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
Flagged first, then by citations
1 of the 76 references couldn’t be matched to a known paper.
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 101–200 of 315
Delaying of insulin signal transduction in skeletal muscle cells by selenium compounds
Pinto, A., Speckmann, B., Heisler, M., Sies, H., & Steinbrenner, H. (2011) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2011.03.010 · Cited by 48
Selenium and Selenoproteins in Immune Mediated Thyroid Disorders
Santos, L. R., Neves, C., Melo, M., & Soares, P. (2018) · Diagnostics · doi:10.3390/diagnostics8040070 · Cited by 51
Norton, R. L., & Hoffmann, P. R. (2011) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.10.003 · Cited by 48
Spanidis, Y., Mpesios, A., Stagos, D., Goutzourelas, N., Bar‐Or, D., Karapetsa, M., Zakynthinos, E. G., Spandidos, D. A., Tsatsakis, A. M., Leon, G., et al. (2016) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2016.2968 · Cited by 48
Association of dietary selenium intake with telomere length in middle-aged and older adults
Shu, Y., Wu, M., Yang, S., Wang, Y., & Li, H. (2020) · Clinical Nutrition · doi:10.1016/j.clnu.2020.01.014 · Cited by 49
Consequences of mutations and inborn errors of selenoprotein biosynthesis and functions
Fradejas‐Villar, N. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.04.572 · Cited by 47
Cavedon, E., Manso, J., Negro, I., Censi, S., Serra, R., Busetto, L., Vettor, R., Plebani, M., Pezzani, R., Nacamulli, D., et al. (2020) · International Journal of Endocrinology · doi:10.1155/2020/4802739 · Cited by 46
Speckmann, B., Gerloff, K., Simms, L. A., Oancea, I., Shi, W., McGuckin, M. A., Radford‐Smith, G. L., & Khanna, K. K. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.11.001 · Cited by 48
Self-citationNg, L., Cordas, E., Wu, X., Vella, K. R., Hollenberg, A. N., & Forrest, D. (2015) · Endocrinology · doi:10.1210/en.2015-1468 · Cited by 44
Cao, L., Zhang, L., Zeng, H., Wu, R. T. Y., Wu, T.-L., & Cheng, W. (2017) · Journal of Nutrition · doi:10.3945/jn.117.247775 · Cited by 44
Genetic Disorders Associated with Metal Metabolism
Umair, M., & Alfadhel, M. (2019) · Cells · doi:10.3390/cells8121598 · Cited by 44
The hsa-miR-181a-5p reduces oxidation resistance by controlling SECISBP2 in osteoarthritis
Xue, J., Min, Z., Xia, Z., Cheng, B., Lan, B.-S., Zhang, F., Han, Y., Wang, K.-Z., & Sun, J. (2018) · BMC Musculoskeletal Disorders · doi:10.1186/s12891-018-2273-6 · Cited by 40
Hoffmann, B. R., El‐Mansy, M. F., Sem, D. S., & Greene, A. S. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm301204r · Cited by 41
Inherited defects in thyroid hormone cell-membrane transport and metabolism
Fu, J., & Dumitrescu, A. M. (2013) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2013.05.014 · Cited by 41
The Neurobiology of Selenium: Looking Back and to the Future
Schweizer, U., Bohleber, S., Zhao, W., & Fradejas‐Villar, N. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.652099 · Cited by 41
Expanding the Frontiers of Guardian Antioxidant Selenoproteins in Cardiovascular Pathophysiology
Angelone, T., Rocca, C., Lionetti, V., Penna, C. R. R., & Pagliaro, P. (2024) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0285 · Cited by 40
ROS, thiols and thiol-regulating systems in male gametogenesis
Conrad, M., Ingold, I., Buday, K., Kobayashi, S., & Angeli, J. P. F. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.10.020 · Cited by 39
Saito, Y., Shichiri, M., Hamajima, T., Ishida, N., Mita, Y., Nakao, S., Hagihara, Y., Yoshida, Y., Takahashi, K., Niki, E., et al. (2015) · Journal of Lipid Research · doi:10.1194/jlr.m059105 · Cited by 38
Wu, R. T., Cao, L., Mattson, E., Witwer, K. W., Cao, J., Zeng, H., He, X., Combs, G. F., & Cheng, W. (2017) · Aging Cell · doi:10.1111/acel.12529 · Cited by 37
