The DOI matches its Crossref record; 70 of the 71 references it cites were found in a registry or an index.
Transcriptional silencing of γ-globin by BCL11A involves long-range interactions and cooperation with SOX6
Open accessAbstract
The developmental switch from human fetal (γ) to adult (β) hemoglobin represents a clinically important example of developmental gene regulation. The transcription factor BCL11A is a central mediator of γ-globin silencing and hemoglobin switching. Here we determine chromatin occupancy of BCL11A at the human β-globin locus and other genomic regions in vivo by high-resolution chromatin immunoprecipitation (ChIP)–chip analysis. BCL11A binds the upstream locus control region (LCR), ɛ-globin, and the intergenic regions between γ-globin and δ-globin genes. A chromosome conformation capture (3C) assay shows that BCL11A reconfigures the β-globin cluster by modulating chromosomal loop formation. We also show that BCL11A and the HMG-box-containing transcription factor SOX6 interact physically and functionally during erythroid maturation. BCL11A and SOX6 co-occupy the human β-globin cluster along with GATA1, and cooperate in silencing γ-globin transcription in adult human erythroid progenitors. These findings collectively demonstrate that transcriptional silencing of γ-globin genes by BCL11A involves long-range interactions and cooperation with SOX6. Our findings provide insight into the mechanism of BCL11A action and new clues for the developmental gene regulatory programs that function at the β-globin locus.
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?
The cited source says what the claim attributes to it.
In the citing paper
“Subsequent studies demonstrated that BCL11A, a zinc- fi nger transcription factor, is a bona fi de repressor of HbF expression (4 -7).”
From Corepressor-dependent silencing of fetal hemoglobin expression by BCL11A (2013) · cites this paper as [6]
The cited source says what the claim attributes to it.
In the citing paper
“Further molecular studies revealed that BCL11A interacts with several erythroid regulators including GATA1, FOG1, and SOX6, and with the nucleosome remodeling and deacetylase complex (NuRD) (4, 6).”
From Corepressor-dependent silencing of fetal hemoglobin expression by BCL11A (2013) · cites this paper as [6]
The cited source says what the claim attributes to it.
In the citing paper
“In control cells, ChIP analysis revealed that BCL11A occupies several discrete regions within the human β -globin cluster, including the DNase I hypersensitive site 3 (HS3) within the locus control region (LCR), the e -globin promoter, and the γδ -intergenic region, consistent with previous analyses (4, 6).”
From Corepressor-dependent silencing of fetal hemoglobin expression by BCL11A (2013) · cites this paper as [6]
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
The Role of Chromatin during Transcription
Li, B., Carey, M., & Workman, J. L. (2007) · Cell · doi:10.1016/j.cell.2007.01.015 · Cited by 3,503
The ENCODE (ENCyclopedia Of DNA Elements) Project
(2004) · Science · doi:10.1126/science.1105136 · Cited by 2,390
Position-independent, high-level expression of the human β-globin gene in transgenic mice
Grosveld, F. G., van Assendelft, G. B., Greaves, D. R., & Kollias, G. A. (1987) · Cell · doi:10.1016/0092-8674(87)90584-8 · Cited by 1,908
The UCSC Genome Browser Database
Karolchik, D. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg129 · Cited by 1,890
A Lentiviral RNAi Library for Human and Mouse Genes Applied to an Arrayed Viral High-Content Screen
Moffat, J., Grueneberg, D. A., Yang, X., Kim, S. Y., Kloepfer, A. M., Hinkle, G., Piqani, B., Eisenhaure, T., Luo, B., Grenier, J. K., et al. (2006) · Cell · doi:10.1016/j.cell.2006.01.040 · Cited by 1,804
Simonis, M., Klous, P., Splinter, E., Moshkin, Y., Willemsen, R., de Wit, E., van Steensel, B., & de Laat, W. (2006) · Nature Genetics · doi:10.1038/ng1896 · Cited by 1,386
