Journal articles on the topic 'Amino acid selenocysteine'
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Böck, A., K. Forchhammer, J. Heider, W. Leinfelder, G. Sawers, B. Veprek, and F. Zinoni. "Selenocysteine: the 21st amino acid." Molecular Microbiology 5, no. 3 (March 1991): 515–20. http://dx.doi.org/10.1111/j.1365-2958.1991.tb00722.x.
Full textGonzalez-Flores, Jonathan N., Sumangala P. Shetty, Aditi Dubey, and Paul R. Copeland. "The molecular biology of selenocysteine." BioMolecular Concepts 4, no. 4 (August 1, 2013): 349–65. http://dx.doi.org/10.1515/bmc-2013-0007.
Full textBaclaocos, Janinah, and John James Mackrill. "Why Multiples of 21? Why does Selenoprotein P Contain Multiple Selenocysteine Residues?" Current Nutraceuticals 1, no. 1 (April 29, 2020): 42–53. http://dx.doi.org/10.2174/2665978601666200213120929.
Full textSeale, Lucia A., Vedbar S. Khadka, Mark Menor, Guoxiang Xie, Ligia M. Watanabe, Alexandru Sasuclark, Kyrillos Guirguis, et al. "Combined Omics Reveals That Disruption of the Selenocysteine Lyase Gene Affects Amino Acid Pathways in Mice." Nutrients 11, no. 11 (October 26, 2019): 2584. http://dx.doi.org/10.3390/nu11112584.
Full textLongtin, R. "A Forgotten Debate: Is Selenocysteine the 21st Amino Acid?" JNCI Journal of the National Cancer Institute 96, no. 7 (April 6, 2004): 504–5. http://dx.doi.org/10.1093/jnci/96.7.504.
Full textCopeland, Paul R., and Michael T. Howard. "Ribosome Fate during Decoding of UGA-Sec Codons." International Journal of Molecular Sciences 22, no. 24 (December 8, 2021): 13204. http://dx.doi.org/10.3390/ijms222413204.
Full textHendrickson, Tamara L., Whitney N. Wood, and Udumbara M. Rathnayake. "Did Amino Acid Side Chain Reactivity Dictate the Composition and Timing of Aminoacyl-tRNA Synthetase Evolution?" Genes 12, no. 3 (March 12, 2021): 409. http://dx.doi.org/10.3390/genes12030409.
Full textSeeher, Sandra, Bradley A. Carlson, Angela C. Miniard, Eva K. Wirth, Yassin Mahdi, Dolph L. Hatfield, Donna M. Driscoll, and Ulrich Schweizer. "Impaired selenoprotein expression in brain triggers striatal neuronal loss leading to co-ordination defects in mice." Biochemical Journal 462, no. 1 (July 24, 2014): 67–75. http://dx.doi.org/10.1042/bj20140423.
Full textLi, Chuang, Myriam Reches, and Hanna Engelberg-Kulka. "The Bulged Nucleotide in the Escherichia coli Minimal Selenocysteine Insertion Sequence Participates in Interaction with SelB: a Genetic Approach." Journal of Bacteriology 182, no. 22 (November 15, 2000): 6302–7. http://dx.doi.org/10.1128/jb.182.22.6302-6307.2000.
Full textCastellano, S., A. M. Andres, E. Bosch, M. Bayes, R. Guigo, and A. G. Clark. "Low Exchangeability of Selenocysteine, the 21st Amino Acid, in Vertebrate Proteins." Molecular Biology and Evolution 26, no. 9 (June 1, 2009): 2031–40. http://dx.doi.org/10.1093/molbev/msp109.
Full textGranold, Matthias, Parvana Hajieva, Monica Ioana Toşa, Florin-Dan Irimie, and Bernd Moosmann. "Modern diversification of the amino acid repertoire driven by oxygen." Proceedings of the National Academy of Sciences 115, no. 1 (December 19, 2017): 41–46. http://dx.doi.org/10.1073/pnas.1717100115.
Full textSeale, Lucia A. "Selenocysteine β-Lyase: Biochemistry, Regulation and Physiological Role of the Selenocysteine Decomposition Enzyme." Antioxidants 8, no. 9 (September 1, 2019): 357. http://dx.doi.org/10.3390/antiox8090357.
Full textSmall-Howard, A. L., and M. J. Berry. "Unique features of selenocysteine incorporation function within the context of general eukaryotic translational processes." Biochemical Society Transactions 33, no. 6 (October 26, 2005): 1493–97. http://dx.doi.org/10.1042/bst0331493.
