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1

Smith, Janet L., and Andrew Thompson. "Reactivity of selenomethionin – dents in the magic bullet?" Structure 6, no. 7 (July 1998): 815–19. http://dx.doi.org/10.1016/s0969-2126(98)00083-5.

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2

AVOSCAN, L., H. KHODJA, M. CARRIÈRE, J. COVÈS, and B. GOUGET. "PIXE ANALYSES OF THE SOLUBLE AND MEMBRANE SE-CONTAINING PROTEINS EXTRACTED FROMCUPRIAVIDUS METALLIDURANSCH34 AFTER SELENIUM OXIDES CHALLENGE." International Journal of PIXE 18, no. 03n04 (January 2008): 91–99. http://dx.doi.org/10.1142/s0129083508001430.

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The soil bacterium Cupriavidus metallidurans CH34 resist selenite by reducing it into the insoluble and less toxic elemental selenium. Two mechanisms of reduction of selenium oxides in C. metallidurans CH34 were highlighted: assimilation leading to organic species and detoxification leading to precipitation of selenite in nanoparticules of elemental selenium. The alkyl selenide detected as an intermediate product during assimilation of selenite or as the major accumulated chemical form during assimilation of selenate was identified as selenomethionine.Soluble and membrane proteins were extracted from C. metallidurans CH34 submitted to selenium oxides challenge. After separation by SDS-PAGE, µPIXE analyses were used for Se identification and quantification at a micrometer scale. The profiles of Se distribution in the different samples suggest a non-specific incorporation of selenium probably reflecting the incorporation of selenomethionin in place of the naturally occurring methionin.
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3

Kelly, Bernard T., Stephen C. Graham, and David J. Owen. "Using selenomethionyl derivatives to assign sequence in low-resolution structures of the AP2 clathrin adaptor." Acta Crystallographica Section D Structural Biology 72, no. 3 (March 1, 2016): 336–45. http://dx.doi.org/10.1107/s2059798315021580.

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Selenomethionine incorporation is a powerful technique for assigning sequence to regions of electron density at low resolution. Genetic introduction of methionine point mutations and the subsequent preparation and crystallization of selenomethionyl derivatives permits unambiguous sequence assignment by enabling the placement of the anomalous scatterers (Se atoms) thus introduced. Here, the use of this approach in the assignment of sequence in a part of the AP2 clathrin adaptor complex that is responsible for clathrin binding is described. AP2 plays a pivotal role in clathrin-mediated endocytosis, a tightly regulated process in which cell-surface transmembrane proteins are internalized from the plasma membrane by incorporation into lipid-enclosed transport vesicles. AP2 binds cargo destined for internalization and recruits clathrin, a large trimeric protein that helps to deform the membrane to produce the transport vesicle. By selenomethionine labelling of point mutants, it was shown that the clathrin-binding site is buried within a deep cleft of the AP2 complex. A membrane-stimulated conformational change in AP2 releases the clathrin-binding site from autoinhibition, thereby linking clathrin recruitment to membrane localization.
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4

& Al-Hassani, Ali. "TEMPERATURE AND SOME BLOOD TRAITS RESPONSE TO ORGANIC AND INORGANIC SELENIUM ADDED TO THE BROILER DIET REARED AT HIGH TEMPERATURES." IRAQI JOURNAL OF AGRICULTURAL SCIENCES 51, no. 3 (June 25, 2020): 734–43. http://dx.doi.org/10.36103/ijas.v51i3.1027.

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This study was conducted at the poultry farm -Animal Production Department/ College of Agricultural Engineering Sciences- University of Baghdad, for the period from 2018/8/17 to 2018/9/28, in order to study the effect of adding inorganic and organic selenium to the broiler diets reared at high temperatures in the physiological performance. A 420 un-sexed chicks of breed (Ross 308) were used in the experiment as a one-day old and with weight rate of 36.4g. The chicks were distributed randomly and equally on 7 treatments, each one included 3 replicates at 20 chicks/replicate. The experiment included the following treatments : T1,T2, and T3 as organic selenium treatments which are selenomethionin with a concentration of 0.3, 0.6, and 0.9 mg/kg feed, respectively, and T4, T5, and T6 as inorganic selenium treatments in the form of Sodium Selenite compound at a concentrations of 0.3, 0.6, and 0.9 mg/kg feed, respectively, and T7 control treatment without any addition of selenium, while the chicks were bred at a high temperature rate of 22.5 - 43.9 ℃. Organic and inorganic Selenium have not shown a clear effect in reducing body temperature compared to the control treatment, as well as, a high significant decreasing in the blood Hematocrit and Hemoglobin concentration for inorganic Selenium treatments compared to the organic Selenium and control treatments. Finally, The results indicated that there were no significant differences in the cholesterol and glucose levels in blood of organic and inorganic Selenium and control treatments.
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5

Kitajima, Toshihiko, Emi Yagi, Tomomi Kubota, Yasunori Chiba, Satoshi Nishikawa, and Yoshifumi Jigami. "Use of novel selenomethionine-resistant yeast to produce selenomethionyl protein suitable for structural analysis." FEMS Yeast Research 9, no. 3 (May 2009): 439–45. http://dx.doi.org/10.1111/j.1567-1364.2009.00484.x.

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6

Ruszel, Kinga, Piotr Pokorski, and Barbara Nieradko-Iwanicka. "Controversies about selenium supplementation." Polish Journal of Public Health 131, no. 1 (January 1, 2021): 20–26. http://dx.doi.org/10.2478/pjph-2021-0005.