Looping and Interaction between Hypersensitive Sites in the Active β-globin Locus
Tolhuis, B., Palstra, R.-J., Splinter, E., Grosveld, F., & de Laat, W. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00781-5 · Cited by 1,344
FoxA1 Translates Epigenetic Signatures into Enhancer-Driven Lineage-Specific Transcription
Lupien, M., Eeckhoute, J., Meyer, C. A., Wang, Q., Zhang, Y., Li, W., Carroll, J. S., Liu, X. S., & Brown, M. (2008) · Cell · doi:10.1016/j.cell.2008.01.018 · Cited by 983
Human Fetal Hemoglobin Expression Is Regulated by the Developmental Stage-Specific Repressor BCL11A
Sankaran, V. G., Menne, T. F., Xu, J., Akie, T. E., Lettre, G., Van Handel, B., Mikkola, H. K. A., Hirschhorn, J. N., Cantor, A. B., & Orkin, S. H. (2008) · Science · doi:10.1126/science.1165409 · Cited by 919
Self-citationFrom head to toes: the multiple facets of Sox proteins
Wegner, M. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.6.1409 · Cited by 890
Flagged first, then by citations
1 of the 71 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 201–300 of 361
The Role of the hGH Locus Control Region in Somatotrope Restriction of hGH-N Gene Expression
Ho, Y., Liebhaber, S. A., & Cooke, N. E. (2011) · Molecular Endocrinology · doi:10.1210/me.2010-0411 · Cited by 17
Analysis of circRNAs and circRNA-associated competing endogenous RNA networks in β-thalassemia
Fang, Y., Ruan, H., Li, S., Hou, W., Qiu, Y., Deng, L., Su, S., Chen, P., Pang, L., & Lai, K. (2022) · Scientific Reports · doi:10.1038/s41598-022-12002-0 · Cited by 16
In The Blood: Connecting Variant to Function In Human Hematopoiesis
Nandakumar, S. K., Liao, X., & Sankaran, V. G. (2020) · Trends in Genetics · doi:10.1016/j.tig.2020.05.006 · Cited by 18
Self-citationMolecular analysis of the erythroid phenotype of a patient with BCL11A haploinsufficiency
Wessels, M. W., Cnossen, M. H., van Dijk, T. B., Gillemans, N., Schmidt, K. L. J., van Lom, K., Vinjamur, D. S., Coyne, S. M., Kurita, R., Nakamura, Y., et al. (2021) · Blood Advances · doi:10.1182/bloodadvances.2020003753 · Cited by 16
Epigenomic analysis of KLF1 haploinsufficiency in primary human erythroblasts
Heshusius, S., Grech, L., Gillemans, N., Brouwer, R. W. W., den Dekker, A. T., van IJcken, W. F. J., Nota, B., Felice, A. E., van Dijk, T. B., Lindern, M. V., et al. (2022) · Scientific Reports · doi:10.1038/s41598-021-04126-6 · Cited by 16
BCL11A expression in acute myeloid leukemia
Tao, H., Ma, X., Su, G., Yin, J., Xie, X., Hu, C., Chen, Z., Tan, D., Xu, Z., Zheng, Y., et al. (2015) · Leukemia Research · doi:10.1016/j.leukres.2015.12.001 · Cited by 18
Fanis, P., Kousiappa, I., Phylactides, M., Kyrri, A. R., Hadjigavriel, M., Christou, S., Sitarou, M., & Kleanthous, M. (2019) · Human Mutation · doi:10.1002/humu.23817 · Cited by 15
Gamage, U., Warnakulasuriya, K., Hansika, S., & Silva, G. N. (2023) · Thalassemia Reports · doi:10.3390/thalassrep13010006 · Cited by 17
Ikuta, T., Adekile, A. D., Gutsaeva, D. R., Parkerson, J. B., Yerigenahally, S. D., Clair, B., Kutlar, A., Odo, N., & Head, C. A. (2011) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2011.08.005 · Cited by 15
Epigenetic interplay at the β-globin locus
Lee, W. S., McColl, B., Maksimovic, J., & Vadolas, J. (2017) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2017.01.014 · Cited by 14
Epo reprograms the epigenome of erythroid cells
Perreault, A. A., Benton, M. L., Koury, M. J., Brandt, S. J., & Venters, B. J. (2017) · Experimental Hematology · doi:10.1016/j.exphem.2017.03.004 · Cited by 18
El-Ghamrawy, M., Yassa, M. E., Tousson, A. M. S., Elhady, M. A., Mikhaeil, E., Mohamed, N. B., & Khorshied, M. M. (2020) · Annals of Hematology · doi:10.1007/s00277-020-04187-z · Cited by 16
Effective therapies for sickle cell disease: are we there yet?
