The DOI matches its Crossref record; 75 of the 76 references it cites were found in a registry or an index.
Mutations in the selenocysteine insertion sequence-binding protein 2 gene lead to a multisystem selenoprotein deficiency disorder in humans
Open accessAbstract
Selenium, a trace element that is fundamental to human health, is incorporated into some proteins as selenocysteine (Sec), generating a family of selenoproteins. Sec incorporation is mediated by a multiprotein complex that includes Sec insertion sequence-binding protein 2 (SECISBP2; also known as SBP2). Here, we describe subjects with compound heterozygous defects in the SECISBP2 gene. These individuals have reduced synthesis of most of the 25 known human selenoproteins, resulting in a complex phenotype. Azoospermia, with failure of the latter stages of spermatogenesis, was associated with a lack of testis-enriched selenoproteins. An axial muscular dystrophy was also present, with features similar to myopathies caused by mutations in selenoprotein N (SEPN1). Cutaneous deficiencies of antioxidant selenoenzymes, increased cellular ROS, and susceptibility to ultraviolet radiation-induced oxidative damage may mediate the observed photosensitivity. Reduced levels of selenoproteins in peripheral blood cells were associated with impaired T lymphocyte proliferation, abnormal mononuclear cell cytokine secretion, and telomere shortening. Paradoxically, raised ROS in affected subjects was associated with enhanced systemic and cellular insulin sensitivity, similar to findings in mice lacking the antioxidant selenoenzyme glutathione peroxidase 1 (GPx1). Thus, mutation of SECISBP2 is associated with a multisystem disorder with defective biosynthesis of many selenoproteins, highlighting their role in diverse biological processes.
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
“Patients with mutations in the SBP2 gene have been identified who have reduced amounts of most selenoproteins and displayed a multiple-symptom disorder [69, 70, 71, 72].”
From Ferroptosis: Death by Lipid Peroxidation (2016) · cites this paper as [71]
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
Characterization of Mammalian Selenoproteomes
Kryukov, G. V., Castellano, S., Novoselov, S. V., Lobanov, A. V., Zehtab, O., Guigó, R., & Gladyshev, V. N. (2003) · Science · doi:10.1126/science.1083516 · Cited by 2,385
Bonner, W. M., Redon, C. E., Dickey, J. S., Nakamura, A. J., Sedelnikova, O. A., Solier, S., & Pommier, Y. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2523 · Cited by 1,623
Seiler, A., Schneider, M., Förster, H., Roth, S., Wirth, E. K., Culmsee, C., Plesnila, N., Kremmer, E., Rådmark, O., Wurst, W., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.07.005 · Cited by 1,470
From Selenium to Selenoproteins: Synthesis, Identity, and Their Role in Human Health
Papp, L. V., Lu, J., Holmgren, A., & Khanna, K. K. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1528 · Cited by 1,357
Self-citationSundaresan, N. R., Gupta, M., Gene, K., Rajamohan, S. B., Isbatan, A., & Gupta, M. P. (2009) · Journal of Clinical Investigation · doi:10.1172/jci39162 · Cited by 1,006
Dual Function of the Selenoprotein PHGPx During Sperm Maturation
Ursini, F., Heim, S., Kieß, M., Maiorino, M., Roveri, A., Wissing, J. B., & Flohé, L. (1999) · Science · doi:10.1126/science.285.5432.1393 · Cited by 902
Mutations in TERT, the Gene for Telomerase Reverse Transcriptase, in Aplastic Anemia
Yamaguchi, H., Calado, R. T., Ly, H., Kajigaya, S., Baerlocher, G. M., Chanock, S. J., Lansdorp, P. M., & Young, N. S. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa042980 · Cited by 723
Berry, M. J., Banu, L., Chen, Y., Mandel, S. J., Kieffer, J. D., Harney, J. W., & Larsen, P. R. (1991) · Nature · doi:10.1038/353273a0 · Cited by 652
