Gotowe bibliografie tematyczne / Selenoproteins

Gotowa bibliografia na temat „Selenoproteins”

Autor: Grafiati
Data publikacji: 4 czerwca 2021
Data aktualizacji: 23 lutego 2023

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Artykuły w czasopismach na temat "Selenoproteins"

1

Ghuge, Sandip A., Ulhas Sopanrao Kadam i Jong Chan Hong. "Selenoprotein: Potential Player in Redox Regulation in Chlamydomonas reinhardtii". Antioxidants 11, nr 8 (22.08.2022): 1630. http://dx.doi.org/10.3390/antiox11081630.

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Selenium (Se) is an essential micro-element for many organisms, including Chlamydomonas reinhardtii, and is required in trace amounts. It is obtained from the 21st amino acid selenocysteine (Sec, U), genetically encoded by the UGA codon. Proteins containing Sec are known as selenoproteins. In eukaryotes, selenoproteins are present in animals and algae, whereas fungi and higher plants lack them. The human genome contains 25 selenoproteins, most of which are involved in antioxidant defense activity, redox regulation, and redox signaling. In algae, 42 selenoprotein families were identified using various bioinformatics approaches, out of which C. reinhardtii is known to have 10 selenoprotein genes. However, the role of selenoproteins in Chlamydomonas is yet to be reported. Chlamydomonas selenoproteins contain conserved domains such as CVNVGC and GCUG, in the case of thioredoxin reductase, and CXXU in other selenoproteins. Interestingly, Sec amino acid residue is present in a catalytically active domain in Chlamydomonas selenoproteins, similar to human selenoproteins. Based on catalytical active sites and conserved domains present in Chlamydomonas selenoproteins, we suggest that Chlamydomonas selenoproteins could have a role in redox regulation and defense by acting as antioxidants in various physiological conditions.
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2

Dery, L., P. Sai Reddy, S. Dery, R. Mousa, O. Ktorza, A. Talhami i N. Metanis. "Accessing human selenoproteins through chemical protein synthesis". Chemical Science 8, nr 3 (2017): 1922–26. http://dx.doi.org/10.1039/c6sc04123j.

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The human body contains 25 selenoproteins, but challenges in their preparations have prevented biological characterizations thus far. Here we report the first total chemical syntheses of two human selenoproteins, selenoprotein M (SELM) and selenoprotein W (SELW).
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3

Sengupta, Aniruddha, Bradley A. Carlson, James A. Weaver, Sergey V. Novoselov, Dmitri E. Fomenko, Vadim N. Gladyshev i Dolph L. Hatfield. "A functional link between housekeeping selenoproteins and phase II enzymes". Biochemical Journal 413, nr 1 (12.06.2008): 151–61. http://dx.doi.org/10.1042/bj20080277.

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Sec (selenocysteine) is biosynthesized on its tRNA and incorporated into selenium-containing proteins (selenoproteins) as the 21st amino acid residue. Selenoprotein synthesis is dependent on Sec tRNA and the expression of this class of proteins can be modulated by altering Sec tRNA expression. The gene encoding Sec tRNA (Trsp) is a single-copy gene and its targeted removal in liver demonstrated that selenoproteins are essential for proper function wherein their absence leads to necrosis and hepatocellular degeneration. In the present study, we found that the complete loss of selenoproteins in liver was compensated for by an enhanced expression of several phase II response genes and their corresponding gene products. The replacement of selenoprotein synthesis in mice carrying mutant Trsp transgenes, wherein housekeeping, but not stress-related selenoproteins are expressed, led to normal expression of phase II response genes. Thus the present study provides evidence for a functional link between housekeeping selenoproteins and phase II enzymes.
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Capone, Francesca, Andrea Polo, Angela Sorice, Alfredo Budillon i Susan Costantini. "Integrated Analysis to Study the Relationship between Tumor-Associated Selenoproteins: Focus on Prostate Cancer". International Journal of Molecular Sciences 21, nr 18 (13.09.2020): 6694. http://dx.doi.org/10.3390/ijms21186694.