Crossley, M., Christakopoulos, G. E., & Weiss, M. J. (2022) · Trends in Genetics · doi:10.1016/j.tig.2022.07.003 · Cited by 18
Kuo, K. H. M. (2017) · Genomics Insights · doi:10.1177/1178631017721178 · Cited by 14
Okam, M. M., & Ebert, B. L. (2012) · Expert Review of Hematology · doi:10.1586/ehm.12.20 · Cited by 14
Adelvand, P., Hamid, M., & Sardari, S. (2017) · Expert Review of Hematology · doi:10.1080/17474086.2018.1406795 · Cited by 13
Lee, B.-S., Dekker, J. D., Lee, B.-K., Iyer, V. R., Sleckman, B. P., Shaffer, A. L., Ippolito, G. C., & Tucker, P. W. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00987-12 · Cited by 13
RetractedJia, W., Jia, S., Chen, P., & He, Y. (2019) · Medical Science Monitor · doi:10.12659/msm.915946 · Cited by 13
Transcriptional Repressor BCL11A in Erythroid Cells
Zheng, G., & Orkin, S. H. (2024) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-62731-6_9 · Cited by 13
Self-citationThe Nucleosome Remodeling and Deacetylase Complex in Development and Disease
Basta, J. M., & Rauchman, M. I. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-800802-7.00003-4 · Cited by 14
Ali, H., Khan, F., & Musharraf, S. G. (2021) · Biochemical Pharmacology · doi:10.1016/j.bcp.2021.114612 · Cited by 12
Ali, H., Iftikhar, F., Shafi, S., Siddiqui, H. L., Khan, I. A., Choudhary, M. I., & Musharraf, S. G. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.05.027 · Cited by 13
Hit and Run Transcriptional Repressors Are Difficult to Catch in the Act
Shah, M., Funnell, A. P. W., Quinlan, K. G. R., & Crossley, M. (2019) · BioEssays · doi:10.1002/bies.201900041 · Cited by 13
Rajendiran, V., Devaraju, N., Haddad, M., Ravi, N. S., Panigrahi, L., Paul, J., Gopalakrishnan, C., Wyman, S. K., Ariudainambi, K., Mahalingam, G., et al. (2024) · Molecular Therapy · doi:10.1016/j.ymthe.2024.01.023 · Cited by 12
Zhu, X., Xi, C., Ward, A., Takezaki, M., Shi, H., Peterson, K. R., & Pace, B. S. (2020) · Experimental Biology and Medicine · doi:10.1177/1535370220945305 · Cited by 11
Fornari, T. A., Lanaro, C., de Albuquerque, D. M., Ferreira, R., & Costa, F. F. (2016) · Experimental Biology and Medicine · doi:10.1177/1535370216668052 · Cited by 12
Physiological and Aberrant γ-Globin Transcription During Development
Barbarani, G., Łabędź, A., Stucchi, S., Abbiati, A., & Ronchi, A. E. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.640060 · Cited by 12
Transcriptional reprogramming in neonatal hematopoietic stem and progenitor cells
Li, Y., & Magee, J. A. (2021) · Experimental Hematology · doi:10.1016/j.exphem.2021.07.004 · Cited by 12
An in vivo model for analysis of developmental erythropoiesis and globin gene regulation
McColl, B., Kao, B., Lourthai, P., Chan, K., Wardan, H., Roosjen, M., Delagneau, O., Gearing, L. J., Blewitt, M. E., Svasti, S., et al. (2014) · The FASEB Journal · doi:10.1096/fj.13-246637 · Cited by 11
Blobel, G. A., Bodine, D., Brand, M., Crispino, J., de Bruijn, M. F. T. R., Nathan, D., Papayannopoulou, T., Porcher, C., Strouboulis, J., Zon, L., et al. (2015) · Experimental Hematology · doi:10.1016/j.exphem.2015.06.008 · Cited by 9
