Threading the needle: getting selenocysteine into proteins

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 2,353 · see citing works

The kink‐turn: a new RNA secondary structure motif

Klein, D. J., Schmeing, T. M., Moore, P. B., & Steitz, T. A. (2001) · The EMBO Journal · doi:10.1093/emboj/20.15.4214 · Cited by 740 · see citing works

Selenoproteins

Lu, J., & Holmgren, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800045200 · Cited by 618 · see citing works

A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs

Copeland, P. R., Fletcher, J. E., Carlson, B. A., Hatfield, D. L., & Driscoll, D. M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.2.306 · Cited by 398 · see citing works

Early embryonic lethality caused by targeted disruption of the mouse selenocysteine tRNA gene ( Trsp )

Bösl, M. R., Takaku, K., Oshima, M., Nishimura, S., & Taketo, M. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.11.5531 · Cited by 337 · see citing works

Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems

Sun, Q.-A., Kirnarsky, L., Sherman, S., & Gladyshev, V. N. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051454398 · Cited by 312 · see citing works

Decoding apparatus for eukaryotic selenocysteine insertion

Tujebajeva, R. M., Copeland, P. R., Xu, X., Carlson, B. A., Harney, J. W., Driscoll, D. M., Hatfield, D. L., & Berry, M. J. (2000) · EMBO Reports · doi:10.1093/embo-reports/kvd033 · Cited by 307 · see citing works

Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation

Fagegaltier, D., Hubert, N., Yamada, K., Mizutani, T., Carbon, P., & Krol, A. (2000) · The EMBO Journal · doi:10.1093/emboj/19.17.4796 · Cited by 294 · see citing works

Selenoproteins and selenocysteine insertion system in the model plant cell system, Chlamydomonas reinhardtii

Novoselov, S. V., Rao, M., Onoshko, N. V., Zhi, H., Kryukov, G. V., Xiang, Y., Weeks, D. P., Hatfield, D. L., & Gladyshev, V. N. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf372 · Cited by 276 · see citing works

A Taste Receptor Required for the Caffeine Response In Vivo

Moon, S. J., Köttgen, M., Jiao, Y., Xu, H., & Montell, C. (2006) · Current Biology · doi:10.1016/j.cub.2006.07.024 · Cited by 272 · see citing works

The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinery

Boulon, S., Marmier‐Gourrier, N., Pradet‐Balade, B., Wurth, L., Verheggen, C., Jády, B. E., Rothé, B., Begon‐Pescia, C., Robert, M.-C., Kiss, T., et al. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200708110 · Cited by 238 · see citing works

Identification of a novel selD homolog from Eukaryotes, Bacteria, and Archaea: Is there an autoregulatory mechanism in selenocysteine metabolism?

Guimarães, M. J., Peterson, D., Vicari, A. P., Cocks, B. G., Copeland, N. G., Gilbert, D. J., Jenkins, N. A., Ferrick, D. A., Kastelein, R. A., Bazán, J. F., et al. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.26.15086 · Cited by 231 · see citing works

A novel RNA structural motif in the selenocysteine insertion element of eukaryotic selenoprotein mRNAs.

Walczak, R., Westhof, É., Carbon, P., & Krol, A. (1996) · Europe PMC (PubMed Central) · Cited by 229 · see citing works

Selenium Deficiency Reduces the Abundance of mRNA for Se-Dependent Glutathione Peroxidase 1 by a UGA-Dependent Mechanism Likely To Be Nonsense Codon-Mediated Decay of Cytoplasmic mRNA

Moriarty, P. M., Reddy, C. C., & Maquat, L. E. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.5.2932 · Cited by 220 · see citing works

Conserved nucleotide sequences in the open reading frame and 3' untranslated region of selenoprotein P mRNA.