Reactive oxygen species enhance insulin sensitivity
Loh, K., Deng, H., Fukushima, A., Cai, X., Boivin, B., Galic, S., Bruce, C., Shields, B. J., Skiba, B., Ooms, L. M., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.08.009 · Cited by 581
Self-citationProtection against reactive oxygen species by selenoproteins
Steinbrenner, H., & Sies, H. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.02.014 · Cited by 522
Research works printed but not linked: 2
- Sundaresan, 2009, J Clin Invest., 119, 2758
- McFadden, 2001, Noise and Health., 3, 49
Cited by
Sorted by citations
Items 201–300 of 315
Cockman, E., Narayan, V., Willard, B. B., Shetty, S. P., Copeland, P. R., & Driscoll, D. M. (2019) · RNA Biology · doi:10.1080/15476286.2019.1653681 · Cited by 10
Liu, A., Li, F., Xu, P., Chen, Y., Liang, X., Zheng, S., Meng, H., Zhu, Y., Mo, J., Gong, C., et al. (2022) · Biological Trace Element Research · doi:10.1007/s12011-022-03118-5 · Cited by 10
Thyroid Hormones and Co-workers: An Overview
Contreras-Jurado, C. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-4252-8_1 · Cited by 11
Syndromic male subfertility: A network view of genome–phenome associations
Mikec, Š., Kolenc, Ž., Peterlin, B., Horvat, S., Pogorevc, N., & Kunej, T. (2022) · Andrology · doi:10.1111/andr.13167 · Cited by 9
Gurnell, M., Visser, T. J., Beck‐Peccoz, P., & Chatterjee, K. (2015) · Elsevier eBooks · doi:10.1016/b978-0-323-18907-1.00095-0 · Cited by 9
Self-citationMel'nichenko, G. A., & Rybakova, A. A. (2018) · Clinical and experimental thyroidology · doi:10.14341/ket9671 · Cited by 8
Disorders of the Thyroid in the Newborn and Infant
Deladoëy, J., Oettingen, J. E. V., & Vliet, G. V. (2021) · Elsevier eBooks · doi:10.1016/b978-0-323-62520-3.00008-7 · Cited by 8
Selenium and Male Reproduction
Turanov, A. A., Malinouski, M., & Gladyshev, V. N. (2011) · Springer eBooks · doi:10.1007/978-1-4614-1025-6_32 · Cited by 8
Mouse Models that Target Individual Selenoproteins
Conrad, M., & Schweizer, U. (2016) · Springer eBooks · doi:10.1007/978-3-319-41283-2_47 · Cited by 8
EEFSEC deficiency: A selenopathy with early-onset neurodegeneration
Laugwitz, L., Buchert, R., Olguı́n, P., Estiar, M. A., Atanasova, M., Marques, W., Enssle, J., Marsden, B. G., Avilés, J., González‐Gutiérrez, A., et al. (2025) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2024.12.001 · Cited by 7
Mutations in Humans That Adversely Affect the Selenoprotein Synthesis Pathway
Schoenmakers, E., Schoenmakers, N. A., & Chatterjee, K. (2016) · Springer eBooks · doi:10.1007/978-3-319-41283-2_44 · Cited by 7
Self-citationZhou, J., Zhou, J., Su, L., Huang, K., & Lei, X. G. (2018) · Molecular and integrative toxicology · doi:10.1007/978-3-319-95390-8_17 · Cited by 7
HIF-1 Has a Central Role in Caenorhabditis elegans Organismal Response to Selenium
Romanelli-Cedrez, L., Doitsidou, M., Alkema, M. J., & Salinas, G. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00063 · Cited by 7
Selenoproteins in Nervous System Development, Function and Degeneration
Schweizer, U. (2016) · Springer eBooks · doi:10.1007/978-3-319-41283-2_36 · Cited by 7
Interpreting Minor Variations in Thyroid Function or Echostructure
Vliet, G. V., & Deladoëy, J. (2015) · Pediatric Clinics of North America · doi:10.1016/j.pcl.2015.04.008 · Cited by 7
N’Guessan, M. F., Sery, B. B., Bi, F. J. V., Ekissi, N. A., Djohan, Y. F., Coulibaly, F. A., & Djaman, A. J. (2023) · Advances in Reproductive Sciences · doi:10.4236/arsci.2023.114011 · Cited by 6
Simon‐Szabó, L., Lizák, B., Sturm, G., Somogyi, A., Takács, I., & Németh, Z. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25169113 · Cited by 8
Selenium Status in Paediatric Patients with Neurodevelopmental Diseases