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Selenoproteins are proteins that contain selenium within selenocysteine residues. To date, twenty-five mammalian selenoproteins have been identified; however, the functions of nearly half of these selenoproteins are unknown. Although alterations in selenoprotein expression and function have been suggested to play a role in cancer development and progression, few detailed studies have been carried out in this field. Network analyses and data mining of publicly available datasets on gene expression levels in different cancers, and the correlations with patient outcome, represent important tools to study the correlation between selenoproteins and other proteins present in the human interactome, and to determine whether altered selenoprotein expression is cancer type-specific, and/or correlated with cancer patient prognosis. Therefore, in the present study, we used bioinformatics approaches to (i) build up the network of interactions between twenty-five selenoproteins and identify the most inter-correlated proteins/genes, which are named HUB nodes; and (ii) analyze the correlation between selenoprotein gene expression and patient outcome in ten solid tumors. Then, considering the need to confirm by experimental approaches the correlations suggested by the bioinformatics analyses, we decided to evaluate the gene expression levels of the twenty-five selenoproteins and six HUB nodes in androgen receptor-positive (22RV1 and LNCaP) and androgen receptor–negative (DU145 and PC3) cell lines, compared to human nontransformed, and differentiated, prostate epithelial cells (EPN) by RT-qPCR analysis. This analysis confirmed that the combined evaluation of some selenoproteins and HUB nodes could have prognostic value and may improve patient outcome predictions.
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Santesmasses, Didac, i Vadim N. Gladyshev. "Pathogenic Variants in Selenoproteins and Selenocysteine Biosynthesis Machinery". International Journal of Molecular Sciences 22, nr 21 (27.10.2021): 11593. http://dx.doi.org/10.3390/ijms222111593.

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Selenium is incorporated into selenoproteins as the 21st amino acid selenocysteine (Sec). There are 25 selenoproteins encoded in the human genome, and their synthesis requires a dedicated machinery. Most selenoproteins are oxidoreductases with important functions in human health. A number of disorders have been associated with deficiency of selenoproteins, caused by mutations in selenoprotein genes or Sec machinery genes. We discuss mutations that are known to cause disease in humans and report their allele frequencies in the general population. The occurrence of protein-truncating variants in the same genes is also presented. We provide an overview of pathogenic variants in selenoproteins genes from a population genomics perspective.
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6

Shimada, Briana K., Sydonie Swanson, Pamela Toh i Lucia A. Seale. "Metabolism of Selenium, Selenocysteine, and Selenoproteins in Ferroptosis in Solid Tumor Cancers". Biomolecules 12, nr 11 (28.10.2022): 1581. http://dx.doi.org/10.3390/biom12111581.

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A potential target of precision nutrition in cancer therapeutics is the micronutrient selenium (Se). Se is metabolized and incorporated as the amino acid selenocysteine (Sec) into 25 human selenoproteins, including glutathione peroxidases (GPXs) and thioredoxin reductases (TXNRDs), among others. Both the processes of Se and Sec metabolism for the production of selenoproteins and the action of selenoproteins are utilized by cancer cells from solid tumors as a protective mechanism against oxidative damage and to resist ferroptosis, an iron-dependent cell death mechanism. Protection against ferroptosis in cancer cells requires sustained production of the selenoprotein GPX4, which involves increasing the uptake of Se, potentially activating Se metabolic pathways such as the trans-selenation pathway and the TXNRD1-dependent decomposition of inorganic selenocompounds to sustain GPX4 synthesis. Additionally, endoplasmic reticulum-resident selenoproteins also affect apoptotic responses in the presence of selenocompounds. Selenoproteins may also help cancer cells adapting against increased oxidative damage and the challenges of a modified nutrient metabolism that result from the Warburg switch. Finally, cancer cells may also rewire the selenoprotein hierarchy and use Se-related machinery to prioritize selenoproteins that are essential to the adaptations against ferroptosis and oxidative damage. In this review, we discuss both the evidence and the gaps in knowledge on how cancer cells from solid tumors use Se, Sec, selenoproteins, and the Se-related machinery to promote their survival particularly via resistance to ferroptosis.
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7

Zhang, Ying, Yeon Jin Roh, Seong-Jeong Han, Iha Park, Hae Min Lee, Yong Sik Ok, Byung Cheon Lee i Seung-Rock Lee. "Role of Selenoproteins in Redox Regulation of Signaling and the Antioxidant System: A Review". Antioxidants 9, nr 5 (5.05.2020): 383. http://dx.doi.org/10.3390/antiox9050383.