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Abstract Introduction. Selenium (Se) is a trace element found mainly in meat, seafood, nuts and grains. Se is found in selenoproteins such as selenocystein or selenomethionin. A well balanced diet provides enough Se. Many regulatory and metabolic enzymes contain Se as their component, which is why Se supplementation is used in the treatment as well as prevention of multiple disorders. Se may, however, be toxic if overdosed. Aim. The aim of this review is to summarize the data about functions of Se in human body and to discuss its use in treatment and prevention of diseases. Materials and methods. The search was conducted using the PubMed and Google Scholar databases in March and April 2020. The key words used were: ‘selenium’, ‘cardiovascular disease’, ‘selenium supplementation’, ‘Keshan disease’, ‘source of selenium’. A total of 68 articles were analysed. Results. The first cases of chronic Se deficiency cases were documented 85 years ago in China. The patients with cardiomyopathy, extensive fibrosis and degenerative changes in the heart were diagnosed with Keshan disease. Human selenoproteonome consists of at least 25 selenoproteins. Se plays a role in immunity and metabolism via its role in functioning of numerous enzymes: glutathione peroxidase, thioredoxine and methionine sulfoxide reductase, methionine-sulfoxide reductase B1. Se plays a role in glucose homeostasis, Alzheimer’s disease, thyroid disorders, infectious, inflammatory diseases, vascular diseases and fertility. Conclusion. Se deficiency increases the risk of Keshan disease, but there is not enough evidence to recommend its supplementation for prevention of cardiovascular disease. However, Se status is important part of health assessment. Se supplementation should not exceed the dose of 55μg/day.
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7

Giraud, Marie-France, Helen J. McMiken, Gordon A. Leonard, Paul Messner, Chris Whitfield, and James H. Naismith. "Overexpression, purification, crystallization and preliminary structural study of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD), the fourth enzyme of the dTDP-L-rhamnose synthesis pathway, from Salmonella enterica serovar Typhimurium." Acta Crystallographica Section D Biological Crystallography 55, no. 12 (December 1, 1999): 2043–46. http://dx.doi.org/10.1107/s0907444999012251.

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L-Rhamnose is an essential component of the cell wall of many pathogenic bacteria. Its precursor, dTDP-L-rhamnose, is synthesized from α-D-glucose-1-phosphate and dTTP via a pathway requiring four distinct enzymes: RmlA, RmlB, RmlC and RmlD. RmlD catalyses the terminal step of this pathway by converting dTDP-6-deoxy-L-lyxo-4-hexulose to dTDP-L-rhamnose. RmlD from Salmonella enterica serovar Typhimurium has been overexpressed in Escherichia coli. The recombinant protein was purified by a two-step protocol involving anion-exchange and hydrophobic chromatography. Dynamic light-scattering experiments indicated that the recombinant protein is monodisperse. Crystals of native and selenomethionine-enriched RmlD have been obtained using the sitting-drop vapour-diffusion method with polyethylene glycol as precipitant. Diffraction data have been collected from orthorhombic crystals of both native and selenomethionyl-derivatized protein, allowing tracing of the protein structure.
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8

Park, Jimin, Hyojin Kim, Suwon Kim, Daeun Lee, and Dong Hae Shin. "Expression and crystallographic studies ofD-glycero-β-D-manno-heptose-1-phosphate adenylyltransferase fromBurkholderia pseudomallei." Acta Crystallographica Section F Structural Biology Communications 73, no. 2 (January 19, 2017): 90–94. http://dx.doi.org/10.1107/s2053230x16020537.

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The Gram-negative bacteriumBurkholderia pseudomalleiis the causative agent of melioidosis. D-glycero-β-D-manno-Heptose-1-phosphate adenylyltransferase (HldC) is the fourth enzyme of the ADP-L-glycero-β-D-manno-heptose biosynthesis pathway, which produces an essential carbohydrate comprising the inner core of lipopolysaccharide. Therefore, HldC is a potential target of antibiotics against melioidosis. In this study, HldC fromB. pseudomalleihas been cloned, expressed, purified and crystallized. Synchrotron X-ray data from a selenomethionine-substituted HldC crystal were also collected to 2.8 Å resolution. The crystal belonged to the primitive triclinic space groupP1, with unit-cell parametersa= 74.0,b= 74.0,c= 74.9 Å, α = 108.4, β = 108.4, γ = 108.0°. Eight protomers are present in the unit cell and three out of five selenomethionines were found in each protomer using thePHENIXsoftware suite. A full structural determination is in progress to elucidate the structure–function relationship of the protein.
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9

Kachuee, R., M. Moeini, and M. Souri. "Effects of organic and inorganic selenium supplementation during late pregnancy on colostrum and serum Se status, performance and passive immunity in Merghoz goats." Animal Production Science 54, no. 8 (2014): 1016. http://dx.doi.org/10.1071/an13150.

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This study was conducted to determine the effects of organic and inorganic selenium (Se) supplementation during late pregnancy on serum Se status, colostrum, performance and passive immunity in Merghoz goats in Iran. Thirty Merghoz goats (30 ± 3 kg) were given the same basal diet containing 0.11 mg Se/kg DM and were randomly allocated to one of three dietary treatments in a randomised complete block design. Four weeks before the expected kidding, the basal diets were supplemented with 0 (control), 0.3 mg Se/head.day in the form of L-selenomethionin (Se-Met) and 0.3 mg Se/head.day in the form of sodium selenite. Blood samples were collected from the goats in three phases: (1) a couple of days before starting the supplementation; (2) before the expected kidding; and (3) on the day of kidding. Blood samples were also taken from the newborn kids from the jugular vein at birth and 7 days of age. The serum Se and immunoglobulin G (IgG) concentrations, the white blood cells (WBC) and differential leukocyte counts were measured. The reproductive parameters such as the number of kids born per kidding, total weight of kids born per goat mating, the pregnancy period and kid birthweights were determined. The results indicated that the serum Se concentration increased in supplemented goats compared with controls. The Se concentrations also significantly increased in the colostrum of treated goats (P < 0.05). Similarly, serum Se concentrations in kids of treated goats were increased at birth. On the other hand, colostrum and daily milk production were not affected by Se supplementation. Likewise, the change in the mean serum IgG levels was not different among goats and kids (P > 0.05). However, the WBC, neutrophil and lymphocyte counts were higher in the kids of goats in the Se-Met group compared with the control group on the day of birth and 7 days of age (P < 0.05). It seemed that Se-Met could have influenced the lamb’s immunity at birth and 7 days of age. By contrast, selenite has not affected the performance and passive immunity in Merghoz goats.
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10

Kitajima, Toshihiko, and Yasunori Chiba. "Selenomethionine metabolism and its toxicity in yeast." BioMolecular Concepts 4, no. 6 (December 1, 2013): 611–16. http://dx.doi.org/10.1515/bmc-2013-0033.