T cell senescence: a new perspective on immunotherapy in lung cancer
Huang, M., Wang, Y., Fang, L., Liu, C., Feng, F., Liu, L., & Sun, C. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1338680 · Cited by 37
Different causes of Reduced Sensitivity to Thyroid Hormone: Diagnosis and Clinical management
Visser, W. E., van Mullem, A. A., Visser, T. J., & Peeters, R. P. (2013) · Clinical Endocrinology · doi:10.1111/cen.12281 · Cited by 37
Schoenmakers, E., & Chatterjee, K. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8097 · Cited by 35
Self-citationHesketh, J. E., & Méplan, C. (2011) · Proceedings of The Nutrition Society · doi:10.1017/s0029665111000115 · Cited by 34
Genome-wide mapping of genomic DNA damage: methods and implications
Amente, S., Scala, G., Majello, B., Azmoun, S., Tempest, H. G., Premi, S., & Cooke, M. S. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03923-6 · Cited by 33
Self-citationDias, C., Sincan, M., Cherukuri, P. F., Rupps, R., Huang, Y., Briemberg, H., Selby, K. A., Mullikin, J. C., Markello, T. C., Adams, D. R., et al. (2012) · Human Mutation · doi:10.1002/humu.22032 · Cited by 35
Tao, Z.-S., Li, T., Yang, M., & Xu, H. (2022) · Calcified Tissue International · doi:10.1007/s00223-021-00936-y · Cited by 33
Syndromes of Resistance to Thyroid Hormone Action
Persani, L., & Campi, I. (2019) · Experientia supplementum · doi:10.1007/978-3-030-25905-1_5 · Cited by 31
Self-citationHuman Genetic Disorders Resulting in Systemic Selenoprotein Deficiency
Schoenmakers, E., & Chatterjee, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312927 · Cited by 30
Self-citationMutational Landscape of Resistance to Thyroid Hormone Beta (RTHβ)
Concolino, P., Costella, A., & Paragliola, R. M. (2019) · Molecular Diagnosis & Therapy · doi:10.1007/s40291-019-00399-w · Cited by 33
Clinical and laboratory aspects of 3,3′,5′-triiodothyronine (reverse T3)
Halsall, D. J., & Oddy, S. (2021) · Annals of Clinical Biochemistry: International Journal of Laboratory Medicine · doi:10.1177/0004563220969150 · Cited by 28
Self-citationSBP2 deficiency in adipose tissue macrophages drives insulin resistance in obesity
Wang, N., Tan, H., Li, S., Wang, D., Xu, Y., Zhang, C., Xia, W., Che, C., & Feng, Y. (2019) · Science Advances · doi:10.1126/sciadv.aav0198 · Cited by 28
Karunasinghe, N., Han, D. Y., Zhu, S., Duan, H., Ko, Y.-J., Yu, J.-F., Triggs, C. M., & Ferguson, L. R. (2013) · Nutrition and Cancer · doi:10.1080/01635581.2013.760743 · Cited by 28
Selenoprotein deficiency disorder predisposes to aortic aneurysm formation
Schoenmakers, E., Marelli, F., Jørgensen, H. F., Visser, W. E., Moran, C., Groeneweg, S., Avalos, C., Jurgens, S. J., Figg, N. L., Finigan, A. J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-43851-6 · Cited by 28
Self-citationCharacterization of the UGA-recoding and SECIS-binding activities of SECIS-binding protein 2
Bubenik, J. L., Miniard, A. C., & Driscoll, D. M. (2014) · RNA Biology · doi:10.1080/15476286.2014.996472 · Cited by 27
Thyroid hormone resistance: mechanisms and therapeutic development
Yao, B., Yang, C., Pan, C., & Li, Y. (2022) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2022.111679 · Cited by 26
Nutrigenetics, Nutrigenomics, and Selenium
Ferguson, L. R., & Karunasinghe, N. (2011) · Frontiers in Genetics · doi:10.3389/fgene.2011.00015 · Cited by 26
Inherited defects of thyroid hormone metabolism
Dumitrescu, A. M., & Refetoff, S. (2011) · Annales d Endocrinologie · doi:10.1016/j.ando.2011.03.011 · Cited by 26
Çatlı, G., Fujisawa, H., Kırbıyık, Ö., Mimoto, M. S., Gençpınar, P., Özdemir, T. R., Dündar, B. N., & Dumitrescu, A. M. (2018) · Thyroid · doi:10.1089/thy.2018.0015 · Cited by 26
Treatment of congenital thyroid dysfunction: Achievements and challenges