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Selenium is a vital trace element present as selenocysteine (Sec) in proteins that are, thus, known as selenoproteins. Humans have 25 selenoproteins, most of which are functionally characterized as oxidoreductases, where the Sec residue plays a catalytic role in redox regulation and antioxidant activity. Glutathione peroxidase plays a pivotal role in scavenging and inactivating hydrogen and lipid peroxides, whereas thioredoxin reductase reduces oxidized thioredoxins as well as non-disulfide substrates, such as lipid hydroperoxides and hydrogen peroxide. Selenoprotein R protects the cell against oxidative damage by reducing methionine-R-sulfoxide back to methionine. Selenoprotein O regulates redox homeostasis with catalytic activity of protein AMPylation. Moreover, endoplasmic reticulum (ER) membrane selenoproteins (SelI, K, N, S, and Sel15) are involved in ER membrane stress regulation. Selenoproteins containing the CXXU motif (SelH, M, T, V, and W) are putative oxidoreductases that participate in various cellular processes depending on redox regulation. Herein, we review the recent studies on the role of selenoproteins in redox regulation and their physiological functions in humans, as well as their role in various diseases.
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8

Stanishevska, N. V. "Selenoproteins and their emerging roles in signaling pathways". Regulatory Mechanisms in Biosystems 11, nr 2 (23.04.2020): 186–99. http://dx.doi.org/10.15421/022028.

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The functional activity of selenoproteins has a wide range of effects on complex pathogenetic processes, including teratogenesis, immuno-inflammatory, neurodegenerative. Being active participants and promoters of many signaling pathways, selenoproteins support the lively interest of a wide scientific community. This review is devoted to the analysis of recent data describing the participation of selenoproteins in various molecular interactions mediating important signaling pathways. Data processing was carried out by the method of complex analysis. For convenience, all selenoproteins were divided into groups depending on their location and function. Among the group of selenoproteins of the ER membrane, selenoprotein N affects the absorption of Ca2+ by the endoplasmic reticulum mediated by oxidoreductin (ERO1), a key player in the CHOP/ERO1 branch, a pathogenic mechanism that causes myopathy. Another selenoprotein of the ER membrane selenoprotein K binding to the DHHC6 protein affects the IP3R receptor that regulates Ca2+ flux. Selenoprotein K is able to affect another protein of the endoplasmic reticulum CHERP, also appearing in Ca2+ transport. Selenoprotein S, associated with the lumen of ER, is able to influence the VCP protein, which ensures the incorporation of selenoprotein K into the ER membrane. Selenoprotein M, as an ER lumen protein, affects the phosphorylation of STAT3 by leptin, which confirms that Sel M is a positive regulator of leptin signaling. Selenoprotein S also related to luminal selenoproteins ER is a modulator of the IRE1α-sXBP1 signaling pathway. Nuclear selenoprotein H will directly affect the suppressor of malignant tumours, p53 protein, the activation of which increases with Sel H deficiency. The same selenoprotein is involved in redox regulation. Among the cytoplasmic selenoproteins, abundant investigations are devoted to SelP, which affects the PI3K/Akt/Erk signaling pathway during ischemia/reperfusion, is transported into the myoblasts through the plasmalemma after binding to the apoER2 receptor, and into the neurons to the megaline receptor and in general, selenoprotein P plays the role of a pool that stores the necessary trace element and releases it, if necessary, for vital selenoproteins. The thioredoxin reductase family plays a key role in the invasion and metastasis of salivary adenoid cystic carcinoma through the influence on the TGF-β-Akt/GSK-3β pathway during epithelial-mesenchymal transition. The deletion of thioredoxin reductase 1 affects the levels of messengers of the Wnt/β-catenin signaling pathway. No less studied is the glutathione peroxidase group, of which GPX3 is able to inhibit signaling in the Wnt/β-catenin pathway and thereby inhibit thyroid metastasis, as well as suppress protein levels in the PI3K/Akt/c-fos pathway. A key observation is that in cases of carcinogenesis, a decrease in GPX3 and its hypermethylation are almost always found. Among deiodinases, deiodinase 3 acts as a promoter of the oncogenes BRAF, MEK or p38, while stimulating a decrease in the expression of cyclin D1. The dependence of the level of deiodinase 3 on the Hedgehog (SHH) signaling pathway is also noted. Methionine sulfoxide reductase A can compete for the uptake of ubiquitin, reduce p38, JNK and ERK promoters of the MAPK signaling pathway; methionine sulfoxide reductase B1 suppresses MAPK signaling messengers, and also increases PARP and caspase 3.
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9

Addinsall, Alex B., Craig R. Wright, Sof Andrikopoulos, Chris van der Poel i Nicole Stupka. "Emerging roles of endoplasmic reticulum-resident selenoproteins in the regulation of cellular stress responses and the implications for metabolic disease". Biochemical Journal 475, nr 6 (20.03.2018): 1037–57. http://dx.doi.org/10.1042/bcj20170920.