Full textMilanovic, Svetlana, Ivan Jovanovic, and Olivera Valcic. "Selenoproteins." Veterinarski glasnik 69, no. 1-2 (2015): 75–89. http://dx.doi.org/10.2298/vetgl1502075m.
Full textITOH, Yuzuru, and Shigeyuki YOKOYAMA. "The Molecular Mechanism of the Synthesis of the 21st Amino Acid, Selenocysteine." Nihon Kessho Gakkaishi 56, no. 3 (2014): 186–93. http://dx.doi.org/10.5940/jcrsj.56.186.
Full textLee, B. J., M. Rajagopalan, Y. S. Kim, K. H. You, K. B. Jacobson, and D. Hatfield. "Selenocysteine tRNA[Ser]Sec gene is ubiquitous within the animal kingdom." Molecular and Cellular Biology 10, no. 5 (May 1990): 1940–49. http://dx.doi.org/10.1128/mcb.10.5.1940-1949.1990.
Full textLee, B. J., M. Rajagopalan, Y. S. Kim, K. H. You, K. B. Jacobson, and D. Hatfield. "Selenocysteine tRNA[Ser]Sec gene is ubiquitous within the animal kingdom." Molecular and Cellular Biology 10, no. 5 (May 1990): 1940–49. http://dx.doi.org/10.1128/mcb.10.5.1940.
Full textCubas-Gaona, Liliana L., Patricia de Francisco, Ana Martín-González, and Juan Carlos Gutiérrez. "Tetrahymena Glutathione Peroxidase Family: A Comparative Analysis of These Antioxidant Enzymes and Differential Gene Expression to Metals and Oxidizing Agents." Microorganisms 8, no. 7 (July 5, 2020): 1008. http://dx.doi.org/10.3390/microorganisms8071008.
Full textSantesmasses, Didac, and Vadim N. Gladyshev. "Pathogenic Variants in Selenoproteins and Selenocysteine Biosynthesis Machinery." International Journal of Molecular Sciences 22, no. 21 (October 27, 2021): 11593. http://dx.doi.org/10.3390/ijms222111593.
Full textMohanta, Tapan Kumar, Yugal Kishore Mohanta, Satya Kumar Avula, Amilia Nongbet, and Ahmed Al-Harrasi. "Virtual 2D map of cyanobacterial proteomes." PLOS ONE 17, no. 10 (October 3, 2022): e0275148. http://dx.doi.org/10.1371/journal.pone.0275148.
Full textFradejas, Noelia, Bradley A. Carlson, Eddy Rijntjes, Niels-Peter Becker, Ryuta Tobe, and Ulrich Schweizer. "Mammalian Trit1 is a tRNA[Ser]Sec-isopentenyl transferase required for full selenoprotein expression." Biochemical Journal 450, no. 2 (February 15, 2013): 427–32. http://dx.doi.org/10.1042/bj20121713.
Full textSkaff, Ojia, David I. Pattison, Philip E. Morgan, Rushad Bachana, Vimal K. Jain, K. Indira Priyadarsini, and Michael J. Davies. "Selenium-containing amino acids are targets for myeloperoxidase-derived hypothiocyanous acid: determination of absolute rate constants and implications for biological damage." Biochemical Journal 441, no. 1 (December 14, 2011): 305–16. http://dx.doi.org/10.1042/bj20101762.
Full textBirk, Ohad S. "Selenocysteinopathies: progressive cerebello–cerebral atrophy and other diseases of the 21st amino acid, selenocysteine." Future Neurology 6, no. 2 (March 2011): 135–38. http://dx.doi.org/10.2217/fnl.11.2.
Full textWelegedara, Adarshi P., Luke A. Adams, Thomas Huber, Bim Graham, and Gottfried Otting. "Site-Specific Incorporation of Selenocysteine by Genetic Encoding as a Photocaged Unnatural Amino Acid." Bioconjugate Chemistry 29, no. 7 (June 6, 2018): 2257–64. http://dx.doi.org/10.1021/acs.bioconjchem.8b00254.
Full textMa, Chi, Verena Martinez-Rodriguez, and Peter R. Hoffmann. "Roles for Selenoprotein I and Ethanolamine Phospholipid Synthesis in T Cell Activation." International Journal of Molecular Sciences 22, no. 20 (October 16, 2021): 11174. http://dx.doi.org/10.3390/ijms222011174.
Full textTupikina, Elena Yu, Valerii V. Karpov, and Peter M. Tolstoy. "On the influence of water molecules on the outer electronic shells of R–SeH, R–Se(−) and R–SeOH fragments in the selenocysteine amino acid residue." Physical Chemistry Chemical Physics 23, no. 25 (2021): 13965–70. http://dx.doi.org/10.1039/d1cp01345a.