Engineering Globin Gene Expression
Davis, R., Gurumurthy, A., Hossain, M. A., Gunn, E. M., & Bungert, J. (2018) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2018.12.004 · Cited by 10
Transcriptional Repressors of Fetal Globin Genes as Novel Therapeutic Targets in Beta-Thalassemia
Martino, M. D., Sessa, R., Storino, M. R., Giuliano, M., Trombetti, S., Catapano, R., Bianco, A. L., Izzo, P., & Grosso, M. (2020) · IntechOpen eBooks · doi:10.5772/intechopen.90762 · Cited by 10
Spatiotemporal expression and control of haemoglobin in space
Borg, J., Loy, C., Loy, C., Buhagiar, A., Chin, C. R., Damle, N., Vlaminck, I. D., Felice, A., Liu, T., Matei, I. R., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49289-8 · Cited by 9
Carrocini, G. C. S., Venâncio, L. P. R., & Bonini-Domingos, C. R. (2015) · Evolutionary Bioinformatics · doi:10.4137/ebo.s15364 · Cited by 10
Genetic Factors Modifying Sickle Cell Disease Severity
Gardner, K., & Thein, S. L. (2016) · Springer eBooks · doi:10.1007/978-3-319-06713-1_15 · Cited by 11
Modelling human haemoglobin switching
Diepstraten, S. T., & Hart, A. H. (2018) · Blood Reviews · doi:10.1016/j.blre.2018.06.001 · Cited by 13
Atypical β-S haplotypes: classification and genetic modulation in patients with sickle cell anemia
Okumura, J. V., da Silva, D. G. H., Torres, L. S., Belini-Junior, E., Venâncio, L. P. R., Carrocini, G. C. S., Nascimento, P. P., Lobo, C. L. C., & Bonini-Domingos, C. R. (2019) · Journal of Human Genetics · doi:10.1038/s10038-018-0554-4 · Cited by 10
Gene Editing-Based Technologies for Beta-hemoglobinopathies Treatment
Rahimmanesh, I., Boshtam, M., Kouhpayeh, S., Khanahmad, H., Dabiri, A., Ahangarzadeh, S., Esmaeili, Y., Bidram, E., Vaseghi, G., Javanmard, S. H., et al. (2022) · Biology · doi:10.3390/biology11060862 · Cited by 11
Li, Y., Ding, L., Yang, C., Kang, B., Liu, L., Story, M. D., & Pace, B. S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0107133 · Cited by 10
Effect of Induced Pluripotent Stem Cell Technology in Blood Banking
Focosi, D., & Pistello, M. (2016) · Stem Cells Translational Medicine · doi:10.5966/sctm.2015-0257 · Cited by 10
The Coup-TFII orphan nuclear receptor is an activator of the γ-globin gene
Fugazza, C., Barbarani, G., Elangovan, S., Marini, M. G., Giolitto, S., Font-Monclus, I., Marongiu, M. F., Manunza, L., Strouboulis, J., Cantù, C., et al. (2020) · Haematologica · doi:10.3324/haematol.2019.241224 · Cited by 10
Andrieu‐Soler, C., & Soler, É. (2020) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000577 · Cited by 10
Zhou, Y., Dogiparthi, V. R., Ray, S., Schaefer, M. A., Harris, H. L., Rowley, M. J., & Hewitt, K. J. (2023) · Blood Advances · doi:10.1182/bloodadvances.2022009163 · Cited by 10
Transcriptional Profiling of Non-Human Primate Lymphoid Organ Responses to Total-Body Irradiation
Caudell, D. L., Michalson, K. T., Andrews, R. N., Snow, W. W., Bourland, J. D., DeBo, R. J., Cline, J. M., Sempowski, G. D., & Register, T. C. (2019) · Radiation Research · doi:10.1667/rr15100.1 · Cited by 9
Ali, H., Khan, F., & Musharraf, S. G. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112058 · Cited by 9