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Chronic metabolic stress leads to cellular dysfunction, characterized by excessive reactive oxygen species, endoplasmic reticulum (ER) stress and inflammation, which has been implicated in the pathogenesis of obesity, type 2 diabetes and cardiovascular disease. The ER is gaining recognition as a key organelle in integrating cellular stress responses. ER homeostasis is tightly regulated by a complex antioxidant system, which includes the seven ER-resident selenoproteins — 15 kDa selenoprotein, type 2 iodothyronine deiodinase and selenoproteins S, N, K, M and T. Here, the findings from biochemical, cell-based and mouse studies investigating the function of ER-resident selenoproteins are reviewed. Human experimental and genetic studies are drawn upon to highlight the relevance of these selenoproteins to the pathogenesis of metabolic disease. ER-resident selenoproteins have discrete roles in the regulation of oxidative, ER and inflammatory stress responses, as well as intracellular calcium homeostasis. To date, only two of these ER-resident selenoproteins, selenoproteins S and N have been implicated in human disease. Nonetheless, the potential of all seven ER-resident selenoproteins to ameliorate metabolic dysfunction warrants further investigation.
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Yao, Haidong, Wei Liu, Wenchao Zhao, Ruifeng Fan, Xia Zhao, Pervez Ahmed Khoso, Ziwei Zhang i Shiwen Xu. "Different responses of selenoproteins to the altered expression of selenoprotein W in chicken myoblasts". RSC Adv. 4, nr 109 (2014): 64032–42. http://dx.doi.org/10.1039/c4ra11502c.

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Rozprawy doktorskie na temat "Selenoproteins"

1

Mariotti, Marco. "Computational genomics of selenoproteins". Doctoral thesis, Universitat Pompeu Fabra, 2013. http://hdl.handle.net/10803/295583.

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Selenoproteins are a diverse class of proteins containing selenocysteine, the 21st aminoacid. Selenocysteine is inserted co-translationally, recoding very specific UGA codons through a dedicated machinery. Standard gene prediction programs consider UGA only as translational stop, and for this reason selenoprotein genes are typically misannotated. In the past years, we developed computational tools to predict selenoproteins at genomics scale. With these, we characterized the set of selenoproteins across many sequenced genomes, and we inferred their phylogenetic history. We dedicated particular attention to selenophosphate synthetase, a selenoprotein family required for selenocysteine biosynthesis, that can be used as marker of the selenocysteine coding trait. We show that selenoproteins went through a very diverse evolution in different lineages. While very conserved in vertebrates, selenoproteins were lost independently in many other organisms. Using genome sequencing, we traced with precision the path of genomic events that lead to recent selenoprotein extinctions in certain fruit flies.
Les selenoproteïnes s’agrupen en una classe heterogènia de proteïnes les quals contenen selenocysteïna, l’aminoàcid 21. La selenocisteïna és insertada durant el procés de traducció, recodificant codons UGA molt específics, mitjançant una maquinàiria dedicada. Els programes estàndard de predicció de gens interpreten el codó UGA només com a senyal d’stop de la traducció, i per aquesta raó els gens de selenoproteïness solen estar mal anotats. En els darrers anys, hem desenvolupat eines computacionals per a predir selenoproteïnes a escala genòmica. Amb aquestes, hem caracteritzat el conjunt de selenoproteïnes en aquells genomes que han estat seqüenciats, inferint la seva història filogenèitca. Hem dedicat especial ateníció a la família selenophosphate synthetase, selenoproteïna necessària per a la síntesi de selenocisteïna, i que per tant pot ser utilitzada com a marcador de codificació de selenocisteïna Mostrem que les selenoproteïnes han patit una evolució molt diversa en diferents llinatges. Tot i que es troben molt conservades en vertebrats, les selenoproteïnes van ser perdudes de manera independent en molts altres organismes. Gràcies a la sequenciació de genomes, vam traçar amb precisió els esdeveniment que van portar a l’extinció de selenoproteïnes a diverses espècies de drosòfila.
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Mariotti, Marco 1984. "Computational genomics of selenoproteins". Doctoral thesis, Universitat Pompeu Fabra, 2013. http://hdl.handle.net/10803/295583.