Hill, K. E., Lloyd, R. S., & Burk, R. F. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.2.537 · Cited by 187 · see citing works

Ribosomal protein L30 is a component of the UGA-selenocysteine recoding machinery in eukaryotes

Chavatte, L., Brown, B. A., & Driscoll, D. M. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb922 · Cited by 184 · see citing works

Structural Basis for Nucleotide Exchange and Competition with tRNA in the Yeast Elongation Factor Complex eEF1A:eEF1Bα

Andersen, G. R., Pedersen, L., Valente, L., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00122-2 · Cited by 182 · see citing works

Supramolecular Complexes Mediate Selenocysteine Incorporation In Vivo

Small-Howard, A. L., Morozova, N., Stoytcheva, Z., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.6.2337-2346.2006 · Cited by 162 · see citing works

Mammalian Selenoprotein in Which Selenocysteine (Sec) Incorporation Is Supported by a New Form of Sec Insertion Sequence Element

Korotkov, K. V., Novoselov, S. V., Hatfield, D. L., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.5.1402-1411.2002 · Cited by 159 · see citing works

The mammalian nonsense‐mediated mRNA decay pathway: To decay or not to decay! Which players make the decision?

Silva, A. L., & Romão, L. (2009) · FEBS Letters · doi:10.1016/j.febslet.2008.12.058 · Cited by 154 · see citing works

Purification, Redox Sensitivity, and RNA Binding Properties of SECIS-binding Protein 2, a Protein Involved in Selenoprotein Biosynthesis

Copeland, P. R., & Driscoll, D. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25447 · Cited by 152 · see citing works

Two distinct SECIS structures capable of directing selenocysteine incorporation in eukaryotes

Grundner‐Culemann, E., Martin, G. W., Harney, J. W., & Berry, M. J. (1999) · RNA · doi:10.1017/s1355838299981542 · Cited by 145 · see citing works

Genetic Code Supports Targeted Insertion of Two Amino Acids by One Codon

Turanov, A. A., Lobanov, A. V., Fomenko, D. E., Morrison, H. G., Sogin, M. L., Klobutcher, L. A., Hatfield, D. L., & Gladyshev, V. N. (2009) · Science · doi:10.1126/science.1164748 · Cited by 139 · see citing works

Selenium Metabolism in Drosophila

Martı́n-Romero, F. J., Kryukov, G. V., Lobanov, A. V., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100422200 · Cited by 139 · see citing works

Selenoprotein H Is a Nucleolar Thioredoxin-like Protein with a Unique Expression Pattern

Novoselov, S. V., Kryukov, G. V., Xu, X., Carlson, B. A., Hatfield, D. L., & Gladyshev, V. N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701605200 · Cited by 129 · see citing works

Selenocysteine tRNA‐specific elongation factor SelB is a structural chimaera of elongation and initiation factors

Leibundgut, M., Frick, C., Thanbichler, M. R., Böck, A., & Ban, N. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600505 · Cited by 121 · see citing works

RNA structure and function in C/D and H/ACA s(no)RNPs

Henras, A. K., Dez, C., & Henry, Y. A. L. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.05.006 · Cited by 120 · see citing works

Insight into Mammalian Selenocysteine Insertion: Domain Structure and Ribosome Binding Properties of Sec Insertion Sequence Binding Protein 2

Copeland, P. R., Stepanik, V. A., & Driscoll, D. M. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.5.1491-1498.2001 · Cited by 116 · see citing works

Translational regulation of glutathione peroxidase 4 expression through guanine-rich sequence-binding factor 1 is essential for embryonic brain developmentPreprint

Ufer, C., Wang, C. C., Fähling, M., Schiebel, H., Thiele, B. J., Billett, E. E., Kühn, H., & Borchert, A. (2008) · Genes & Development · doi:10.1101/gad.466308 · Cited by 115 · see citing works

The Selenium-rich C-terminal Domain of Mouse Selenoprotein P Is Necessary for the Supply of Selenium to Brain and Testis but Not for the Maintenance of Whole Body Selenium*

Hill, K., Zhou, J.-D., Austin, L. M., Motley, A., Ham, A., Olson, G., Atkins, J., Gesteland, R., & Burk, R. F. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700436200 · Cited by 115 · see citing works

Dietary Selenium Stabilizes Glutathione Peroxidase mRNA in Rat Liver

Christensen, M. J., & Burgener, K. (1992) · Journal of Nutrition · doi:10.1093/jn/122.8.1620 · Cited by 112 · see citing works

The Redox State of SECIS Binding Protein 2 Controls Its Localization and Selenocysteine Incorporation Function

Papp, L. V., Lu, J., Striebel, F., Kennedy, D. D., Holmgren, A., & Khanna, K. K. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.02284-05 · Cited by 112 · see citing works

The selenocysteine incorporation machinery: interactions between the SECIS RNA and the SECIS-binding protein SBP2.