Görlich, C. L., Sun, Q., Roggenkamp, V., Hackler, J., Mehl, S. R., Minich, W. B., Kaindl, A. M., & Schomburg, L. (2022) · Nutrients · doi:10.3390/nu14122375 · Cited by 6
Role of the Thyroid Gland in Expression of the Thyroid Phenotype of Sbp2-Deficient Mice
Fujisawa, H., Korwutthikulrangsri, M., Fu, J., Liao, X.-H., & Dumitrescu, A. M. (2019) · Endocrinology · doi:10.1210/endocr/bqz032 · Cited by 6
Syndromes of Impaired Sensitivity to Thyroid Hormone
Weiss, R. E., Dumitrescu, A. M., & Refetoff, S. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800892-8.00009-9 · Cited by 6
Novel Missense Variants in PAX8 and NKX2-1 Cause Congenital Hypothyroidism
Li, M., Li, Z., Chen, M., Hu, Z., Zhou, M., Wu, L., Zhang, C., & Liang, D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24010786 · Cited by 5
Uncovering the Importance of Selenium in Muscle Disease
Lescure, A., Baltzinger, M., & Zito, E. (2018) · Molecular and integrative toxicology · doi:10.1007/978-3-319-95390-8_18 · Cited by 5
Nonneoplastic Diseases of the Testis
Nistal, M., Paniagua, R., & González‐Peramato, P. (2020) · Elsevier eBooks · doi:10.1016/b978-0-323-54941-7.00012-8 · Cited by 5
Disorders in the Transport of Copper, Iron, Magnesium, Manganese, Selenium and Zinc
van Hasselt, P. M., Clayton, P. T., & Houwen, R. H. J. (2016) · Springer eBooks · doi:10.1007/978-3-662-49771-5_37 · Cited by 5
Iron and Selenium: At the Crossroads of Development and Death in Oligodendrocytes
Ma, C., Wurlitzer, K., Nunes, L. G. A., Hoffmann, P. R., & Pitts, M. W. (2025) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2025.110509 · Cited by 5
Schweizer, U., & Fabiano, M. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104083 · Cited by 7
Congenital (Structural) Myopathies
Jungbluth, H., & Wallgren‐Pettersson, C. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.05599-9 · Cited by 4
Qi, Y., Wu, Y., Pang, K., Cao, Y., Li, H., Yu, Q., Yuan, D., Liu, X., Li, Z., Hu, F., et al. (2024) · Biology of Reproduction · doi:10.1093/biolre/ioae130 · Cited by 4
Selenium Transport in Mammals: Selenoprotein P and Its Receptors
Köhrle, J., Schweizer, U., & Schomburg, L. (2011) · Springer eBooks · doi:10.1007/978-1-4614-1025-6_16 · Cited by 4
Resistance to Thyroid Hormone (RTH) and Resistance to TSH (RTSH)
Dumitrescu, A. M., & Cohen, R. (2018) · Springer eBooks · doi:10.1007/978-3-319-73782-9_20 · Cited by 4
Thyroid Dysfunction and COVID-19: The Emerging Role of Selenium in This Intermingled Relationship
Gorini, F., Sabatino, L., Coi, A., Iervasi, G., & Vassalle, C. (2022) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph19116912 · Cited by 4
Disorders in the Transport of Copper, Iron, Magnesium, Manganese, Selenium and Zinc
Bierings, M., Clayton, P. T., & Houwen, R. H. J. (2011) · Springer eBooks · doi:10.1007/978-3-642-15720-2_38 · Cited by 4
Polak, M., & Szinnai, G. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-383834-6.00088-4 · Cited by 4
Sárközy, A., Bushby, K. M. D., & Mercuri, E. M. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-383834-6.00134-8 · Cited by 4
Syndromes of Resistance to Thyroid Hormone Action
Persani, L., Campi, I., & Marelli, F. (2015) · Springer eBooks · doi:10.1007/978-3-319-19213-0_10 · Cited by 4
Self-citationEffects of molecular interactions between the exposome and oxylipin metabolism on healthspan
Hinman, J., Alan, J. K., & Lee, K. S. S. (2025) · Frontiers in Physiology · doi:10.3389/fphys.2025.1584195 · Cited by 3
Persani, L., & Campi, I. (2021) · Springer eBooks · doi:10.1007/978-3-030-62011-0_20 · Cited by 3
Self-citationSelenoprotein N: Its Role in Disease
Lescure, A., Castets, P., Grunwald, D. J., Allamand, V., & Howard, M. T. (2011) · Springer eBooks · doi:10.1007/978-1-4614-1025-6_22 · Cited by 3
Self-citationWhat Do We Know About Selenium Contributions to Muscle Physiology?