Luanpitpong, S., Kang, X., Janan, M., Thumanu, K., Li, J., Kheolamai, P., & Issaragrisil, S. (2022) · Stem Cell Research & Therapy · doi:10.1186/s13287-022-02954-5 · Cited by 9
Wunderlich, T. M., Deshpande, C. N., Paasche, L. W., Friedrich, T., Diegmüller, F., Haddad, E., Kreienbaum, C., Naseer, H., Stebel, S. E., Daus, N., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae926 · Cited by 7
Key Pharmacogenomic Considerations for Sickle Cell Disease Patients
Κολλιοπούλου, Α., Στρατόπουλος, Α., Siamoglou, S., Sgourou, A., Ali, B. R., Papachatzopoulou, A., Κάτσιλα, Θ., & Patrinos, G. P. (2017) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2017.0058 · Cited by 8
Geard, A. F., Pule, G. D., Chelo, D., Bitoungui, V. J. N., & Wonkam, A. (2016) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2016.0125 · Cited by 8
CRISPR Editing Enables Consequential Tag-Activated MicroRNA-Mediated Endogene Deactivation
Papasavva, P. L., Patsali, P., Loucari, C. C., Kurita, R., Nakamura, Y., Kleanthous, M., & Lederer, C. W. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031082 · Cited by 7
de la Torre, L. D. C. R., Borrayo-LóPez, F. J., Perea, F. J., Aquino, E., Venegas, M., Hernández-Carbajal, C., Espinoza-Mata, L. L., & Ibarra‐Cortés, B. (2022) · Journal of Tropical Pediatrics · doi:10.1093/tropej/fmac073 · Cited by 7
The Genomic Relationship Between Primary Breast Carcinomas and Their Nodal Metastases
Desouki, M. M., Liao, S., Conroy, J. M., Nowak, N. J., Shepherd, L. A., Gaile, D. P., & Geradts, J. (2011) · Cancer Investigation · doi:10.3109/07357907.2011.568564 · Cited by 7
Maroofi, N., Azarkeivan, A., Banihashemi, S., Mohammadparast, S., Aghajanirefah, A., & Banan, M. (2017) · Pharmacogenomics · doi:10.2217/pgs-2017-0019 · Cited by 7
Inhibition of γ/β Globin Gene Switching in CD 34+ Derived Erythroid Cells by BCL11A RNA Silencing
Taghavi, S. A., Hosseini, K. M., Tamaddon, G., & Kasraian, L. (2019) · Indian Journal of Hematology and Blood Transfusion · doi:10.1007/s12288-019-01131-8 · Cited by 7
Makino, T., Haruyama, M., Katayama, K., Terashima, H., Tsunemi, T., Miyazaki, K., Terakawa, M., Yamashiro, K., Yoshioka, R., & Maeda, H. (2019) · Biochemical Pharmacology · doi:10.1016/j.bcp.2019.113717 · Cited by 7
Shariati, L., Modarressi, M. H., Tabatabaiefar, M. A., Kouhpayeh, S., Hejazi, Z., Shahbazi, M., Sabzehei, F., Salehi, M., & Khanahmad, H. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.28130 · Cited by 7
Jiang, J., Ren, R., Cheng, Y.-J., Li, X., & Zhang, G. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1327466 · Cited by 6
Unravelling pathways downstream Sox6 induction in K562 erythroid cells by proteomic analysis
Barbarani, G., Ronchi, A. E., Ruoppolo, M., Santorelli, L., Steinfelder, R. S., Elangovan, S., Fugazza, C., & Caterino, M. (2017) · Scientific Reports · doi:10.1038/s41598-017-14336-6 · Cited by 6
Wang, W., Zhao, H., Yang, Y., Chi, Y., Lv, X., & Zhang, L. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.10.068 · Cited by 6