Fletcher, J. E., Copeland, P. R., Driscoll, D. M., & Krol, A. (2001) · PubMed Central · Cited by 111 · see citing works

SBP2 Binding Affinity Is a Major Determinant in Differential Selenoprotein mRNA Translation and Sensitivity to Nonsense-Mediated Decay

Squires, J. E., Stoytchev, I., Forry, E. P., & Berry, M. J. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00793-07 · Cited by 107 · see citing works

A novel RNA-binding motif in omnipotent suppressors of translation termination, ribosomal proteins and a ribosome modification enzyme?

Koonin, E. V., Peer Bork, B., & Sander, C. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.11.2166 · Cited by 106 · see citing works

Interaction of translation factor SELB with the formate dehydrogenase H selenopolypeptide mRNA.

Baron, C., Heider, J., & Böck, A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.9.4181 · Cited by 100 · see citing works

Recoding elements located adjacent to a subset of eukaryal selenocysteine‐specifying UGA codons

Howard, M. T., Aggarwal, G., Anderson, C. B., Khatri, S., Flanigan, K. M., & Atkins, J. F. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600642 · Cited by 96 · see citing works

An essential non-Watson-Crick base pair motif in 3'UTR to mediate selenoprotein translation.

Walczak, R., Carbon, P., & Krol, A. (1998) · PubMed · Cited by 96 · see citing works

Selenoproteins in Archaea and Gram-positive bacteria

Stock, T., & Rother, M. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.03.022 · Cited by 95 · see citing works

Efficiency of Mammalian Selenocysteine Incorporation

Mehta, A., Rebsch, C. M., Kinzy, S. A., Fletcher, J. E., & Copeland, P. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404639200 · Cited by 94 · see citing works

Selenoproteinless animals: Selenophosphate synthetase SPS1 functions in a pathway unrelated to selenocysteine biosynthesis

Lobanov, A. V., Hatfield, D. L., & Gladyshev, V. N. (2007) · Protein Science · doi:10.1110/ps.073261508 · Cited by 88 · see citing works

Dynamics and efficiency in vivo of UGA‐directed selenocysteine insertion at the ribosome

Suppmann, S., Persson, B. C., & Böck, A. (1999) · The EMBO Journal · doi:10.1093/emboj/18.8.2284 · Cited by 85 · see citing works

A mutation in theSEPN1selenocysteine redefinition element (SRE) reduces selenocysteine incorporation and leads toSEPN1-related myopathy

Maiti, B., Arbogast, S., Allamand, V., et al. (2008) · Human Mutation · doi:10.1002/humu.20879 · Cited by 84 · see citing works

An RNA-Binding Protein Recognizes a Mammalian Selenocysteine Insertion Sequence Element Required for Cotranslational Incorporation of Selenocysteine

Lesoon, A., Mehta, A., Singh, R. P., et al. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.4.1977 · Cited by 83 · see citing works

Relaxation of Selective Constraints Causes Independent Selenoprotein Extinction in Insect Genomes

Chapple, C. E., & Guigó, R. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002968 · Cited by 81 · see citing works

Regulation of gene expression by stop codon recoding: selenocysteine

Copeland, P. R. (2003) · Gene · doi:10.1016/s0378-1119(03)00588-2 · Cited by 80 · see citing works

Coupled tRNASec-Dependent Assembly of the Selenocysteine Decoding Apparatus

Zavacki, A. M., Mansell, J. B., Chung, M., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00064-9 · Cited by 80 · see citing works