Lescure, A., Briens, M., & Ferreiro, A. (2016) · Springer eBooks · doi:10.1007/978-3-319-41283-2_40 · Cited by 3
Selenoproteins and Epigenetic Regulation in Mammals
Lu, H.-Y., Somuncu, B., Zhu, J., Müftüoğlu, M., & Cheng, W.-H. (2019) · Springer eBooks · doi:10.1007/978-3-319-55530-0_31 · Cited by 3
Mineral-enriched yeast biomass: A promising mineral food and feed supplement
Meena, K., Sharma, V., Manzoor, M., Aseri, G. K., Sohal, J. S., Singh, D., Khare, N., & Sharma, D. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-821007-9.00013-9 · Cited by 5
Loss of Mfn1 but not Mfn2 enhances adipogenesis
Mann, J. P., Tábara, L. C., Patel, S., Pushpa, P., Álvarez-Guaita, A., Dong, L., Haider, A., Lim, K., Tandon, P., Scurria, F., et al. (2024) · PLoS ONE · doi:10.1371/journal.pone.0306243 · Cited by 5
Self-citationGharipour, M., Sadeghi, M., Behmanesh, M., Salehi, M., Roohafza, H., Nezafati, P., Khosravi, E., Hosseini, M., Keshvari, M., Rouhi-Bourojeni, H., et al. (2019) · Acta bio-medica dell'Ateneo parmense/Acta biomedica · doi:10.23750/abm.v90i1.6167 · Cited by 3
Oxidative Stress: Impact in Neuroscience Research
Sies, H. (2013) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-1-62703-598-9_1 · Cited by 3
Zavacki, A. M., Marsili, A., & Larsen, P. R. (2011) · Springer eBooks · doi:10.1007/978-1-4614-1025-6_29 · Cited by 3
Tissue-Specific Regulation of Thyroid Status by Selenodeiodinases
Marsili, A., Larsen, P. R., & Zavacki, A. M. (2016) · Springer eBooks · doi:10.1007/978-3-319-41283-2_41 · Cited by 3
Dissertation zur Erlangung des Doktorgrades der Fakultät für Biologie
München, L.-M.-U. (2013) · Cited by 3
Peters, C. J., & Schoenmakers, N. A. (2019) · Wiley eBooks · doi:10.1002/9781119152712.ch8 · Cited by 3
Self-citationLiu, Z., He, M., Luo, X., Pan, H., Hu, J., Wan, Z., Peng, Y., Luo, Y., Wang, H., & Mao, X. O. (2025) · Journal of Neurodevelopmental Disorders · doi:10.1186/s11689-025-09632-6 · Cited by 2
Body Selenium Status and Diabetes and Complications: The Multiphased Effect of Selenium
Liang, X., Li, L., Lü, H., Li, Y., Zhang, Q., & Liu, L. (2025) · Journal of Nutrition · doi:10.1016/j.tjnut.2025.11.001 · Cited by 2
Selenoproteins in Nervous System Development, Function, and Degeneration
Schweizer, U. (2011) · Springer eBooks · doi:10.1007/978-1-4614-1025-6_18 · Cited by 2
Thyroid Hormone and the Mammalian Auditory System
Forrest, D., & Ng, L. (2016) · Springer handbook of auditory research · doi:10.1007/978-3-319-26597-1_7 · Cited by 2
Thyroid Hormone in Bone and Joint Disorders
Bassett, J. H. D., & Williams, G. R. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-804182-6.00031-9 · Cited by 2
Fradejas‐Villar, N., & Schweizer, U. (2018) · Molecular and integrative toxicology · doi:10.1007/978-3-319-95390-8_9 · Cited by 3
Chellan, B., Zhao, L., Landeche, M., Carmean, C. M., Dumitrescu, A., & Sargis, R. M. (2020) · Scientific Reports · doi:10.1038/s41598-020-75595-4 · Cited by 2
Congenital (Structural) Myopathies
Jungbluth, H., & Wallgren‐Pettersson, C. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-383834-6.00136-1 · Cited by 2
Speckmann, B., Klotz, L., & Steinbrenner, H. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805377-5.00017-5 · Cited by 2
Resistance to Thyroid Hormone and TSH Receptor Mutations
Cohen, R. (2013) · Humana Press eBooks · doi:10.1007/978-1-60761-395-4_18 · Cited by 2
Pitfalls in the measurement and interpretation of thyroid function tests
Gurnell, M. (2014) · Endocrine Abstracts · doi:10.1530/endoabs.35.s26.2 · Cited by 2
Self-citationBiosynthesis, Transport, Metabolism, and Actions of Thyroid Hormones