Kaewsakulthong, W., Pongpaksupasin, P., Nualkaew, T., Hongeng, S., Fucharoen, S., Jearawiriyapaisarn, N., & Sripichai, O. (2021) · Hematology Reports · doi:10.4081/hr.2021.9215 · Cited by 6
Structural insights into the DNA-binding mechanism of BCL11A: The integral role of ZnF6
Viennet, T., Yin, M., Jayaraj, A., Kim, W., Sun, Z.-Y. J., Fujiwara, Y., Zhang, K., Seruggia, D., Seo, H., Dhe‐Paganon, S., et al. (2024) · Structure · doi:10.1016/j.str.2024.09.022 · Cited by 8
Self-citationKarkashon, S., Raghupathy, R., Bhatia, H., Dutta, A., Hess, S. Y., Higgs, J., Tifft, C. J., & Little, J. A. (2015) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2015.05.006 · Cited by 7
Gao, Y., He, D., Chen, S., Yan, X., Hu, X., & Li, Y. (2011) · Clinical Oncology and Cancer Research · doi:10.1007/s11805-011-0588-2 · Cited by 7
Génétique des maladies de l’hémoglobine
Couque, N., Trawinski, E., & Élion, J. (2016) · Revue Francophone des Laboratoires · doi:10.1016/s1773-035x(16)30128-9 · Cited by 8
Heydari, N., Shariati, L., Khanahmad, H., Hejazi, Z., Shahbazi, M., & Salehi, M. (2016) · PubMed Central · doi:10.22038/ijbms.2016.7731 · Cited by 6
Advances in β-Thalassemia Gene Therapy: CRISPR/Cas Systems and Delivery Innovations
Liu, H., & Zhang, P. (2025) · Cells · doi:10.3390/cells14201595 · Cited by 8
-globin expression is regulated by SUV4-20h1
Wang, Y., Rank, G., Li, Z., Wang, Y., Ju, J., Nuber, A., Wu, Y., Liu, M., Nie, M., Huang, F., et al. (2016) · Haematologica · doi:10.3324/haematol.2015.139980 · Cited by 5
Listı̀, F., Sclafani, S., Agrigento, V., Barone, R. M. E., Maggio, A., & D’Alcamo, E. (2018) · Hemoglobin · doi:10.1080/03630269.2018.1482832 · Cited by 5
Tepakhan, W., Kanjanaopas, S., & Srewaradachpisal, K. (2020) · Hemoglobin · doi:10.1080/03630269.2020.1811117 · Cited by 5
Chang, Y.-J., Kang, Z., Bei, J., Chou, S., Lu, M. J., Su, Y.-L., Lin, S., Wang, H., Lin, S., & Chang, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23126839 · Cited by 5
Wang, Y., Wang, Y., Ma, L., Nie, M., Ju, J., Liu, M., Deng, Y., Yao, B., Gui, T., Li, X., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.768515 · Cited by 5
Sankaran, V. G., Menne, J., & Heller, R. (2011) · Blood · doi:10.1182/blood-2010-11-320887 · Cited by 5
Self-citationEpigenetic Regulation of Erythropoiesis: From Developmental Programs to Therapeutic Targets
Vasiloudis, N.-I., Paschoudi, K., Beta, C., Georgolopoulos, G., & Psatha, N. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26136342 · Cited by 8
Papaioannou, N. Y., Patsali, P., Klermund, J., Papasavva, P. L., Andrieux, G., Koniali, L., Naiisseh, B., Christou, S., Sitarou, M., Kleanthous, M., et al. (2026) · Genome biology · doi:10.1186/s13059-026-03974-7 · Cited by 4
Chauhan, W., & Zennadi, R. (2026) · Antioxidants · doi:10.3390/antiox15030324 · Cited by 5
Transcriptional repression of the oncofetal LIN28B gene by the transcription factor SOX6
Pastori, V., Zambanini, G., Citterio, E., Weiss, T., Nakamura, Y., Cantù, C., & Ronchi, A. E. (2024) · Scientific Reports · doi:10.1038/s41598-024-60438-3 · Cited by 4
Mehraei, M., Bashirov, R., & Tüzmen, Ş. (2016) · Journal of Bioinformatics and Computational Biology · doi:10.1142/s0219720016500268 · Cited by 5