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Selenoproteins are a diverse class of proteins containing selenocysteine, the 21st aminoacid. Selenocysteine is inserted co-translationally, recoding very specific UGA codons through a dedicated machinery. Standard gene prediction programs consider UGA only as translational stop, and for this reason selenoprotein genes are typically misannotated. In the past years, we developed computational tools to predict selenoproteins at genomics scale. With these, we characterized the set of selenoproteins across many sequenced genomes, and we inferred their phylogenetic history. We dedicated particular attention to selenophosphate synthetase, a selenoprotein family required for selenocysteine biosynthesis, that can be used as marker of the selenocysteine coding trait. We show that selenoproteins went through a very diverse evolution in different lineages. While very conserved in vertebrates, selenoproteins were lost independently in many other organisms. Using genome sequencing, we traced with precision the path of genomic events that lead to recent selenoprotein extinctions in certain fruit flies.
Les selenoproteïnes s’agrupen en una classe heterogènia de proteïnes les quals contenen selenocysteïna, l’aminoàcid 21. La selenocisteïna és insertada durant el procés de traducció, recodificant codons UGA molt específics, mitjançant una maquinàiria dedicada. Els programes estàndard de predicció de gens interpreten el codó UGA només com a senyal d’stop de la traducció, i per aquesta raó els gens de selenoproteïness solen estar mal anotats. En els darrers anys, hem desenvolupat eines computacionals per a predir selenoproteïnes a escala genòmica. Amb aquestes, hem caracteritzat el conjunt de selenoproteïnes en aquells genomes que han estat seqüenciats, inferint la seva història filogenèitca. Hem dedicat especial ateníció a la família selenophosphate synthetase, selenoproteïna necessària per a la síntesi de selenocisteïna, i que per tant pot ser utilitzada com a marcador de codificació de selenocisteïna Mostrem que les selenoproteïnes han patit una evolució molt diversa en diferents llinatges. Tot i que es troben molt conservades en vertebrats, les selenoproteïnes van ser perdudes de manera independent en molts altres organismes. Gràcies a la sequenciació de genomes, vam traçar amb precisió els esdeveniment que van portar a l’extinció de selenoproteïnes a diverses espècies de drosòfila.
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Santesmasses, Ruiz Didac 1978. "Selenoproteins across the tree of life: Methods and applications". Doctoral thesis, Universitat Pompeu Fabra, 2016. http://hdl.handle.net/10803/565634.

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La selenocïsteina és coneguda com a l'aminoàcid 21. Les selenoproteïnes incorporen selenocïsteina en resposta a codons UGA específics mitjançant un mecanisme de recodificació, el qual és present en els tres dominis de la vida, però no en tots els organismes. Els programes estàndard per a la predicció de gens consideren UGA només com a codó stop, per aquesta raó l'anotació de selenoproteínes és, generalment, incorrecte. Hem desenvolupat mètodes computacionals per a la predicció de selenoproteïnes. Mitjançant l'aplicació d'aquestes i altres eines, hem caracteritzat selenoproteïnes a través de l'Arbre de la Vida, on hem observat una evolució dinàmica en la utilització de selenocïsteina en els diferents llinatges. Hem caracteritzat l'abundància i distribució de selenoproteïnes en el microbioma humà. Hem caracteritzat les selenoproteïnes presents a Lokiarchaeota, les quals presenten trets eucariòtics. Finalment hem dedicat especial atenció als insectes, en els quals una progressiva reducció en el nombre de selenoproteïnes culminà en múltiples extincions de selenoproteïnes en esdeveniments evolutius independents.
Selenocysteine is known as the 21st amino acid. Selenoproteins incorporate selenocysteine in response to specific UGA codons through a recoding mechanism, which present in the three domains of life, but not in all organisms. Standard gene prediction programs consider UGA only as stop, and selenoproteins are normally misannotated. We have developed computational methods for prediction of selenoproteins. By applying these and other tools, we have characterized selenoproteins across the Tree of Life, showing a diverse evolution of the utilization of selenocysteine in different lineages. We have characterized the abundance and distribution of selenoproteins in the human microbiota. We characterized the selenoproteins in Lokiarchaeota, which have some eukaryotic-like features. Finally we gave special attention to insects, in which a progressive reduction in the number of selenoproteins culminated in multiple independent selenoprotein extinctions.
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Evangelista, Jaqueline Pesciutti. "Selenoproteínas: Seril-tRNA Sintetase e as selenoproteínas do Trypanosoma brucei". Universidade de São Paulo, 2014. http://www.teses.usp.br/teses/disponiveis/76/76132/tde-13112014-171709/.

