2013) · Hematology · doi:10.1182/asheducation-2013.1.545 · Cited by 25 · see citing works
Park, D. S., Akuffo, A. A., Muench, D. E., Grimes, H. L., Epling‐Burnette, P. K., Maini, P. K., Anderson, A. R. A., & Bonsall, M. B. (2019) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1006913 · Cited by 23 · see citing works
Self-citationTabarroki, A., Saunthararajah, Y., Visconte, V., Cinalli, T., Colaluca, K., Rogers, H. J., Sekeres, M. A., Duong, H. K., Stein, B. L., & Tiu, R. V. (2014) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2014.916805 · Cited by 20 · see citing works
Cerquozzi, S., Farhadfar, N., & Tefferi, A. (2016) · The Cancer Journal · doi:10.1097/ppo.0000000000000169 · Cited by 10 · see citing works
JAK2 Inhibitors: Not the Next Imatinib But Researchers See Other Possibilities
Garber, K. (2009) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djp216 · Cited by 9 · see citing works
Novel therapies for myelofibrosis
Stein, B. L., Cervantes, F., Giles, F. J., et al. (2015) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2015.1037762 · Cited by 8 · see citing works
Transcriptional Control of Stem and Progenitor Potential
Muench, D. E., & Grimes, H. L. (2015) · Current Stem Cell Reports · doi:10.1007/s40778-015-0019-z · Cited by 5 · see citing works
Self-citationMesenchymal Cell Reprogramming in Experimental MPLW515L Mouse Model of Myelofibrosis
Han, Y., Yue, L., Wei, M., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0166014 · Cited by 4 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
HDACs and the epigenetic plasticity of cancer cells: target the complexity
Brancolini, C., Gagliano, T., & Minisini, M. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108190 · Cited by 55 · see citing works
Mostofa, A., Distler, A., Meads, M. B., Sahakian, E., Powers, J. J., Achille, A., Noyes, D., Wright, G., Fang, B., Izumi, V., et al. (2021) · JCI Insight · doi:10.1172/jci.insight.151713 · Cited by 27 · see citing works
Self-citationBaselious, F., Robaa, D., & Sippl, W. (2023) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2023.107700 · Cited by 20 · see citing works
- Authors
- Yue, L., Sharma, V., Horvat, N. P., Akuffo, A. A., Beatty, M. S., Murdun, C., Colin, C., Billington, J. M. R., Goodheart, W. E., Sahakian, E., Zhang, L., Powers, J. J., Amin, N. E., Lambert-Showers, Q. T., Darville, L. N., Pinilla-Ibarz, J., Reuther, G. W., Wright, K. L., Conti, C., Lee, J. Y., Zheng, X., Ng, P. Y., Martin, M. W., Marshall, C. G., Koomen, J. M., Levine, R. L., Verma, A., Grimes, H. L., Sotomayor, E. M., Shao, Z., & Epling-Burnette, P. K.
- Affiliations
- Tianjin Medical University General Hospital (CN)
- Moffitt Cancer Center (US)
- University of South Florida (US)
- Forma Therapeutics (United States) (US)
- Memorial Sloan Kettering Cancer Center (US)
- Albert Einstein College of Medicine (US)
- Cincinnati Children's Hospital Medical Center (US)
- Department of Hematology & Oncology, George Washington Cancer Center, Washington, DC; and
- Department of Immunology, H. Lee Moffitt Cancer Center & Research Institute, Tampa, FL;
- Corresponding author
- Yue, Lanzhu
- Sharma, Vasundhara
- ORCID
- Yue, Lanzhu
- Sharma, Vasundhara
- Horvat, Nathan P.
- Akuffo, Afua A.
- Beatty, Matthew S.
- Murdun, Cem
- Colin, Christelle
- Billington, Julia M. R.
- Sahakian, Eva
- Zhang, Ling
- Powers, John J.
- Amin, Narmin E.
- Lambert-Showers, Que T.
- Darville, Lancia N.
- Pinilla-Ibarz, Javier
- Reuther, Gary W.
- Wright, Kenneth L.
- Conti, Chiara
- Lee, Jennifer Y.
- Zheng, Xiaozhang
- Martin, Matthew W.
- Marshall, C. Gary
- Koomen, John M.
- Levine, Ross L.
- Verma, Amit
- Grimes, H. Leighton
- Sotomayor, Eduardo M.
- Shao, Zonghong
- Epling-Burnette, Pearlie K.
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2020-01-16
- Volume
- 135
- Issue
- 3
- Pages
- 191-207
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- PMC
- PMC6966930
- OpenAlex
- W2990269696
- Cited by
- 67
- References
- 91
- Citations by year
- 2026: 9 · 2025: 5 · 2024: 11 · 2023: 10 · 2022: 11 · 2021: 12 · 2020: 8 · 2019: 1
- FWCI
- 4.39
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Blood (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Veterans Affairs (I01 CX000114)
- National Cancer Institute (P30CA008748, P01CA108671, P30CA076292)
- Topics
- Health Sciences › Medicine › Genetics › Myeloproliferative Neoplasms: Diagnosis and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Health Sciences › Medicine › Hematology › Acute Myeloid Leukemia Research
- Keywords
- HDAC11, HDAC6, myeloproliferative neoplasms, JAK2, protein acetylation, histone deacetylase inhibitors, megakaryocytes, hematopoietic stem and progenitor cells, splenic fibrosis, therapeutic target
- MeSH terms
- Animals, Cell Cycle, Hematopoiesis, Histone Deacetylases, Humans, Mice, Inbred C57BL, Mutation, Myeloproliferative Disorders, Oncogenes, Tumor Cells, Cultured, Apoptosis, Mice, Knockout, Cell Proliferation, STAT Transcription Factors, Mice, Janus Kinase 1, Histone Deacetylase Inhibitors
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