Krude, H., Kühnen, P., & Biebermann, H. (2015) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2015.04.004 · Cited by 25
Liewluck, T., Milone, M., Xia, T., Engel, A. G., Staff, N. P., & Wong, L.-J. C. (2016) · Muscle & Nerve · doi:10.1002/mus.25054 · Cited by 25
Impaired Sensitivity to Thyroid Hormone: Defects of Transport, Metabolism and Action
Dumitrescu, A. M., & Refetoff, S. (2015) · Cited by 24
Selenoprotein P and Selenium Distribution in Mammals
Schweizer, U., Schomburg, L., & Köhrle, J. (2016) · Springer eBooks · doi:10.1007/978-3-319-41283-2_22 · Cited by 25
Ghezzi, P., & Mooradian, A. D. (2020) · Handbook of experimental pharmacology · doi:10.1007/164_2020_379 · Cited by 25
Khurana, A., Allawadhi, P., Singh, V., Khurana, I., Yadav, P., Sathua, K. B., Allwadhi, S., Banothu, A. K., Navik, U., & Bharani, K. K. (2023) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2023.104663 · Cited by 23
The genomics of selenium: Its past, present and future
Davy, T., & Castellano, S. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.05.020 · Cited by 23
Maintenance of SOX9 stability and ECM homeostasis by selenium-sensitive PRMT5 in cartilage
Sun, M., Hussain, S., Hu, Y., Yan, J., Min, Z., Lan, X., Guo, Y., Zhao, Y., Huang, H. Y., Feng, M., et al. (2019) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2019.02.797 · Cited by 23
Budachetri, K., Crispell, G., & Karim, S. (2017) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2017.07.006 · Cited by 22
Burke, S. L., Cobb, J., Agarwal, R., Maddux, M., & Cooke, M. S. (2020) · Journal of Autism and Developmental Disorders · doi:10.1007/s10803-020-04611-3 · Cited by 22
Self-citationProoxidative toxicity and selenoprotein suppression by cerivastatin in muscle cells
Fuhrmeister, J., Tews, M., Kromer, A., & Moosmann, B. (2012) · Toxicology Letters · doi:10.1016/j.toxlet.2012.10.010 · Cited by 21
Li, M., Cheng, W., Luo, J., Hu, X., Nie, T., Lai, H., Zheng, X., Li, F., & Li, H. (2017) · Placenta · doi:10.1016/j.placenta.2017.05.007 · Cited by 22
Thyroid Hormone Metabolism Defects in a Mouse Model of SBP2 Deficiency
Fu, J., Fujisawa, H., Follman, B., Liao, X.-H., & Dumitrescu, A. M. (2017) · Endocrinology · doi:10.1210/en.2017-00618 · Cited by 22
Hofstee, P., Cuffe, J. S. M., & Perkins, A. V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21062210 · Cited by 22
Regulation of Thyroid Function, Synthesis, and Function of Thyroid Hormones
Visser, T. J. (2018) · Endocrinology · doi:10.1007/978-3-319-45013-1_1 · Cited by 22
Yamato, M., Nagahama, K., Kotani, T., Kato, S., & Takeuchi, K. (2005) · Digestion · doi:10.1159/000088365 · Cited by 22
Ciorba, A., Corazzi, V., Bianchini, C., Aimoni, C., Skarżyńśki, H., Skarzynski, P. H., & Stavros Hatzopoulos, A. (2016) · International Journal of Immunopathology and Pharmacology · doi:10.1177/0394632016673845 · Cited by 22
Huang, Y., Wu, T.-L., Zeng, H., & Cheng, W. (2021) · Journal of Nutrition · doi:10.1093/jn/nxab053 · Cited by 21
Selenium status and type 2 diabetes risk
Huang, Y., Combs, G. F., Wu, T.-L., Zeng, H., & Cheng, W. (2022) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2022.109400 · Cited by 21
Yan, J., Tian, J., Zheng, Y., Han, Y., & Lu, S. (2012) · Cell Biochemistry and Function · doi:10.1002/cbf.2845 · Cited by 21
Qiao, L., Yang, G., Deng, T., Chang, J., Dou, X., Song, X., Zeng, X., Ren, L., & Xu, C. (2025) · Journal of Advanced Research · doi:10.1016/j.jare.2025.04.023 · Cited by 21
Fradejas‐Villar, N., Zhao, W., Reuter, U., Doengi, M., Ingold, I., Bohleber, S., Conrad, M., & Schweizer, U. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102188 · Cited by 21
Simonović, M., & Puppala, A. K. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.03.018 · Cited by 22
Thyroid hormone status in patients with severe selenium deficiency
Kawai, M., Shoji, Y., Onuma, S., Etani, Y., & Ida, S. (2018) · Clinical Pediatric Endocrinology · doi:10.1297/cpe.27.67 · Cited by 20