Visser, W. E. (2022) · doi:10.1093/med/9780198870197.003.0039 · Cited by 2
Loss of Mfn1 but not Mfn2 enhances adipogenesisPreprint
Mann, J. P., Tábara, L. C., Álvarez-Guaita, A., Dong, L., Haider, A., Lim, K., Tandon, P., Minchin, J., O’Rahilly, S., Patel, S., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.04.515167 · Cited by 2
Self-citationBirk, O. S. (2011) · Future Neurology · doi:10.2217/fnl.11.2 · Cited by 1
Hartwig, A., Köberle, B., & Michalke, B. (2013) · Repository KITopen (Karlsruhe Institute of Technology) · doi:10.5445/ksp/1000036003 · Cited by 4
Hypothyroidism: diagnosis and screening, genetic influences, and treatment options
Torres-Manzo, A. P., Cano-Europa, E., Blas-Valdivia, V., Franco-Colín, M., & Ortiz-Butrón, R. (2014) · Clinical and Experimental Medical Sciences · doi:10.12988/cems.2014.3129 · Cited by 1
Mutations in human genes that increase the risk for severe influenza infection
Киселев, О. И., Komissarov, A. B., Коншина, О. С., Dmitrieva, M. N., Германовна, Д. Э., Tv, S., & Pokrovskiy, V. I. (2015) · Microbiology Independent Research Journal (MIR Journal) · doi:10.18527/2500-2236-2015-2-1-10-18 · Cited by 1
Мутации в генах человека, повышающие риск тяжелого течения гриппозной инфекции
Киселев, О. И., Komissarov, A. B., Коншина, О. С., Dmitrieva, M. N., Германовна, Д. Э., Tv, S., & Покровский, В. И. (2015) · Microbiology Independent Research Journal (MIR Journal) · doi:10.18527/2500-2236-2015-2-1-1-9 · Cited by 1
Disorders of Thyroid Hormone Transporters and Receptors
Visser, W. E. (2019) · Springer eBooks · doi:10.1007/978-3-319-72102-6_4 · Cited by 1
Angeborene Schilddrüsenerkrankungen bei Neugeborenen und Kleinkindern
Krude, H., & Grüters‐Kieslich, A. (2019) · Springer Reference Medizin · doi:10.1007/978-3-662-57309-9_31 · Cited by 1
50 years of the ETA: “the selenium connection”
Smyth, P. P. A., & Duntas, L. H. (2019) · HORMONES · doi:10.1007/s42000-019-00117-5 · Cited by 1
La resistenza e le altre sindromi da ridotta sensibilità agli ormoni tiroidei
Cosmo, C. D. (2022) · L Endocrinologo · doi:10.1007/s40619-021-01008-x · Cited by 1
Bohleber, S., Fradejas‐Villar, N., Zhao, W., Reuter, U., & Schweizer, U. (2022) · Biomolecules · doi:10.3390/biom12101504 · Cited by 1
Overview of Thyroid Disease in Children and Adolescents
Zwaveling‐Soonawala, N., & van Trotsenburg, A. S. P. (2023) · Endocrinology · doi:10.1007/978-3-030-18901-3_3-1 · Cited by 1
Miyoshi myopathy associated with spine rigidity and multiple contractures: a case report
Bardakov, S. N., Андреевна, Т. А., Nikitin, S. S., Nikitins, V., Sokolova, M. O., Tsargush, V. A., Yuhno, E. A., Vetrovoj, O. V., Carlier, P. G., Sofronova, Y. V., et al. (2024) · BMC Musculoskeletal Disorders · doi:10.1186/s12891-024-07270-y · Cited by 1
Stoupa, A., Carré, A., Polak, M., & Szinnai, G. (2024) · Elsevier eBooks · doi:10.1016/b978-0-12-812531-1.00013-0 · Cited by 1
Almohammadi, L., Alsayel, L. T., Aljumaa, M., Alhuthil, R. T., & Alsagheir, A. (2025) · Frontiers in Pediatrics · doi:10.3389/fped.2025.1637116 · Cited by 1
Functional Genomics of Selenoproteins and Se-responsive Pathways
Méplan, C., & Hesketh, J. E. (2016) · Springer eBooks · doi:10.1007/978-3-319-41283-2_13 · Cited by 1
Selenoproteins and Epigenetic Regulation in Mammals
Lu, H., Somuncu, B., Zhu, J., Müftüoğlu, M., & Cheng, W. (2017) · Springer eBooks · doi:10.1007/978-3-319-31143-2_31-1 · Cited by 1
Disorders in the Transport of Copper, Iron, Magnesium, Manganese, Selenium and Zinc
van Hasselt, P. M., Clayton, P. T., & Houwen, R. H. J. (2022) · Springer eBooks · doi:10.1007/978-3-662-63123-2_34 · Cited by 1
Functional Aspects of the Genomics of Selenoproteins and Selenocysteine Incorporation Machinery