Full textMoustafa, Mohamed E., Bradley A. Carlson, Muhammad A. El-Saadani, Gregory V. Kryukov, Qi-An Sun, John W. Harney, Kristina E. Hill, et al. "Selective Inhibition of Selenocysteine tRNA Maturation and Selenoprotein Synthesis in Transgenic Mice Expressing Isopentenyladenosine-Deficient Selenocysteine tRNA." Molecular and Cellular Biology 21, no. 11 (June 1, 2001): 3840–52. http://dx.doi.org/10.1128/mcb.21.11.3840-3852.2001.
Full textPeng, Jing-Jing, Shi-Yang Yue, Yu-Hui Fang, Xiao-Ling Liu, and Cheng-Hua Wang. "Mechanisms Affecting the Biosynthesis and Incorporation Rate of Selenocysteine." Molecules 26, no. 23 (November 25, 2021): 7120. http://dx.doi.org/10.3390/molecules26237120.
Full textKremer, Penny M., Daniel J. Torres, Ann C. Hashimoto, and Marla J. Berry. "Disruption of Selenium Handling During Puberty Causes Sex-Specific Neurological Impairments in Mice." Antioxidants 8, no. 4 (April 24, 2019): 110. http://dx.doi.org/10.3390/antiox8040110.
Full textSteegborn, Clemens, and Ulrich Schweizer. "Structure and Mechanism of Iodothyronine Deiodinases – What We Know, What We Don’t Know, and What Would Be Nice to Know." Experimental and Clinical Endocrinology & Diabetes 128, no. 06/07 (November 7, 2019): 375–78. http://dx.doi.org/10.1055/a-1022-9916.
Full textMundaganore, D. S., Y. D. Mundagnore, and K. V. Ashokan. "In Silico Validation of Middle East Respiratory Syndrome (MERS) Virus Proteins for Better Drug Development." International Journal of Applied Sciences and Biotechnology 1, no. 4 (December 21, 2013): 272–78. http://dx.doi.org/10.3126/ijasbt.v1i4.9184.
Full textVank, Judith C., Carlos P. Sosa, Andras Perczel, and Imre G. Csizmadia. "Peptide models XXVII. An exploratory ab initio study on the 21st amino acid side-chain conformations of N-formyl-L-selenocysteinamide (For-L-Sec-NH2) and N-acetyl-L-selenocysteine-N-methylamide (Ac-L-Sec-NHMe) in their γL backbone conformation." Canadian Journal of Chemistry 78, no. 3 (March 1, 2000): 395–408. http://dx.doi.org/10.1139/v00-029.
Full textPeters, Franziska, Michael Rother, and Matthias Boll. "Selenocysteine-Containing Proteins in Anaerobic Benzoate Metabolism of Desulfococcus multivorans." Journal of Bacteriology 186, no. 7 (April 1, 2004): 2156–63. http://dx.doi.org/10.1128/jb.186.7.2156-2163.2004.
Full textBellinger, Frederick P., Arjun V. Raman, Mariclair A. Reeves, and Marla J. Berry. "Regulation and function of selenoproteins in human disease." Biochemical Journal 422, no. 1 (July 29, 2009): 11–22. http://dx.doi.org/10.1042/bj20090219.
Full textThanbichler, Martin, Bernhard Neuhierl, and August Böck. "S-Methylmethionine Metabolism in Escherichia coli." Journal of Bacteriology 181, no. 2 (January 15, 1999): 662–65. http://dx.doi.org/10.1128/jb.181.2.662-665.1999.
Full textSchoenmakers, Erik, and Krishna Chatterjee. "Human Genetic Disorders Resulting in Systemic Selenoprotein Deficiency." International Journal of Molecular Sciences 22, no. 23 (November 29, 2021): 12927. http://dx.doi.org/10.3390/ijms222312927.
Full textItoh, Yuzuru, Markus J. Bröcker, Shun-ichi Sekine, Gifty Hammond, Shiro Suetsugu, Dieter Söll, and Shigeyuki Yokoyama. "Decameric SelA•tRNASec Ring Structure Reveals Mechanism of Bacterial Selenocysteine Formation." Science 340, no. 6128 (April 4, 2013): 75–78. http://dx.doi.org/10.1126/science.1229521.
Full textSonet, Jordan, Maurine Mosca, Katarzyna Bierla, Karolina Modzelewska, Anna Flis-Borsuk, Piotr Suchocki, Iza Ksiazek, et al. "Selenized Plant Oil Is an Efficient Source of Selenium for Selenoprotein Biosynthesis in Human Cell Lines." Nutrients 11, no. 7 (July 4, 2019): 1524. http://dx.doi.org/10.3390/nu11071524.