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O aminoácido selenocisteína (Sec) representa a principal forma biológica de selênio sendo requerida uma complexa maquinaria molecular para sua síntese e incorporação co-traducional em selenoproteínas. A Seril-tRNA sintetase (SerRS) inicia essa via, aminoacilando o Ser-tRNASec (SelC) com uma serina e também aminoacila os tRNAsSer. Sendo assim, um dos focos deste trabalho foi estudar a interação da SerRS de Trypanosoma brucei (T. brucei) com os tRNAsSer e o SelC utilizando a técnica de anisotropia de fluorescência para determinar suas constantes de dissociação. Em Kinetoplastidae, além da via de síntese de selenocisteína, há três selenoproteínas: SelT, SelK e SelTryp. No entanto, pouco se sabe a respeito das mesmas, sendo o estudo destas selenoproteínas o outro foco deste trabalho. Os fragmentos de DNA que codificam estas selenoproteínas foram subclonados em vetor de expressão pET 28a e 29a para posterior uso em células de Escherichia coli (E. coli). Para as proteínas SelK e SelTryp os ensaios de expressão apresentaram resultados insuficientes para dar continuidade aos experimentos planejados, pois o rendimento foi baixo e a purificação não foi possível. Já com a proteína SelT, devido à grande dificuldade encontrada para tornà-la solúvel, descobriu-se, no decorrer do trabalho, que tratava-se de uma proteína de membrana, ocasionando mudanças de alguns objetivos previamente propostos e consequentemente busca por novas estratégias. Conseguiu-se expressá-la na de forma solúvel e purificá-la por cromatografias. Ensaios realizados no SEC-MALLS mostraram uma estabilidade do complexo proteína-detergente. Com a TbSerRS é possível concluir que a organização de especificidade de ligação da enzima com seus ligantes se dá crescentemente: SelC>tRNASer7>tRNASer3a>tRNASer3b. E com as selenoproteínas do T. brucei faz-se necessários novas contruções para SelK e SelTryp e dar continuidade aos experimentos com a SelT tentando cristalizá-la, já que prototolo para a obtenção do complexo proteína-detergente está montado e estabilizado.
Selenocysteine (Sec) amino acid is the major biological form of selenium and requires a complex molecular machinery for its synthesis and co-translational incorporation into selenoproteins. The Seryl-tRNA synthetase (SerRS) starts this biosynthesis and matches the tRNASec (SELC) with a serine and the tRNAsSer, therefore the focus of this study is on SerRS of Trypanosoma brucei (T. brucei) and tRNAsSer and SELC interactions, with fluorescence anisotropy techinic to determinat dissociation constants. Three selenoproteins, namely SelT, SelK and SelTryp, besides the route of selenocysteine synthesis there be in Kinetoplastidae. DNA fragments that coding for these selenoproteins were subcloned in 28a and 29a to use into Escherichia coli (E. coli) cells. For Selk and SelTryp proteins, the expression protocol did not show an unsatisfactory result to continue the experiments. Many difficulties were encountered in studies with Selt protein, mainly in attempts to make it soluble. Our analyses revealed SelT was a membrane protein, therefore it could cause changes in some objectives and search for new strategies. It could be expressed and purified in cromatographis. SEC-MALLS assays showed a stability of the protein detergent complex. With TbSerRS is possible to conclude that the organization of binding specificity of the enzyme with its ligands occurs increasingly: SelC>tRNASer7>tRNASer3a>tRNASer3b. And selenoproteins in T. brucei, it is necessary for new constructions to SelK and SelTryp to continue the experiments trying to crystallizes SelT, since prototolo for obtaining the protein-detergent complex is assembled and stabilized.
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5

Zhou, Xiaodong. "The effect of estrogen status on selenium metabolism in female rats". Columbus, Ohio : Ohio State University, 2007. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1179976985.

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6

Mallion, Stephen Nicholas. "The development of the time differential perturbed directional correlation technique for biomedical applications". Thesis, University of Surrey, 1994. http://epubs.surrey.ac.uk/844138/.