Méplan, C., & Hesketh, J. E. (2011) · Springer eBooks · doi:10.1007/978-1-4614-1025-6_40 · Cited by 1
Gradual repression of selenoprotein W ensures physiological bone remodellingPreprint
Kim, H., Lee, K. H., Kim, J., Kim, J.-R., Lee, H., Chung, Y. W., Shin, H., Park, E., Rho, J., Lee, S. H., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/254433 · Cited by 1
Tanda, M. L., & Ippolito, S. (2022) · Encyclopedia of pathology · doi:10.1007/978-3-030-62345-6_5290 · Cited by 1
Steinbrenner, H. (2014) · OpenEdition (OpenEdition)
Supplementieren oder nicht? Das Spurenelement Selen
Schweizer, U., Köhrle, J., & Schweizer, S. (2013) · Perspectives in Medicine · doi:10.1016/j.permed.2013.11.001
Perspectives in Pediatric Pathology, Chapter 21. Testicular Pathology in Heritable Metabolic Disease
Nistal, M., Paniagua, R., González‐Peramato, P., & Reyes‐Múgica, M. (2014) · Pediatric and Developmental Pathology · doi:10.2350/14-06-1519-pb.1
SECIS-Binding Proteins Regulate the Expression of the Selenoproteome
Driscoll, D. M., & Bubenik, J. L. (2011) · Springer eBooks · doi:10.1007/978-1-4614-1025-6_4
The Post-Transcriptional Regulation of Antioxidant Enzymes
Reinke, E. N. (2013) · Figshare
Syndromes of Resistance to Thyroid Hormone and Brain Development
Campi, I., & Beck‐Peccoz, P. (2016) · Contemporary clinical neuroscience · doi:10.1007/978-1-4939-3737-0_12
Self-citationIMPAIRED SENSITIVITY TO THYROID HORMONE: Defects of Transport,
Dumitrescu, A. M., & Refetoff, S. (2015)
De Novo Interstitial Deletion of 9q in a Pediatric Patient With Global Developmental Delay
Keselman, D. J., Singh, R. J., Cohen, N., & Fefer, Z. (2019) · Child Neurology Open · doi:10.1177/2329048x19844920
Bhattacharyya, R., Mandal, S. K., Mallick, B. N., Bhattacharyya, S., Ray, U., & Bhattacharyya, J. (2016) · Bengal Journal of Psychiatry · doi:10.51332/bjp.2016.v21.i1.32
Thyroid hormone, thyroid medication, and the skeleton
Freudenthal, B., Watts, L., Bassett, J. H. D., & Williams, G. R. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-813073-5.00046-0
Tanda, M. L., & Ippolito, S. (2021) · Encyclopedia of pathology · doi:10.1007/978-3-319-28845-1_5290-1
Syndromes of Resistance to Thyroid Hormone
Moran, C., Gurnell, M., & Chatterjee, K. (2022) · doi:10.1093/med/9780198870197.003.0071
Self-citation(2011) · Current Opinion in Pediatrics · doi:10.1097/mop.0b013e3283496fc1
Angeborene Schilddrüsenerkrankungen bei Neugeborenen und Kleinkindern
Krude, H., & Grüters‐Kieslich, A. (2018) · Springer Reference Medizin · doi:10.1007/978-3-662-52794-8_31-1
Samaranayake, G. J., Troccoli, C. I., Zhang, L., Huynh, M., Jayaraj, C. J., Ji, D., McPherson, L. A., Onishi, Y., Nguyen, D. M., Robbins, D. J., et al. (2023) · doi:10.1158/1535-7163.c.6538503.v1
Self-citationRole of selenium and selenoprotein in animal liver health
Hui, Z. H. O. U., YiWen, H. E., Yin, Y., TieJun, L. I., & He, L. (2024) · Scientia Sinica Vitae · doi:10.1360/ssv-2024-0107
Metadata
- Authors
- Schoenmakers, E., Agostini, M., Mitchell, C., Schoenmakers, N., Papp, L., Rajanayagam, O., Padidela, R., Ceron-Gutierrez, L., Doffinger, R., Prevosto, C., Luan, J., Montano, S., Lu, J., Castanet, M., Clemons, N., Groeneveld, M., Castets, P., Karbaschi, M., Aitken, S., Dixon, A., Williams, J., Campi, I., Blount, M., Burton, H., Muntoni, F., O’Donovan, D., Dean, A., Warren, A., Brierley, C., Baguley, D., Guicheney, P., Fitzgerald, R., Coles, A., Gaston, H., Todd, P., Holmgren, A., Khanna, K. K., Cooke, M., Semple, R., Halsall, D., Wareham, N., Schwabe, J., Grasso, L., Beck-Peccoz, P., Ogunko, A., Dattani, M., Gurnell, M., & Chatterjee, K.