Lee, K. W., Shin, Y., Lee, S., & Lee, S. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.803024 · Cited by 20
Taguchi, T., Kurata, M., Onishi, I., Kinowaki, Y., Sato, Y., Shiono, S., Ishibashi, S., Ikeda, M., Yamamoto, M., Kitagawa, M., et al. (2020) · Laboratory Investigation · doi:10.1038/s41374-020-00495-0 · Cited by 19
Identification of a novel endogenous long non-coding RNA that inhibits selenoprotein P translation
Mita, Y., Uchida, R., Yasuhara, S., Kishi, K., Hoshi, T., Matsuo, Y., Yokooji, T., Shirakawa, Y., Toyama, T., Urano, Y., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab498 · Cited by 19
Bifano, A. L., Atassi, T., Ferrara, T. M., & Driscoll, D. M. (2013) · BMC Molecular Biology · doi:10.1186/1471-2199-14-12 · Cited by 18
Concurrent TSHR mutations and DIO2 T92A polymorphism result in abnormal thyroid hormone metabolism
Park, E., Jung, J., Araki, O., Tsunekawa, K., Park, S. Y., Kim, J., Murakami, M., Jeong, S., & Lee, S. (2018) · Scientific Reports · doi:10.1038/s41598-018-28480-0 · Cited by 18
Zhao, W., Bohleber, S., Schmidt, H., Seeher, S., Howard, M. T., Braun, D., Arndt, S., Reuter, U., Wende, H., Birchmeier, C., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009369 · Cited by 18
The Effect of tRNA[Ser]Sec Isopentenylation on Selenoprotein Expression
Fradejas‐Villar, N., Bohleber, S., Zhao, W., Reuter, U., Kötter, A., Helm, M., Knoll, R., McFarland, R., Taylor, R. W., Mo, Y., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111454 · Cited by 18
Modulation of muscle redox and protein aggregation rescues lethality caused by mutant lamins
Coombs, G. S., Rios-Monterrosa, J. L., Lai, S., Dai, Q., Goll, A. C., Ketterer, M. R., Valdes, M. F., Uche, N., Benjamin, I. J., & Wallrath, L. L. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102196 · Cited by 20
Selenium Deficiency and Thyroid Disease
Rayman, M. P., & Duntas, L. H. (2019) · Springer eBooks · doi:10.1007/978-3-319-72102-6_9 · Cited by 17
Fu, J., Korwutthikulrangsri, M., Gonc, E. N., Sillers, L., Liao, X.-H., Alikaşifoğlu, A., Kandemir, N., Menucci, M. B., Burman, K. D., Weiss, R. E., et al. (2020) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgz169 · Cited by 17
Gene polymorphisms and thyroid hormone signaling: implication for the treatment of hypothyroidism
Penna, G., Salas-Lucia, F., Ribeiro, M. O., & Bianco, A. C. (2023) · Endocrine · doi:10.1007/s12020-023-03528-y · Cited by 17
Samaranayake, G. J., Troccoli, C. I., Zhang, L., Huynh, M. Q., Jayaraj, C. J., Ji, D., McPherson, L. A., Onishi, Y., Nguyen, D. M., Robbins, D. J., et al. (2019) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-19-0437 · Cited by 16
Self-citationIdentification of Resistance to Exogenous Thyroxine in Humans
Lacámara, N., Beatriz Lecumberri, S., Barquiel, B., Escribano, A., Casado, I. G., Álvarez‐Escolá, C., Blanquer, F. A., Morales, F., Alfayate, R., Bernal-Soriano, M. C., et al. (2020) · Thyroid · doi:10.1089/thy.2019.0825 · Cited by 16
Disorders of the thyroid in the newborn and infant
Vliet, G. V., & Deladoëy, J. (2014) · Elsevier eBooks · doi:10.1016/b978-1-4557-4858-7.00016-0 · Cited by 16
Sun, J., Min, Z., Zhao, W., Hussain, S., Zhao, Y., Guo, D., Zhang, F., Guo, Y., Sun, M., Huang, H., et al. (2018) · Cartilage · doi:10.1177/1947603518809406 · Cited by 15
Vindry, C., Guillin, O., Mangeot, P. E., Ohlmann, T., & Chavatte, L. (2019) · Cells · doi:10.3390/cells8060574 · Cited by 17
Redox Signaling and Stress in Inherited Myopathies
Doğan, Ş. A., Giacchin, G., Zito, E., & Viscomi, C. F. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0266 · Cited by 15
Selenoproteins and the Thioredoxin System
Lu, J., & Holmgren, A. (2011) · Springer eBooks · doi:10.1007/978-1-4614-1025-6_12 · Cited by 14