Full textPerry, A. C. F., R. Jones, L. S. P. Niang, R. M. Jackson, and L. Hall. "Genetic evidence for an androgen-regulated epididymal secretory glutathione peroxidase whose transcript does not contain a selenocysteine codon." Biochemical Journal 285, no. 3 (August 1, 1992): 863–70. http://dx.doi.org/10.1042/bj2850863.
Full textGhuge, Sandip A., Ulhas Sopanrao Kadam, and Jong Chan Hong. "Selenoprotein: Potential Player in Redox Regulation in Chlamydomonas reinhardtii." Antioxidants 11, no. 8 (August 22, 2022): 1630. http://dx.doi.org/10.3390/antiox11081630.
Full textTuranov, Anton A., Xue-Ming Xu, Bradley A. Carlson, Min-Hyuk Yoo, Vadim N. Gladyshev, and Dolph L. Hatfield. "Biosynthesis of Selenocysteine, the 21st Amino Acid in the Genetic Code, and a Novel Pathway for Cysteine Biosynthesis." Advances in Nutrition 2, no. 2 (March 1, 2011): 122–28. http://dx.doi.org/10.3945/an.110.000265.
Full textWatabe, Shoji, Yumiko Makino, Kazuo Ogawa, Tomoko Hiroi, Yoshimi Yamamoto, and Susumu Y. Takahashi. "Mitochondrial thioredoxin reductase in bovine adrenal cortex. Its purification, properties, nucleotide/amino acid sequences, and identification of selenocysteine." European Journal of Biochemistry 264, no. 1 (August 15, 1999): 74–84. http://dx.doi.org/10.1046/j.1432-1327.1999.00578.x.
Full textSliwkowski, M. X., and T. C. Stadtman. "Selenoprotein A of the clostridial glycine reductase complex: purification and amino acid sequence of the selenocysteine-containing peptide." Proceedings of the National Academy of Sciences 85, no. 2 (January 1, 1988): 368–71. http://dx.doi.org/10.1073/pnas.85.2.368.
Full textPremadasa, Lakmini, Gabrielle Dailey, Jan A. Ruzicka, and Ethan Will Taylor. "Selenium-Dependent Read Through of the Conserved 3’-Terminal UGA Stop Codon of HIV-1 nef." American Journal of Biopharmacy and Pharmaceutical Sciences 1 (November 1, 2021): 1. http://dx.doi.org/10.25259/ajbps_6_2021.
Full textHaruna, Ken-ichi, Muhammad H. Alkazemi, Yuchen Liu, Dieter Söll, and Markus Englert. "Engineering the elongation factor Tu for efficient selenoprotein synthesis." Nucleic Acids Research 42, no. 15 (July 26, 2014): 9976–83. http://dx.doi.org/10.1093/nar/gku691.
Full textLabunskyy, Vyacheslav M., Dolph L. Hatfield, and Vadim N. Gladyshev. "Selenoproteins: Molecular Pathways and Physiological Roles." Physiological Reviews 94, no. 3 (July 2014): 739–77. http://dx.doi.org/10.1152/physrev.00039.2013.
Full textShimada, Briana K., Sydonie Swanson, Pamela Toh, and Lucia A. Seale. "Metabolism of Selenium, Selenocysteine, and Selenoproteins in Ferroptosis in Solid Tumor Cancers." Biomolecules 12, no. 11 (October 28, 2022): 1581. http://dx.doi.org/10.3390/biom12111581.
Full textNovoselov, Sergey V., Deame Hua, Alexey V. Lobanov, and Vadim N. Gladyshev. "Identification and characterization of Fep15, a new selenocysteine-containing member of the Sep15 protein family." Biochemical Journal 394, no. 3 (February 24, 2006): 575–79. http://dx.doi.org/10.1042/bj20051569.
Full textKazi Tani, Latifa Sarra, Nouria Dennouni-Medjati, Benoit Toubhans, and Laurent Charlet. "Selenium Deficiency—From Soil to Thyroid Cancer." Applied Sciences 10, no. 15 (August 4, 2020): 5368. http://dx.doi.org/10.3390/app10155368.
Full textSengupta, Aniruddha, Bradley A. Carlson, Vyacheslav M. Labunskyy, Vadim N. Gladyshev, and Dolph L. Hatfield. "Selenoprotein T deficiency alters cell adhesion and elevates selenoprotein W expression in murine fibroblast cells." Biochemistry and Cell Biology 87, no. 6 (December 2009): 953–61. http://dx.doi.org/10.1139/o09-064.
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