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Consideration is given to the use of the time differential perturbed directional correlation (TDPDC) technique in biomedical applications such as structural studies of the selenoproteins. Mathematical models of the perturbed directional correlations show that the application of the TDPDC technique to the study of the electric quadrupole interactions experienced by an ensemble of probe nuclei bound to a protein is capable of yielding the fraction of probe nuclei occupying each of a number of distinct types of binding site in the protein, the strength, symmetry and inhomogeneity of the nuclear quadrupole interaction occurring at each different type of site and, if the environment of the protein is a viscous solution, the diffusion constant for the protein in the solution, from which the associated correlation time and hence the radius of the protein may be derived. A time spectrometer employing a pair of barium fluoride (BaF2) scintillation counters was designed and constructed to allow TDPDC experiments to be performed. The optimum time resolution of the spectrometer was found to be 354+/-10 ps for the 1.173 and 1.332 MeV gamma-rays emitted in the decay of 60Co. The characteristics of the spectrometer were inferior to those of similar systems which are described elsewhere. A number of improvements to the spectrometer that was used in this work have been suggested. The manner in which various deviations from the ideal experimental arrangement affect both the observed perturbed directional correlation and the optimum methods of conducting TDPDC experiments has been carefully considered. Of particular importance was the effect of source decentring, since the employed apparatus does not allow the radioactive source to be precisely centred. It was found that the implications of source decentring are that the values of the parameters describing the perturbation of the directional correlation must be derived from a single TDPDC spectrum, as must those of a number of additional parameters which are of little interest. The viability of this procedure was investigated by carrying out a TDPDC study of the 356-81 keV gamma-gamma cascade in 133Cs, taking account of the interference from sum-coincidence effects and competing cascades. From the TDPDC spectrum that was obtained, the smearing effects of the finite time resolution of the spectrometer were partially removed by deconvolution, resulting in an unfolded time spectrum to which attempts were made to fit a suitable model. Although it was not possible to achieve a satisfactory fit, a number of potential remedies for the poor fit have been proposed. A TDPDC study of the 121-280 keV gamma-gamma cascade in 75As was performed for the purpose of assessing the feasibility of using the TDPDC technique in future investigations employing 75Se-labelled selenoproteins. Account was again taken of the interference from sum-coincidence effects and competing cascades. A bid to deconvolve the smeared TDPDC spectrum that was acquired was not successful, and so attempts were made to fit to the smeared spectrum a model which allowed for the finite time resolution of the spectrometer. The fitting proved to be problematic, indicating that it would be difficult to apply the TDPDC technique to an investigation of 75Se-labelled selenoproteins. However, this conclusion is perhaps unduly pessimistic because some of the problems that arose in the feasibility study will not be present in practice when a 75Se-labelled selenoprotein is used. The available evidence suggests that 73Se offers advantages over 75Se as a radiolabel in TDPDC studies of the selenoproteins.
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Terry, Emily Nicole. "Regulation of selected selenoproteins in porcine and bovine skeletal muscle". Online access for everyone, 2008. http://www.dissertations.wsu.edu/Thesis/Spring2008/e_terry_041108.pdf.

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Cockman, Eric Michael. "Post-Transcriptional Regulation of Selenoprotein S". Case Western Reserve University School of Graduate Studies / OhioLINK, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=case1562593531805034.

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Rosario, Sarah. "Bacterial Selenoproteins: A Role in Pathogenesis and Targets for Antimicrobial Development". Doctoral diss., University of Central Florida, 2009. http://digital.library.ucf.edu/cdm/ref/collection/ETD/id/2655.