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AbstractThe importance of selenium for organisms can be explained by its existence as selenocysteine in the catalytic centers of glutathione peroxidase and thioredoxin reductase. Another selenoamino acid, selenomethionine, is the major form of selenium in foods, and organisms that require selenium as a nutrient directly metabolize selenomethionine to a reactive form of selenium or store it in general proteins. Selenium is recognized as an essential nutrient for human and animal health; however, its excessive uptake harms mammals and the cytotoxic mechanism of selenium remains unclear. Recent progress in the development of selenium-enriched yeast and selenomethionine-resistant mutant to produce selenomethionine-containing proteins for X-ray crystallography has provided new insights into the molecular mechanism of selenomethionine toxicity. In this review, we describe the metabolism of seleno-compounds in yeast and discuss the cytotoxicity caused by selenomethionine against yeast from a metabolic viewpoint.
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11

Okopien, Boguslaw, and Robert Krysiak. "Haemostatic effects of levothyroxine and selenomethionine in euthyroid patients with Hashimoto’s thyroiditis." Thrombosis and Haemostasis 108, no. 11 (2012): 973–80. http://dx.doi.org/10.1160/th12-04-0275.

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SummaryThe aim of this prospective study was to investigate for the first time whether levothyroxine and selenomethionine, administered alone or in combination, affect coagulation and fibrinolysis in Hashimoto’s thyroiditis patients with normal thyroid function tests. A group of 155 ambulatory women with recently diagnosed and previously untreated Hashimoto’s thyroiditis, of whom 149 completed the study, were randomly assigned in a double-blind fashion to six months of treatment with levothyroxine, selenomethionine, levothyroxine plus selenomethionine, or placebo. The control group included 39 matched healthy women. The prothrombin time ratio, the activated partial thromboplastin time, and plasma levels/activities of fibrinogen, factor VII, von Willebrand factor, factor X and plasminogen activator inhibitor-1 (PAI-1) were assessed at baseline and after three and six months of treatment. Compared with the healthy subjects, Hashimoto’s thyroiditis patients exhibited higher plasma levels/activities of all of the parameters studied, as well as were characterised by the abnormal prothrombin time ratio and activated partial thromboplastin time. All these haemostatic disturbances were reduced or normalised by levothyroxine + selenomethionine treatment, while the effect of levothyroxine or selenomethionine was limited to fibrinogen and PAI-1, respectively. Our results demonstrate that euthyroid women with Hashimoto’s thyroiditis are characterised by abnormal coagulation and fibrinolysis. Levothyroxine and selenomethionine, especially if administered together, produce a beneficial effect on haemostasis in euthyroid patients with this disorder.Note: This study was in part a sub-study of another trial (ACTRN 12611000238976), which assessed the effect of levothyroxine and selenomethionine, administered alone or in combination, on monocyte and lymphocyte cytokine release in Hashimoto“s thyroiditis patients. Trial no.: ACTRN12612000271808.
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12

LeBlanc, Kelly L., Phuong-Mai Le, Juris Meija, Jianfu Ding, Jeremy E. Melanson, and Zoltán Mester. "Preparation and certification of natural and 82Se-labelled selenomethionine reference materials." Journal of Analytical Atomic Spectrometry 36, no. 2 (2021): 416–28. http://dx.doi.org/10.1039/d0ja00411a.

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Herein, we present the certification campaign for two new selenomethionine Certified Reference Materials: SENS-1, a high-purity powder of natural isotopic abundance, and SEES-1, a solution of selenium-82 labelled selenomethionine.
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13

Jamwal, Ankur, Yusuf Saibu, Tracy C. MacDonald, Graham N. George, and Som Niyogi. "The effects of dietary selenomethionine on tissue-specific accumulation and toxicity of dietary arsenite in rainbow trout (Oncorhynchus mykiss) during chronic exposure." Metallomics 11, no. 3 (2019): 643–55. http://dx.doi.org/10.1039/c8mt00309b.

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Selenomethionine facilitated arsenic deposition in the brain and likely in other tissues, possibly via bio-complexation. Elevated dietary selenomethionine can increase the tissue-specific accumulation and toxicity of As3+ in fish during chronic dietary exposure.
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14

Koch, Troels, and Ole Buchardt. "Synthesis of L-(+)-Selenomethionine." Synthesis 1993, no. 11 (1993): 1065–67. http://dx.doi.org/10.1055/s-1993-25996.

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15

Kitajima, Toshihiko, Yasunori Chiba, and Yoshifumi Jigami. "Mutation of High-Affinity Methionine Permease Contributes to Selenomethionyl Protein Production in Saccharomyces cerevisiae." Applied and Environmental Microbiology 76, no. 19 (August 6, 2010): 6351–59. http://dx.doi.org/10.1128/aem.01026-10.

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ABSTRACT The production of selenomethionine (SeMet) derivatives of recombinant proteins allows phase determination by single-wavelength or multiwavelength anomalous dispersion phasing in X-ray crystallography, and this popular approach has permitted the crystal structures of numerous proteins to be determined. Although yeast is an ideal host for the production of large amounts of eukaryotic proteins that require posttranslational modification, the toxic effects of SeMet often interfere with the preparation of protein derivatives containing this compound. We previously isolated a mutant strain (SMR-94) of the methylotrophic yeast Pichia pastoris that is resistant to both SeMet and selenate and demonstrated its applicability for the production of proteins suitable for X-ray crystallographic analysis. However, the molecular basis for resistance to SeMet by the SMR-94 strain remains unclear. Here, we report the characterization of SeMet-resistant mutants of Saccharomyces cerevisiae and the identification of a mutant allele of the MUP1 gene encoding high-affinity methionine permease, which confers SeMet resistance. Although the total methionine uptake by the mup1 mutant (the SRY5-7 strain) decreased to 47% of the wild-type level, it was able to incorporate SeMet into the overexpressed epidermal growth factor peptide with 73% occupancy, indicating the importance of the moderate uptake of SeMet by amino acid permeases other than Mup1p for the alleviation of SeMet toxicity. In addition, under standard culture conditions, the mup1 mutant showed higher productivity of the SeMet derivative relative to other SeMet-resistant mutants. Based on these results, we conclude that the mup1 mutant would be useful for the preparation of selenomethionyl proteins for X-ray crystallography.
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16

Sies, Helmut, Lars-Oliver Klotz, Victor S. Sharov, Annika Assmann, and Karlis Briviba. "Protection against Peroxynitrite by Selenoproteins." Zeitschrift für Naturforschung C 53, no. 3-4 (April 1, 1998): 228–32. http://dx.doi.org/10.1515/znc-1998-3-412.