Self-citationCandidate Genes in Bull Semen Production Traits: An Information Approach Review
Modiba, M. C., Nephawe, K. A., Hadebe, K., Lu, W., & Mtileni, B. J. (2022) · Veterinary Sciences · doi:10.3390/vetsci9040155 · Cited by 13
Alteration of Selenoprotein Expression During Stress and in Aging
Touat-Hamici, Z., Legrain, Y., Sonet, J., Bulteau, A., & Chavatte, L. (2016) · Springer eBooks · doi:10.1007/978-3-319-41283-2_45 · Cited by 14
Regulation of Thyroid Function, Synthesis and Function of Thyroid Hormones
Visser, T. J. (2018) · Endocrinology · doi:10.1007/978-3-319-29195-6_1-1 · Cited by 20
Thyroid Hormone Hyposensitivity: From Genotype to Phenotype and Back
Rurale, G., Cicco, E. D., Dentice, M., Salvatore, D., Persani, L., Marelli, F., & Luongo, C. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00912 · Cited by 13
Higher Serum Selenoprotein P Level as a Novel Inductor of Metabolic Complications in Psoriasis
Baran, A. M., Nowowiejska, J., Krahel, J. A., Kaminski, T. W., Maciaszek, M., & Flisiak, I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134594 · Cited by 13
Yepes-Calderón, M., Sotomayor, C. G., Neto, A. W. G., Gans, R. O. B., Berger, S. P., Rimbach, G. H., Esatbeyoglu, T., Rodrigo, R., Geleijnse, J. M., Navis, G., et al. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8040453 · Cited by 13
Morse, D. R., Cohen, L., Furst, M. L., & Martin, J. S. (1984) · PubMed · Cited by 13
Conrad, M., & Angeli, J. P. F. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.95621-6 · Cited by 15
Wilpert, N., Thamm, R., Thamm, M., Kratzsch, J., Seelow, D., Vogel, M., Krude, H., & Schuelke, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25168585 · Cited by 12
Mendieta‐Serrano, M. A., Schnabel, D., Lomelı́, H., & Vidal, E. S. (2015) · Gene Expression Patterns · doi:10.1016/j.gep.2015.08.003 · Cited by 12
Endocrinology of Fetal Development
Dattani, M., & Gevers, E. F. (2016) · Elsevier eBooks · doi:10.1016/b978-0-323-29738-7.00022-8 · Cited by 13
Self-citationIdentification of Genetic Disorders Causing Disruption of Selenoprotein Biosynthesis
Schoenmakers, E., & Chatterjee, K. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7258-6_23 · Cited by 12
Self-citationGill, J. S., Bansal, B., Poojary, R., Singh, H., Huang, F., Weis, J., Herman, K., Schultz, B., Coban, E., Guo, K., et al. (2024) · Cancers · doi:10.3390/cancers16132399 · Cited by 11
Stoupa, A., França, M. M., Abdulhadi‐Atwan, M., Fujisawa, H., Korwutthikulrangsri, M., Marchand, I., Polak, G., Beltrand, J., Polak, M., Kariyawasam, D., et al. (2024) · Genetics in Medicine · doi:10.1016/j.gim.2024.101280 · Cited by 11
Selenium Metabolism in Herbivores and Higher Trophic Levels Including Mammals
Schomburg, L., & Arnér, E. S. J. (2017) · Plant ecophysiology · doi:10.1007/978-3-319-56249-0_8 · Cited by 12
Inherited Selenocysteine Transfer RNA Mutation: Clinical and Hormonal Evaluation of 2 Patients
Geslot, A., Savagner, F., & Caron, P. J. (2021) · European Thyroid Journal · doi:10.1159/000518275 · Cited by 11
Fetal and Neonatal Endocrinology
Gevers, E. F., Fisher, D. A., & Dattani, M. (2015) · Elsevier eBooks · doi:10.1016/b978-0-323-18907-1.00145-1 · Cited by 11
Self-citationUnderstanding the role of tRNA modifications in UGA recoding as selenocysteine in eukaryotes
Chavatte, L., Lange, L., Schweizer, U., & Ohlmann, T. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169017 · Cited by 10
The selenoprotein P–LRP5/6–WNT3A complex promotes tumorigenesis in sporadic colorectal cancer
Prabhu, K. S. (2023) · Journal of Clinical Investigation · doi:10.1172/jci171885 · Cited by 10
“Alphabet” Selenoproteins: Implications in Pathology
Dogaru, C. B., Duţă, C., Muscurel, C., & Stoian, I. A.-M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242015344 · Cited by 10
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