Iftikhar, F., Khan, M. B. N., Tehreem, S., Kanwal, N., & Musharraf, S. G. (2023) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2023.106768 · Cited by 4
Quantification of human embryonic ζ-globin chains in Southeast Asian deletion (--SEA) carriers
Ye, Y.-H., Sun, G., Ren, Z., Liang, Y.-M., Luo, H., Lin, P., Wang, X., Dong, Z., Huang, L., Qin, L., et al. (2022) · Journal of Clinical Pathology · doi:10.1136/jcp-2022-208159 · Cited by 3
Maroofi, N., Maleki, M. S. M., Tahmasebi, M., Khorshid, H. R. K., Modaberi, Y., Najafipour, R., & Banan, M. (2024) · Molecular Biotechnology · doi:10.1007/s12033-024-01155-0 · Cited by 3
Impact of hydroxycarbamide treatment on the whole‐blood transcriptome in sickle cell disease
Bhat, V., Potdar, A. A., Yu, G. K., Gibson, G. C., & Sheehan, V. (2024) · British Journal of Haematology · doi:10.1111/bjh.19839 · Cited by 3
Direct and indirect regulation of fetal globin transcript by the RNA-binding protein IGF2BP1
Coyne, S. M., Hwang, G.-H., Wu, T., Hossain, M. A., Vinjamur, D. S., Starrs, M. M., Zeng, J., Andresen, F., Gutierrez, A. M., Shimamura, A., et al. (2026) · Blood · doi:10.1182/blood.2025031840 · Cited by 4
Ferenz, K. B., Karaman, O., & Shah, S. B. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-823971-1.00018-0 · Cited by 4
miR-365-3p mediates BCL11A and SOX6 erythroid-specific coregulation: A new player in HbF activation
Simbula, M., Manchinu, M. F., Mingoia, M., Pala, M., Asunis, I., Caria, C. A., Perseu, L., Shah, M., Crossley, M., Moi, P., et al. (2023) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2023.09.002 · Cited by 3
Buccheri, M. A., Spina, S., Ruberto, C., Lombardo, T., Labie, D., & Ragusa, A. (2013) · Hemoglobin · doi:10.3109/03630269.2013.800823 · Cited by 3
Mahdavi, M. R., Pourfarzad, F., Kosaryan, M., & Akbari, M. T. (2017) · PubMed Central · Cited by 3
DNA regulatory element cooperation and competition in transcription
Lee, H., Friedman, M. J., Kim, S. B., & Oh, S. (2024) · BMB Reports · doi:10.5483/bmbrep.2024-0069 · Cited by 4
Role of B-Cell Lymphoma/Leukemia 11A in Normal and Malignant Hematopoiesis
Zhang, H., Zeng, J., Zhang, F., Liu, J., & Liang, L. (2025) · Biology · doi:10.3390/biology14010026 · Cited by 4
Song, M., Wei, X., Luo, H., Wang, J., Ye, Y., Qin, L., Niu, C., Long, Y., Wang, X., Shao, C., et al. (2025) · Blood Advances · doi:10.1182/bloodadvances.2024013695 · Cited by 3
Yang, D. C., Ma, Z.-F., Lin, W., Yang, J., Tian, C., Wei, H., Jiang, Y., & He, F. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2012.12.014 · Cited by 3
Lentiviral vector containing beta-globin gene for beta thalassemia gene therapy
Abbasalipour, M., Khosravi, M. A., Zeinali, S., Khanahmad, H., Azadmanesh, K., & Karimipoor, M. (2022) · Gene Reports · doi:10.1016/j.genrep.2022.101615 · Cited by 3
Khan, F., Ali, H., & Musharraf, S. G. (2022) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2022.175036 · Cited by 3
Rise of the Chromodomain Helicase DNA‐Binding (CHD) Chromatin Remodelling Machines