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Abstract Cellular defense against excessive peroxynitrite generation is required to protect against DNA strand-breaks and mutations and against interference with protein tyrosine-based sig­ naling and other protein functions due to formation of 3-nitrotyrosine. We recently demon­ strated a role of selenium-containing enzymes catalyzing peroxynitrite reduction. Glutathione peroxidase (GPx) protected against the oxidation of dihydrorhodamine 123 (D H R) by perox­ ynitrite more effectively than ebselen (2-phenyl-1,2-benzisoselenazol-3(2H)-one), a selenoor-ganic compound exhibiting a high second-order rate constant for the reaction with peroxynit­ rite, 2 × 106 M-1 S-1. The maintenance of protection by GPx against peroxynitrite requires GSH as reductant. Similarly, selenomethionine but not selenomethionine oxide exhibited inhibition of rhodamine 123 formation from DHR caused by peroxynitrite. In steady-state experiments, in which peroxynitrite was infused to maintain a 0.2 μᴍ con­ centration, GPx in the presence of GSH, but neither GPx nor GSH alone, effectively inhib­ ited the hydroxylation of benzoate by peroxynitrite. Under these steady-state conditions peroxynitrite did not cause loss of ‘classical’ GPx activity. GPx, like selenomethionine, pro­ tected against protein 3-nitrotyrosine formation in human fibroblast lysates, shown in West­ern blots. The formation of nitrite rather than nitrate from peroxynitrite was enhanced by GPx , ebselen or selenomethionine. The selenoxides can be effectively reduced by glutathione, establishing a biological line of defense against peroxynitrite. The novel function of GPx as a peroxynitrite reductase may extend to other selenoproteins containing selenocysteine or selenomethionine. Recent work on organotellurium compounds revealed peroxynitrite reductase activity as well. Inhibition of dihydrorhodamine 123 oxidation correlated well with the GPx-like activity of a variety of diaryl tellurides.
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17

Turker, Omer, Kamil Kumanlioglu, Inanc Karapolat, and Ismail Dogan. "Selenium treatment in autoimmune thyroiditis: 9-month follow-up with variable doses." Journal of Endocrinology 190, no. 1 (July 2006): 151–56. http://dx.doi.org/10.1677/joe.1.06661.

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The aim of this study is to investigate the long-term (9 months) effects of variable doses (200/100 μg/day) of l-selenomethionine on autoimmune thyroiditis (AIT) and the parameters affecting the success rate of this therapy. The present study was designed in three steps: (1) 88 female patients with AIT (mean age = 40.1 ± 13.3 years) were randomized into two groups according to their initial serum TSH, thyroid peroxidase antibody (TPOAb) concentrations, and age. All the patients were receiving l-thyroxine to keep serum TSH ≤2 mIU/l. Group S2 (n = 48, mean TPOAb = 803.9 ± 483.8 IU/ml) received 200 μg l-selenomethionine per day, orally for 3 months, and group C (n = 40, mean TPOAb = 770.3 ± 406.2 IU/ml) received placebo. (2) 40 volunteers of group S2 were randomized into two age- and TPOAb-matched groups. Group S22 (n = 20) went on taking l-selenomethionine 200 μg/day, while others (group S21) lowered the dose to 100 μg/day. (3) 12 patients of group S22 (group S222) went on taking l-selenomethionine 200 μg/day, while 12 patients of group S21 (S212) increased the dose to 200 μg/day. Serum titers of TPOAb decreased significantly in group S2 (26.2%, P < 0.001), group S22 (23.7%, P < 0.01) and group S212 (30.3%, P < 0.01). There were no significant changes in group C and group S222 (P > 0.05). TPOAb titers increased significantly in group S21 (38.1%, P < 0.01). A significant decrease in thyroglobulin antibody titers was only noted in group S2 (5.2%, P < 0.01). l-selenomethionine substitution suppresses serum concentrations of TPOAb in patients with AIT, but suppression requires doses higher than 100 μg/day which is sufficient to maximize glutathione peroxidase activities. The suppression rate decreases with time.
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18

Baran, Enrique J. "Structural Data and Vibrational Spectra of the Copper(II) Complex of L-Selenomethionine." Zeitschrift für Naturforschung B 60, no. 6 (June 1, 2005): 663–66. http://dx.doi.org/10.1515/znb-2005-0609.

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A Cu(II) complex of the amino acid L-selenomethionine of stoichiometry Cu(L-SeMet)2, has been prepared and characterized. Crystallographic data were obtained by means of X-ray powder diffractometry and showed that the compound is isostructural with the related complex of L-methionine, Cu(L-Met)2. The structural analogy is also supported by the analysis of the IR and Raman spectra of the complex, which are briefly discussed in comparison with those of free L-selenomethionine.
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19

Abrams, M. M., C. Shennan, R. J. Zasoski, and R. G. Burau. "Selenomethionine Uptake by Wheat Seedlings." Agronomy Journal 82, no. 6 (November 1990): 1127–30. http://dx.doi.org/10.2134/agronj1990.00021962008200060021x.

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20

RAFFERTY, Teresa S., Roderick C. McKENZIE, John A. A. HUNTER, A. Forbes HOWIE, John R. ARTHUR, Fergus NICOL, and Geoff J. BECKETT. "Differential expression of selenoproteins by human skin cells and protection by selenium from UVB-radiation-induced cell death." Biochemical Journal 332, no. 1 (May 15, 1998): 231–36. http://dx.doi.org/10.1042/bj3320231.

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The generation of reactive oxygen species has been implicated as part of the mechanism responsible for UVB-radiation-induced skin damage. In mice, evidence suggests that increased dietary selenium intake may protect skin from many of the harmful effects of UVB radiation. We sought to determine the selenoprotein profile of cultured human skin cells and whether selenium supplementation could protect keratinocytes and melanocytes from the lethal effects of UVB radiation. Labelling experiments using [75Se]selenite showed qualitative and quantitative differences in selenoprotein expression by human fibroblasts, keratinocytes and melanocytes. This was most noticeable for thioredoxin reductase (60 kDa) and phospholipid glutathione peroxidase (21 kDa); these proteins were identified by Western blotting. Despite these differences, we found that a 24 h preincubation with sodium selenite or selenomethionine protected both cultured human keratinocytes and melanocytes from UVB-induced cell death. With primary keratinocytes, the greatest reduction in cell death was found with 10 nM sodium selenite (79% cell death reduced to 21.7%; P< 0.01) and with 50 nM selenomethionine (79% cell death reduced to 13.2%; P< 0.01). Protection could be obtained with concentrations as low as 1 nM with sodium selenite and 10 nM with selenomethionine. When selenium was added after UVB radiation, little protection could be achieved, with cell death only being reduced from 88.5% to about 50% with both compounds. In all of the experiments sodium selenite was more potent than selenomethionine at providing protection from UVB radiation.
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21

Thomson, Christine D., Marion F. Robinson, Judy A. Butler, and Phllip D. Whanger. "Long-term supplementation with selenate and selenomethionine: Selenium and glutathione peroxidase (EC1.11.1.9) in blood components of New Zealand women." British Journal of Nutrition 69, no. 2 (March 1993): 577–88. http://dx.doi.org/10.1079/bjn19930057.