- Affiliations
- University of Cambridge (GB)
- QIMR Berghofer Medical Research Institute (AU)
- Great Ormond Street Hospital (GB)
- MRC Epidemiology Unit (GB)
- Karolinska Institutet (SE)
- Inserm (FR)
- University of Leicester (GB)
- University of Pisa (IT)
- Darent Valley Hospital (GB)
- ORCID
- Schoenmakers, Erik
- Agostini, Maura
- Schoenmakers, Nadia
- Padidela, Raja
- Luan, Jian’an
- Lu, Jun
- Castanet, Mireille
- Groeneveld, Matthijs
- Castets, Perrine
- Campi, Irene
- Brierley, Charlotte
- Baguley, David
- Guicheney, Pascale
- Fitzgerald, Rebecca
- Coles, Alasdair
- Gaston, Hill
- Holmgren, Arne
- Khanna, Kum Kum
- Cooke, Marcus
- Semple, Robert
- Halsall, David
- Wareham, Nicholas
- Schwabe, John
- Dattani, Mehul
- Gurnell, Mark
- Chatterjee, Krishna
- Venue
- Journal of Clinical Investigation
- Published
- 2010-12-01
- Volume
- 120
- Issue
- 12
- Pages
- 4220-4235
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC2993594
- OpenAlex
- W2123186374
- Cited by
- 315
- References
- 76
- Citations by year
- 2026: 8 · 2025: 10 · 2024: 18 · 2023: 11 · 2022: 24 · 2021: 17 · 2020: 23 · 2019: 23 · 2018: 23 · 2017: 18 · 2016: 24 · 2015: 22 · 2014: 21 · 2013: 27 · 2012: 19
- FWCI
- 21.33
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- QUT ePrints (Queensland University of Technology) (submittedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- CINECA IRIS Institutial research information system (University of Pisa) (submittedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Leicester Research Archive (University of Leicester) (submittedVersion)
- University of Birmingham Research Portal (University of Birmingham) (submittedVersion, other-oa)
- Funders
- Wellcome Trust
- National Institute for Health and Care Research
- Muscular Dystrophy UK
- Medical Research Council
- NIHR Cambridge Biomedical Research Centre
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
- Physical Sciences › Chemistry › Organic Chemistry › Organoselenium and organotellurium chemistry
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genomics and Rare Diseases
- Keywords
- selenocysteine incorporation, selenoproteins, compound heterozygosity, azoospermia, spermatogenesis, muscular dystrophy, SEPN1, photosensitivity, reactive oxygen species, T cell proliferation, cytokine production, telomere shortening, insulin sensitivity, glutathione peroxidase 1, multisystem disease
- MeSH terms
- Adult, Aged, Amino Acid Sequence, Animals, Base Sequence, Child, Child, Preschool, DNA, Female, Hearing Loss, Sensorineural, Humans, Insulin Resistance, Male, Middle Aged, Models, Molecular, Molecular Sequence Data, Muscular Dystrophies, Mutation, Pedigree, Photosensitivity Disorders, Spermatogenesis, T-Lymphocytes, RNA-Binding Proteins, Selenocysteine, Reactive Oxygen Species, Sequence Homology, Amino Acid, Codon, Nonsense, Mutation, Missense, Selenoproteins, Mice, Azoospermia
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