Alendar, A. (2023) · Wiley eBooks · doi:10.1002/9780470015902.a0029448 · Cited by 3
Liu, J., Park, K., Shen, Z., Ye, Y., Lee, E., Herman, R. A., Zhu, X., Lu, W., Nuhfer, J., Bassal, M. A., et al. (2024) · Transfusion Medicine Reviews · doi:10.1016/j.tmrv.2024.150861 · Cited by 2
The induction effect of hydroxyurea and metformin on fetal globin in the K562 cell line
Eini, M., Safarpour, H., & Miri-Moghddam, E. (2025) · Molecular Medicine · doi:10.1186/s10020-025-01184-8 · Cited by 1
Zhu, J., Chin, K., Zou, J., Aerbajinai, W., Lin, W.-C., Li, H., & Rodgers, G. P. (2025) · Blood · doi:10.1182/blood.2025029969 · Cited by 2
Jin, T., Zhang, Z., Han, Y., Li, D., Liu, J., Jiang, M., Zhu, J., Kurita, R., Nakamura, Y., Hu, F., et al. (2022) · Journal of Immunology Research · doi:10.1155/2022/8440422 · Cited by 2
Mehra, P., & Kalani, A. (2018) · Life Sciences · doi:10.1016/j.lfs.2018.09.021 · Cited by 2
Nitric Oxide / Cyclic Nucleotide Regulation of Globin Genes in Erythropoiesis
Vladan, P., Bojana, B., Jovi, G., Raj, K., & Alan, N. (2012) · InTech eBooks · doi:10.5772/34534 · Cited by 2
Lulli, V., Romania, P., Morsilli, O., Ilari, R., Gabbianelli, M., Testa, U., & Marziali, G. (2014) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2014.10.004 · Cited by 2
Metadata
- Authors
- Xu, J., Sankaran, V. G., Ni, M., Menne, T. F., Puram, R. V., Kim, W., & Orkin, S. H.
- Affiliations
- Boston Children's Hospital (US)
- Harvard University (US)
- Harvard–MIT Division of Health Sciences and Technology (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2010-04-15
- Volume
- 24
- Issue
- 8
- Pages
- 783-798
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC2854393
- OpenAlex
- W2134881764
- Semantic Scholar
- 097ee5589990708503598c372d66d87bf5262280
- Cited by
- 361
- References
- 71
- Citations by year
- 2026: 12 · 2025: 19 · 2024: 19 · 2023: 15 · 2022: 23 · 2021: 21 · 2020: 20 · 2019: 17 · 2018: 21 · 2017: 31 · 2016: 30 · 2015: 25 · 2014: 26 · 2013: 23 · 2012: 22
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Howard Hughes Medical Institute
- Kay Kendall Leukaemia Fund
- National Institutes of Health
- National Heart, Lung, and Blood Institute (R01HL032259, T32HL116324)
- National Cancer Institute (K12CA087723)
- National Institute of General Medical Sciences (T32GM007753)
- National Institute of Diabetes and Digestive and Kidney Diseases
- Topics
- Health Sciences › Medicine › Genetics (clinical) › Hemoglobinopathies and Related Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Keywords
- BCL11A, SOX6, beta-globin locus, hemoglobin switching, long-range chromatin interactions, chromatin looping, locus control region, erythroid maturation, GATA-1, erythroid progenitor cells, developmental gene regulation, chromatin occupancy
- MeSH terms
- Adult, Animals, Carrier Proteins, Cell Line, Erythropoiesis, Histones, Humans, Nuclear Proteins, Protein Binding, Repressor Proteins, Gene Expression Regulation, Developmental, Gene Silencing, Protein Transport, Erythroid Cells, GATA1 Transcription Factor, Mice, gamma-Globins, SOXD Transcription Factors
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