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Thirty-three New Zealand women aged 18–23 years received daily for 32 weeks, 200 μg Se as Seenriched yeast (selenomethionine), or brewer's yeast mixed with selenate, or no added Se (placebo) in a double-blind trial. Se supplementation raised (P= 0.001), platelet glutathione peroxidase (EC1.11.1.9; GSHPx) activity, and also Se and GSHPx in whole blood, erythrocytes and plasma. Selenomethionine was more effective in raising blood Se concentrations than selenate, but both were equally effective in raising GSHPx activities in whole blood, erythrocytes and plasma, indicating a similar bioavailability for the two forms. These observations and those of gel filtration studies of erythrocytes and plasma proteins reported elsewhere (Butleret al.1991) are consistent with the incorporation of Se from selenomethionine into a general tissue protein pool while selenate is directly available for GSHPx synthesis, and explain the poorer correlation between Se and GSHPx in individuals with higher Se status. However, selenate raised platelet GSHPx activities to a greater extent than did selenomethionine suggesting some other effect of selenate on platelets which needs further investigation. A response of GSHPx activity in these New Zealand subjects indicates that their dietary Se intake is insufficient to meet recommended intakes based on the criterion of saturation of GSHPx activity, and could reflect a marginal Se status. The level of blood Se necessary for saturation of GSHPx of about 100 ng Se/ml whole blood confirms observations in earlier studies.
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22

Hosfield, Christopher M., Qilu Ye, J. Simon C. Arthur, Carol Hegadorn, Dorothy E. Croall, John S. Elce, and Zongchao Jia. "Crystallization and X-ray crystallographic analysis of m-calpain, a Ca2+-dependent protease." Acta Crystallographica Section D Biological Crystallography 55, no. 8 (August 1, 1999): 1484–86. http://dx.doi.org/10.1107/s0907444999007386.

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The absolute requirement of Ca2+ for proteolytic activity is a feature unique to the calpains, a family of heterodimeric cysteine proteases. Conditions are described which give rise to diffraction-quality crystals of m-calpain in two crystal forms, P1 and P21. Data have been collected from native crystals of m-calpain in both P1 and P21 forms, to 2.6 and 2.15 Å, respectively. Selenomethionine-containing crystals have been grown in both forms, and anomalous data from the P21 selenomethionine enzyme provided the location of 17 of the 19 Se atoms in the protein.
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Hamzah, Muhaimin, Muhammad Agus Suprayudi, Nur Bambang Priyo Utomo, and Wasmen Manalu. "Growth and viability of juvenile humpback grouper (Cromileptes altivelis) supplemented with inorganic and organic selenium." Jurnal Akuakultur Indonesia 11, no. 2 (November 14, 2013): 141. http://dx.doi.org/10.19027/jai.11.141-152.

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<p>This study was conducted to determine the effects of inorganic selenium (sodium selenite) and organic selenium (selenomethionine) supplementation on growth and viability of juvenile humpback grouper (Cromileptes altivelis). The experiment was designed as a completely randomized design with eight treatments and three replications. The treatment being tested was source and dosages of selenium ie., inorganic selenium (sodium selenite) supplementation with dosages of 0.5, 1, 2, and 4 mg Se/kg diet and organic selenium (selenomethionine) with dosages of 1, 2, and 4 mg Se/kg diet. Another treatment was unsupplemented selenium. Juveniles humpback grouper at an initial average length of 6,39±0,41 cm and body weight of 4,49±0,65 g were reared in 90×40×35 cm3 aquaria and fed artificial diet (pellet) two times daily (08.00 and 16.00) at satiation. Fishes were reared for 40 days at a stocking density of 12 fish per aquarium on sea water with salinity of 30–31 ppt and temperature of 28–29 °C. The results of this study showed that the source of selenium supplementation (inorganic or organic) affected growth performance, glutathione peroxidase (GPx) enzyme activity, and blood profiles of the experimental fish. Generally, it was found that selenomethionine supplementation resulted in better fish performance than sodium selenite. In sodium selenite supplementation, survival declined with the increased dosages of Se in the diet, and the supplementation at dosage of 0,5 mg Se/kg diet showed a toxic effects. Histopatological test showed that there were damage in livers, kidneys, and intestines of fish supplemented with sodium selenite from 0.5 to 4 mg Se/kg diet. On the contrary, supplementation of selenomethionine up to 4 mg Se/kg did not show any signs of toxicity and the survival was on 86.11 to 97.22%. Feed efficiency, protein retention, lipid retention, and Se retention indicated that a dosage of 4 mg Se/kg selenomethionine supplementation was the best dosage.</p><p>Keywords: selenium, viability, growth, Cromileptes altivelis, humpback grouper</p>
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Krysiak, Robert, Witold Szkróbka, and Bogusław Okopień. "The Effect of Hypolipidemic Agents on Thyroid Autoimmunity in Women with Hashimoto’s Thyroiditis Treated with Levothyroxine and Selenomethionine." Experimental and Clinical Endocrinology & Diabetes 126, no. 05 (November 8, 2017): 321–26. http://dx.doi.org/10.1055/s-0043-120342.