Cis-acting elements are required for selenium regulation of glutathione peroxidase-1 mRNA levels

Weiss, S. L., & Sunde, R. A. (1998) · RNA · doi:10.1017/s1355838298971990 · Cited by 77 · see citing works

A highly efficient form of the selenocysteine insertion sequence element in protozoan parasites and its use in mammalian cells

Novoselov, S. V., Lobanov, A. V., Hua, D., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0610683104 · Cited by 73 · see citing works

Heterologous expression of archaeal selenoprotein genes directed by the SECIS element located in the 3′ non‐translated region

Rother, M., Resch, A., Gardner, W. L., et al. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02433.x · Cited by 70 · see citing works

The SBP2 and 15.5 kD/Snu13p proteins share the same RNA binding domain: Identification of SBP2 amino acids important to SECIS RNA binding

Allmang, C., Carbon, P., & Krol, A. (2002) · RNA · doi:10.1017/s1355838202020034 · Cited by 68 · see citing works

A recoding element that stimulates decoding of UGA codons by Sec tRNA [Ser]Sec

Howard, M. T., Moyle, M. W., Aggarwal, G., Carlson, B. A., & Anderson, C. B. (2007) · RNA · doi:10.1261/rna.473907 · Cited by 66 · see citing works

A Novel Protein Domain Induces High Affinity Selenocysteine Insertion Sequence Binding and Elongation Factor Recruitment

Donovan, J., Caban, K., Ranaweera, R. S., González-Flores, J., & Copeland, P. R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806008200 · Cited by 64 · see citing works

Altered RNA Binding Activity Underlies Abnormal Thyroid Hormone Metabolism Linked to a Mutation in Selenocysteine Insertion Sequence-binding Protein 2

Bubenik, J. L., & Driscoll, D. M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707059200 · Cited by 64 · see citing works

Regulation of the extracellular antioxidant selenoprotein plasma glutathione peroxidase (GPx-3) in mammalian cells

Ottaviano, F. G., Tang, S., Handy, D. E., et al. (2009) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-009-0049-x · Cited by 63 · see citing works

L30 Binds the Nascent RPL30 Transcript to Repress U2 snRNP Recruitment

Macías, S., Bragulat, M., Tardiff, D. F., & Vilardell, J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.05.002 · Cited by 60 · see citing works

cDNA cloning, expression pattern and RNA binding analysis of human selenocysteine insertion sequence (SECIS) binding protein 2

Lescure, A., Allmang, C., Yamada, K., Carbon, P., & Krol, A. (2002) · Gene · doi:10.1016/s0378-1119(02)00629-7 · Cited by 58 · see citing works

Efficient Incorporation of Multiple Selenocysteines Involves an Inefficient Decoding Step Serving as a Potential Translational Checkpoint and RibosomeBottleneck

Stoytcheva, Z., Tujebajeva, R. M., Harney, J. W., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00856-06 · Cited by 58 · see citing works

Structural studies of elongation and release factors

Noble, C. G., & Song, H. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7495-6 · Cited by 55 · see citing works

Structure of Prokaryotic SECIS mRNA Hairpin and its Interaction with Elongation Factor SelB

Fourmy, D., Guittet, É., & Yoshizawa, S. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01030-6 · Cited by 53 · see citing works

Selenocysteine Inserting RNA Elements Modulate GTP Hydrolysis of Elongation Factor SelB

Hüttenhofer, A., & Böck, A. (1998) · Biochemistry · doi:10.1021/bi972298k · Cited by 53 · see citing works

Nuclear Assembly of UGA Decoding Complexes on Selenoprotein mRNAs: a Mechanism for Eluding Nonsense-Mediated Decay?