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Abstract Background Levothyroxine and selenomethionine were found to reduce thyroid antibody titers in patients with Hashimoto’s thyroiditis. The same effect was produced by intensive statin therapy. The aim of the present study was to assess whether hypolipidemic agents modulate the impact of thyroid hormone supplementation and selenomethionine on thyroid autoimmunity. Methods The study included 62 women with Hashimoto's thyroiditis treated for at least 6 months with levothyroxine and selenomethionine. On the basis of plasma lipids, women were divided into three groups: women with isolated hypercholesterolemia (group A; n=20), women with isolated hypertriglyceridemia (group B; n=17), and women with normal plasma lipids (group C; n=25). Group A were then treated with atorvastatin (20 mg daily), while group B received micronized fenofibrate (200 mg daily). Serum titers of thyroid peroxidase and thyroglobulin antibodies, as well as serum levels of thyrotropin, free thyroxine and free triiodothyronine were measured at the beginning of the study and 6 months later. Results Fenofibrate decreased triglycerides and increased HDL cholesterol, while simvastatin decreased total and LDL cholesterol. Fenofibrate reduced titers of thyroid peroxidase and, to a lesser extent, thyroglobulin antibodies. Atorvastatin tended to increase thyroid peroxidase antibodies. No changes in thyrotropin, free thyroxine and free triiodothyronine were observed in any treatment group. Fenofibrate-induced changes in thyroid antibody titers correlated with baseline antibody titers, as well as with treatment-induced changes in HDL cholesterol and insulin sensitivity. Conclusions The obtained results indicate that only fibrates may potentiate the effect of selenomethionine and levothyroxine on thyroid autoimmunity in women.
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Liu, Mengjie, Xinqi Liu, Hongmei Zeng, and Dewen Qiu. "Purification, crystallization and preliminary X-ray diffraction analysis of effector protein MoHrip2 fromMagnaporthe oryzae." Acta Crystallographica Section F Structural Biology and Crystallization Communications 69, no. 4 (March 29, 2013): 463–67. http://dx.doi.org/10.1107/s1744309113007094.

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MoHrip2, a novel effector protein from the pathogenic fungusMagnaporthe oryzae, was purified and crystallized using the sitting-drop vapour-diffusion method. Native crystals and selenomethionine-labelled crystals were obtained using 2.2 Mammonium sulfate as a precipitant. A native data set was collected to 2.0 Å resolution at 100 K using an in-house X-ray source and a selenomethionine-labelled data set containing anomalous signal was collected to 1.8 Å resolution at 100 K using a synchrotron source. Based on the anomalous signal generated from the Se atom, the MoHrip2 structure was successfully solved using the single-wavelength anomalous dispersion (SAD) method.
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26

Isab, Anvarhusein A., and Mohamed I. M. Wazeer. "A13C NMR study of the interactions of Ag13CN and Ag(CN)2–with thiomalic acid, L-methionine and DL-selenomethionine." Spectroscopy 19, no. 5,6 (2005): 275–81. http://dx.doi.org/10.1155/2005/850959.

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Complexation of Ag+as AgNO3, solid AgCN and Ag(CN)2–by labeled and unlabeled L-methionine, DL-selenomethionine and d,l-thiomalate were studied by nuclear magnetic resonance methods. The13C NMR indicates that only Ag+react with the both L-methionine, DL-selenomethionine at neutral and higher pH via CO2–and S or Se atom forming a chelate. The Ag(CN)2–and AgCN do not bind to either of these two ligands at any pH. The Ag13CN, which is an insoluble polymer, can react with thiomalate to form chelate complexes at neutral pH. Various structures for the chelate formations are proposed.
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Mintzer, Mary Rose, Thomas Troxler, and Feng Gai. "p-Cyanophenylalanine and selenomethionine constitute a useful fluorophore–quencher pair for short distance measurements: application to polyproline peptides." Physical Chemistry Chemical Physics 17, no. 12 (2015): 7881–87. http://dx.doi.org/10.1039/c5cp00050e.

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28

Barbé, F., E. Chevaux, M. Castex, G. Elcoso, and A. Bach. "Comparison of selenium bioavailability in milk and serum in dairy cows fed different sources of organic selenium." Animal Production Science 60, no. 2 (2020): 269. http://dx.doi.org/10.1071/an18719.

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Context Selenium (Se) bioavailability is an important parameter to consider when supplementing trace minerals to optimise animal health and performance. Aims To assess the biological transfer of Se in milk and serum of three sources of organic Se in dairy cattle: two different pure selenomethionines (SM1, SM2) and Se-yeast (SY) containing selenomethionine, selenocysteine and other forms of organic Se. Methods Forty-five lactating Holstein dairy cows were randomly distributed in nine groups (three sources of organic Se supplemented at three doses: 0.1, 0.2 and 0.3 ppm organic Se in addition to 0.3 ppm of inorganic Se) and the Se concentrations in milk and serum were analysed at different times over 34 days of supplementation. Dry matter intake, milk yield, as well as milk fat and protein contents were recorded daily for each cow. Selenium bioavailability in milk was assessed as the ratio between amount of Se secreted in milk and amount of Se consumed. Key results The lowest Se dose (0.1 ppm), independent of source, did not allow detection a different pattern of transfer into milk and serum, suggesting that at this level, the Se supplied was mainly used to cover the animal needs. Supplementing SY at 0.2 and 0.3 ppm resulted in the most consistent secretion of Se into milk, whereas SM2 was most effective at increasing serum Se concentrations. Conclusions At the supplementing doses of 0.2 and 0.3 ppm, SY elicits an increased transfer of Se into milk concentrations compared with SM1 and SM2, whereas SM2 induces the greatest increase in Se serum concentrations. Implications SY is more effective than SM1 and SM2 at increasing Se transfer into milk. Supplementation of SM2 induces a pattern of Se transfer into milk and serum that differs from the other Se sources suggesting a different metabolism of this particular Se source.
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Ogra, Yasumitsu, Maya Shimizu, Kazuaki Takahashi, and Yasumi Anan. "Biotransformation of organic selenium compounds in budding yeast,Saccharomyces cerevisiae." Metallomics 10, no. 9 (2018): 1257–63. http://dx.doi.org/10.1039/c8mt00176f.

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Ogra, Yasumitsu, Yurie Ogihara, and Yasumi Anan. "Comparison of the metabolism of inorganic and organic selenium species between two selenium accumulator plants, garlic and Indian mustard." Metallomics 9, no. 1 (2017): 61–68. http://dx.doi.org/10.1039/c6mt00128a.

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Katarzyna, Bierla, Rachel M. Taylor, Joanna Szpunar, Ryszard Lobinski, and Roger A. Sunde. "Identification and determination of selenocysteine, selenosugar, and other selenometabolites in turkey liver." Metallomics 12, no. 5 (2020): 758–66. http://dx.doi.org/10.1039/d0mt00040j.

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32

Tang, Jia-Yong, Long-Qiong Wang, Gang Jia, Guang-Mang Liu, Xiao-Ling Chen, Gang Tian, Jing-Yi Cai, Hai-Ying Shang, and Hua Zhao. "The hydroxy-analogue of selenomethionine alleviated lipopolysaccharide-induced inflammatory responses is associated with recover expression of several selenoprotein encoding genes in the spleens of Kunming mice." RSC Advances 9, no. 69 (2019): 40462–70. http://dx.doi.org/10.1039/c9ra07260h.

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Zhang, Zhong-Hao, Chen Chen, Qiu-Yan Wu, Rui Zheng, Qiong Liu, Jia-Zuan Ni, Peter R. Hoffmann, and Guo-Li Song. "Selenomethionine reduces the deposition of beta-amyloid plaques by modulating β-secretase and enhancing selenoenzymatic activity in a mouse model of Alzheimer's disease." Metallomics 8, no. 8 (2016): 782–89. http://dx.doi.org/10.1039/c6mt00117c.

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34

Tamás, M., and J. Csapó. "Examination of the selenium content of wheat grasses produced in different soil types in Csik Basin." Acta Universitatis Sapientiae, Alimentaria 8, no. 1 (January 1, 2015): 30–44. http://dx.doi.org/10.1515/ausal-2015-0002.

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Abstract In the course of the research, we determined selenium and dry matter content of 35 wheat grass and 35 wheat seed samples. The selenium content of the preparation plant probes was measured by spectrofluorimetric determination (λexcitation = 380 nm, λemission = 519 nm) of the resulted piazselenol complex. It was established that between the selenium content of the wheat grass and wheat seed the correlation coefficient was 0.36 at p = 0.05 level, which indicates a medium-close correlation. Similarly, there was a medium-close correlation between the selenium content of the wheat grass calculated on dry-matter basis and total selenium content of the wheat, with a correlation coefficient of 0.40 at p = 0.02 level. Afterwards, beside the selenium content, we measured the selenomethionine content by ion-exchange chromatography and highperformance liquid chromatography, and the organic selenium content was calculated. A very close correlation was established between the total selenium, selenomethionine and calculated organic selenium content of wheat (the correlation coefficients were between 0.92 and 0.99 at p = 0.01 level). The correlation between the selenomethionine content of wheat grass and wheat seed was very weak (r = 0.23).
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Wu, WenYu, Xiangkai Zhen, and Ning Shi. "DNA-binding domain of myelin-gene regulatory factor: purification, crystallization and X-ray analysis." Acta Crystallographica Section F Structural Biology Communications 73, no. 7 (June 17, 2017): 393–97. http://dx.doi.org/10.1107/s2053230x17007828.

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The myelin sheath, which envelops axons in the vertebrate central nervous system, is crucial for the rapid conduction of action potentials. Myelin-gene regulatory factor (MRF) is a recently identified transcription factor that is required for myelin-sheath formation. Loss of MRF leads to demyelinating diseases and motor learning deficiency. MRF is a membrane-bound transcription factor that undergoes autocleavage from the endoplasmic reticulum membrane. The N-terminus of MRF contains a DNA-binding domain (DBD) that functions as a homotrimer. In this study, the MRF DBD was cloned, purified and crystallized in order to understand the molecular mechanism that regulates the transcription of myelin genes. Selenomethionine was subsequently introduced into the crystals to obtain the phases for the MRF DBD structure. The native and selenomethionine-labelled crystals exhibited diffraction to 2.50 and 2.51 Å resolution, respectively. The crystals belonged to space groupP321 and the selenomethionine-labelled crystals had unit-cell parametersa= 104.0,b= 104.0,c= 46.7 Å, α = 90, β = 90, γ = 120°. The calculated Matthews coefficient was 3.04 Å3Da−1and the solvent content was 59.5%, indicating the presence of one MRF DBD molecule in the asymmetric unit.
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Dauplais, Marc, Katarzyna Bierla, Coralie Maizeray, Roxane Lestini, Ryszard Lobinski, Pierre Plateau, Joanna Szpunar, and Myriam Lazard. "Methylselenol Produced In Vivo from Methylseleninic Acid or Dimethyl Diselenide Induces Toxic Protein Aggregation in Saccharomyces cerevisiae." International Journal of Molecular Sciences 22, no. 5 (February 24, 2021): 2241. http://dx.doi.org/10.3390/ijms22052241.

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Methylselenol (MeSeH) has been suggested to be a critical metabolite for anticancer activity of selenium, although the mechanisms underlying its activity remain to be fully established. The aim of this study was to identify metabolic pathways of MeSeH in Saccharomyces cerevisiae to decipher the mechanism of its toxicity. We first investigated in vitro the formation of MeSeH from methylseleninic acid (MSeA) or dimethyldiselenide. Determination of the equilibrium and rate constants of the reactions between glutathione (GSH) and these MeSeH precursors indicates that in the conditions that prevail in vivo, GSH can reduce the major part of MSeA or dimethyldiselenide into MeSeH. MeSeH can also be enzymatically produced by glutathione reductase or thioredoxin/thioredoxin reductase. Studies on the toxicity of MeSeH precursors (MSeA, dimethyldiselenide or a mixture of MSeA and GSH) in S.cerevisiae revealed that cytotoxicity and selenomethionine content were severely reduced in a met17 mutant devoid of O-acetylhomoserine sulfhydrylase. This suggests conversion of MeSeH into selenomethionine by this enzyme. Protein aggregation was observed in wild-type but not in met17 cells. Altogether, our findings support the view that MeSeH is toxic in S. cerevisiae because it is metabolized into selenomethionine which, in turn, induces toxic protein aggregation.
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37

Frénois, Frédéric, Pierre Legrand, and Sébastien Fribourg. "Sqt1p is an eight-bladed WD40 protein." Acta Crystallographica Section F Structural Biology Communications 72, no. 1 (January 1, 2016): 59–64. http://dx.doi.org/10.1107/s2053230x15024097.

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Ribosome biogenesis in eukaryotes is a complex and highly orchestrated process involving more than 200 accessory factors in addition to ribosomal RNAs and ribosomal proteins. Among the many factors involved, Sqt1p has been reported to specifically bind to uL16 and to act as a chaperone. The crystal structure of full-length Sqt1p from the yeastSaccharomyces cerevisiaehas been solved at 3.35 Å resolution. A SAD experiment at the Se Kedge and an S-SAD experiment on the same selenomethionine-substituted protein crystal allowed unambiguous positioning of the selenomethionine and Cys residues. On the basis of the atomic structure of Sqt1p, the potential residues involved in uL16 interaction were identified and tested.
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38

Brumbaugh, William G., and Michael J. Walther. "Improved Selenium Recovery from Tissue with Modified Sample Decomposition." Journal of AOAC INTERNATIONAL 74, no. 3 (May 1, 1991): 570–71. http://dx.doi.org/10.1093/jaoac/74.3.570.