Seale, L. A., Hoffmann, P. R., Michaud, T., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.5.1795-1805.2006 · Cited by 53 · see citing works

The L7Ae RNA Binding Motif Is a Multifunctional Domain Required for the Ribosome-Dependent Sec Incorporation Activity of Sec Insertion Sequence Binding Protein 2

Caban, K., Kinzy, S. A., & Copeland, P. R. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00632-07 · Cited by 53 · see citing works

Size matters: a view of selenocysteine incorporation from the ribosome

Caban, K., & Copeland, P. R. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5402-y · Cited by 50 · see citing works

Characterization of the SECIS binding protein 2 complex required for the co-translational insertion of selenocysteine in mammals

Kinzy, S. A. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki826 · Cited by 49 · see citing works

A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins

Takeuchi, A., Schmitt, D. C., Chapple, C. E., et al. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp078 · Cited by 46 · see citing works

Evolutionary history of selenocysteine incorporation from the perspective of SECIS binding proteins

Donovan, J., & Copeland, P. R. (2009) · BMC Evolutionary Biology · doi:10.1186/1471-2148-9-229 · Cited by 46 · see citing works

SelD homolog from Drosophila lacking selenide-dependent monoselenophosphate synthetase activity

Persson, B. C., Böck, A., Jäckle, H., et al. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1371 · Cited by 45 · see citing works

SECIS elements in the coding regions of selenoprotein transcripts are functional in higher eukaryotes

Mix, H., Lobanov, A. V., & Gladyshev, V. N. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl1060 · Cited by 44 · see citing works

Functional characterization of alternatively spliced human SECISBP2 transcript variants

Papp, L. V., Wang, J., Kennedy, D. D., Boucher, D., Zhang, Y., Gladyshev, V. N., Singh, R. N., & Khanna, K. K. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn829 · Cited by 43 · see citing works

Disruption of selenoprotein biosynthesis affects cell proliferation in the imaginal discs and brain of Drosophila melanogaster

Alsina, B., Corominas, M., Berry, M. J., et al. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.17.2875 · Cited by 42 · see citing works

Conserved selenoprotein synthesis is not critical for oxidative stress defence and the lifespan of Drosophila

Hirosawa‐Takamori, M., Chung, H., & Jäckle, H. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400097 · Cited by 42 · see citing works

Expression and characterization of nonmammalian selenoprotein P in the zebrafish,Danio rerio

Tujebajeva, R. M., Ransom, D. G., Harney, J. W., & Berry, M. J. (2000) · Genes to Cells · doi:10.1046/j.1365-2443.2000.00375.x · Cited by 40 · see citing works

SECISaln, a web-based tool for the creation of structure-based alignments of eukaryotic SECIS elements

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The class 2 selenophosphate synthetase gene of Drosophila contains a functional mammalian‐type SECIS

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K-Turn Motifs in Spatial RNA Coding

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Functional Analysis of the Interplay between Translation Termination, Selenocysteine Codon Context, and Selenocysteine Insertion Sequence-binding Protein 2

Gupta, M., & Copeland, P. R. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707061200 · Cited by 26 · see citing works

How an obscure archaeal gene inspired the discovery of selenocysteine biosynthesis in humans

Su, D., Hohn, M. J., Palioura, S., Sherrer, R. L., Yuan, J., Söll, D. G., & O’Donoghue, P. (2008) · IUBMB Life · doi:10.1002/iub.136 · Cited by 23 · see citing works

The presence of an intron within the rat gene for selenium-dependent glutathione peroxidase 1 is not required to protect nuclear RNA from UGA-mediated decay.

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Secondary structure and stability of the selenocysteine insertion sequences (SECIS) for human thioredoxin reductase and glutathione peroxidase

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Ferroptosis: Death by Lipid Peroxidation

Yang, W. S., & Stockwell, B. R. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.10.014 · Cited by 3,088 · see citing works

Glutathione Peroxidase-1 in Health and Disease: From Molecular Mechanisms to Therapeutic Opportunities

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Why Nature Chose Selenium

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Mutations in the selenocysteine insertion sequence-binding protein 2 gene lead to a multisystem selenoprotein deficiency disorder in humans

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Protein Threading Based on Multiple Protein Structure Alignment.

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Threading a database of protein cores

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Improving protein threading accuracy via combining local and global potential using TreeCRF modelPreprint

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Tertiary Structure Predictions on a Comprehensive Benchmark of Medium to Large Size Proteins

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Protein structure prediction and modelling

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