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Abstract The present paper describes a simple modification of a recently reported decomposition method for determination of selenium In biological tissue by hydride generation atomic absorption. The modified method yielded slightly higher selenium recoveries (3-4%) for selected reference tissues and fish tissue spiked with selenomethionine. Radiotracer experiments indicated that the addition of a small volume of hydrochloric acid to the wet digestate mixture reduced slight losses of selenium as the sample initially went to dryness before ashing. With the modified method, selenium spiked as selenomethionine behaved more like the selenium in reference tissues than did the inorganic spike forms when this digestion modification was used
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39

Peran, Ivan, Matthew D. Watson, Osman Bilsel, and Daniel P. Raleigh. "Selenomethionine, p-cyanophenylalanine pairs provide a convenient, sensitive, non-perturbing fluorescent probe of local helical structure." Chemical Communications 52, no. 10 (2016): 2055–58. http://dx.doi.org/10.1039/c5cc08232c.

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40

Rui, WANG, BAI Yan, LIANG Zhi-Hong, LIU Ying, HUANG Li-Li, and ZHENG Wen-Jie. "Interaction between Selenomethionine and Copper Ions." Acta Physico-Chimica Sinica 26, no. 12 (2010): 3225–29. http://dx.doi.org/10.3866/pku.whxb20101213.

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41

Assmann, Annika, Marija Bonifačić, Karlis Briviba, Helmut Sies, and Klaus-Dieter Asmus. "One-electron reduction of selenomethionine oxide." Free Radical Research 32, no. 4 (January 2000): 371–76. http://dx.doi.org/10.1080/10715760000300371.

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42

Yasumoto, Kyoden, Tetsuya Suzuki, and Munehiro Yoshida. "Identification of selenomethionine in soybean protein." Journal of Agricultural and Food Chemistry 36, no. 3 (May 1988): 463–67. http://dx.doi.org/10.1021/jf00081a014.

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43

KOCH, T., and O. BUCHARDT. "ChemInform Abstract: Synthesis of L-(+)-Selenomethionine." ChemInform 25, no. 13 (August 19, 2010): no. http://dx.doi.org/10.1002/chin.199413236.

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44

Choy, Wai Nang, Calvin C. Willhite, Matthew J. Cukierski, and Steven A. Book. "Primate Micronucleus Study of L-Selenomethionine." Environmental and Molecular Mutagenesis 14, no. 2 (1989): 123–25. http://dx.doi.org/10.1002/em.2850140208.

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45

Kitajima, Toshihiko, Yoshifumi Jigami, and Yasunori Chiba. "Cytotoxic Mechanism of Selenomethionine in Yeast." Journal of Biological Chemistry 287, no. 13 (February 6, 2012): 10032–38. http://dx.doi.org/10.1074/jbc.m111.324244.

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46

Wolf, W. R., H. Zainal, and B. Yager. "Selenomethionine content of candidate reference materials." Fresenius' Journal of Analytical Chemistry 370, no. 2-3 (June 1, 2001): 286–90. http://dx.doi.org/10.1007/s002160100829.

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47

Bai, Yan, Tingting Wang, Ying Liu, and Wenjie Zheng. "Electrochemical oxidation of selenocystine and selenomethionine." Colloids and Surfaces B: Biointerfaces 74, no. 1 (November 2009): 150–53. http://dx.doi.org/10.1016/j.colsurfb.2009.07.010.

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48

Kajander, E. Olavi, Raija-Leena Pajula, Rauno J. Harvima, and Terho O. Eloranta. "Synthesis and analysis of selenomethionine metabolites." Analytical Biochemistry 179, no. 2 (June 1989): 396–400. http://dx.doi.org/10.1016/0003-2697(89)90151-6.

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49

Plenevaux, A., R. Cantineau, M. Guillaume, L. Christiaens, and G. Tihange. "Fast chemical synthesis of [75Sel-selenomethionine." International Journal of Radiation Applications and Instrumentation. Part A. Applied Radiation and Isotopes 38, no. 1 (January 1987): 59–61. http://dx.doi.org/10.1016/0883-2889(87)90237-1.

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50

Kieliszek, Marek, and Stanisław Błażejak. "Speciation Analysis of Selenium in Candida utilis Yeast Cells Using HPLC-ICP-MS and UHPLC-ESI-Orbitrap MS Techniques." Applied Sciences 8, no. 11 (October 25, 2018): 2050. http://dx.doi.org/10.3390/app8112050.

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Selenium plays a key role in the proper metabolism of living organisms. The search for new selenium compounds opens up new possibilities for understanding selenometabolome in yeast cells. This study was aimed at the identification of compounds containing selenium in the feed yeasts Candida utilis ATCC 9950. Yeast biomass was kept in aqueous solutions enriched with inorganic selenium (20 mg·L−1) for 24 h. Speciation analysis of the element was performed using the HPLC-ICP-MS and UHPLC-ESI-Orbitrap MS techniques. The obtained selenium value in the yeast was 629 μg·g−1, while the selenomethionine value was 31.57 μg·g−1. The UHPLC-ESI-Orbitrap MS analysis conducted allowed for the identification of six selenium compounds: dehydro-selenomethionine-oxide, selenomethionine, selenomethionine-NH3, a Se-S conjugate of selenoglutathione-cysteine, methylthioselenoglutathione, and 2,3-DHP-selenocysteine-cysteine. In order to explain the structure of selenium compounds, the selected ions were subjected to fragmentation. The selenium compounds obtained with a low mass play a significant role in the metabolism of the compound. However, the bioavailability of such components and their properties have not been fully understood. The number of signals indicating the presence of selenium compounds obtained using the UHPLC-ESI-Orbitrap MS method was characterized by higher sensitivity than when using the HPLC-ICP-MS method. The obtained results will expand upon knowledge about the biotransformation of selenium in eukaryotic yeast cells. Future research should focus on understanding the entire selenium metabolism in cells and on the search for new transformation pathways for this element. This opens up new possibilities for obtaining functional food, rich in easily absorbable selenium sources, and constituting an alternative to dietary supplements based on this compound found primarily in inorganic form.
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