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Selenoproteins are unique proteins in which selenocysteine is inserted into the polypeptide chain by highly specialized translational machinery. They exist within all three kingdoms of life. The functions of these proteins in biology are still being defined. In particular, the importance of selenoproteins in pathogenic microorganisms has received little attention. We first established that a nosocomial pathogen, Clostridium difficile, utilizes a selenoenzyme dependent pathway for energy metabolism. Following this initial characterization, we demonstrate that this pathway is linked to production of toxins by this organism. Finally, we show that interruption of selenium metabolism is a viable pathway for development of antimicrobials against this, and other selenoprotein dependent pathogens. We investigated whether Stickland reactions (paired amino acid fermentation) might be at the heart of C. difficile's bioenergetic pathways. Growth of C. difficile on Stickland pairs yielded large increases in cell density in a limiting basal medium, demonstrating these reactions are tied to ATP production. Selenium supplementation was required for this increase in cell yield. Analysis of genome sequence data reveals genes encoding the protein components of two key selenoenzyme reductases; glycine and D-proline reductase. These selenoenzymes were expressed upon addition of the corresponding Stickland acceptor (glycine, proline or hydroxyproline). Purification of the selenoenzyme D-proline reductase revealed a mixed complex of PrdA and PrdB (SeCys containing) proteins. D-proline reductase utilized only D-proline but not L-hydroxyproline, even in the presence of an expressed and purified proline racemase. The enzyme was found to be independent of divalent cations, and zinc was a potent inhibitor. These results show that Stickland reactions are key to the growth of C. difficile and that the mechanism of D-proline reductase may differ significantly from similar enzymes from non-pathogenic species. C. difficile pathogenesis is due to the production of toxins, A and B, members of the large clostridial cytotoxin family. Previous studies have shown that toxin production by this organism is influenced by the composition of the growth medium. We examined the impact of Stickland acceptor amino acids (Stickland acceptors; glycine, proline and hydroxyproline) on growth kinetics and yield, protein synthesis, toxin production and gene expression. Although addition of Stickland acceptors moderately increases growth yield and total protein synthesis, there does not appear to be a clear impact on entry into stationary phase. Glycine dramatically increases the amount of toxin released into the growth medium. Conversely, the addition of hydroxyproline suppresses toxin production. We examine possible mechanisms of regulation and demonstrate that CodY, a regulator of toxin gene transcription does not appear to mediate this effect. Given the importance of selenium dependent Stickland reactions to C. difficile growth and toxin production we aimed to examine the efficacy of blocking such pathways as a means of antimicrobial development. Selenide is the only known substrate for selenophosphate synthetase, the first enzyme involved in the specific incorporation of selenium into selenoproteins. We have identified a stable complex formed upon reaction of auranofin (a gold containing drug) with selenide in vitro. Auranofin potently inhibits the growth of C. difficile but does not similarly affect other clostridia that do not utilize selenoproteins to obtain energy. Moreover, auranofin inhibits the incorporation of radioisotope selenium (75Se) in selenoproteins in both E. coli, the prokaryotic model for selenoprotein synthesis, and C. difficile without impacting total protein synthesis. Auranofin blocks the uptake of selenium and results in the accumulation of the auranofin-selenide adduct in the culture medium. Addition of selenium in the form of selenite or L-selenocysteine to the growth media significantly reduces the inhibitory action of auranofin on the growth of C. difficile. Based on these results, we propose that formation of this complex and the subsequent deficiency in available selenium for selenoprotein synthesis is the mechanism by which auranofin inhibits C. difficile growth. The antimicrobial potential of blocking selenium metabolism is further demonstrated in the dental pathogen Treponema denticola. We show that auranofin blocks the growth this organism which also participates in Stickland fermentation. In addition, we provide evidence that the antimicrobial action of stannous salts against T. denticola is also mediated through inhibition of the metabolism of selenium. These studies clearly show that, at least in a subset of microbes that use selenium for the synthesis of selenoproteins, the need for this metalloid can be a useful target for future antimicrobial development.
Ph.D.
Department of Biomolecular Science
Burnett College of Biomedical Sciences
Biomedical Sciences PhD
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Waschulewski, Ingo Herbert 1962. "Effect of dietary methionine on selenomethionine metabolism and utilization for selenoproteins". Thesis, The University of Arizona, 1988. http://hdl.handle.net/10150/276933.

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The effects of dietary methionine (Met) on the utilization of selenium (Se) from stored tissue Se and dietary selenomethionine (SeMet) for glutathione peroxidase (GSH-Px) synthesis were studied in male rats. Plasma, liver and muscle Se significantly increased when rats were fed 0.5 mg Se/kg diet as SeMet in a Met-deficient diet for 21 d, whereas tissue GSH-Px activities decreased 43-50% during the SeMet supplementation period, suggesting that Se is deposited as SeMet in general body proteins. By calculation, a significant lower percentage of Se was associated with GSH-Px in Met-deficient as compared to Met-supplemented rats. Dietary Met supplementation increased the incorporation of 75Se from 75SeMet into specific rat selenoproteins in addition to liver GSH-Px. Overall, these results suggest that intact SeMet is preferentially incorporated non-specifically into general body proteins in Met-deficient rats, whereas with supplemental Met, more SeMet is degraded and the released Se used for specific selenoprotein synthesis. (Abstract shortened with permission of author.)
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Książki na temat "Selenoproteins"

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Chavatte, Laurent, red. Selenoproteins. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-7258-6.

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Liu, Junqiu, Guimin Luo i Ying Mu. Selenoproteins and Mimics. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-22236-8.

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Kohrle, Josef. Selenoproteins. Eurekah.Com Inc, 2004.

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Mu, Ying, Guimin Luo i Junqiu Liu. Selenoproteins and Mimics. Springer, 2012.

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Mu, Ying, Guimin Luo i Junqiu Liu. Selenoproteins and Mimics. Springer London, Limited, 2012.

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Selenoproteins And Mimics. Springer, 2012.

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Chavatte, Laurent. Selenoproteins: Methods and Protocols. Springer New York, 2018.

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Chavatte, Laurent. Selenoproteins: Methods and Protocols. Springer New York, 2017.

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Tew, Kenneth D., i Francesco Galli. Selenium and Selenoproteins in Cancer. Elsevier Science & Technology Books, 2017.

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Tew, Kenneth D., i Francesco Galli. Selenium and Selenoproteins in Cancer. Elsevier Science & Technology Books, 2017.

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Części książek na temat "Selenoproteins"

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Liu, Xiaoman, Wei Zhang i Junqiu Liu. "Semisynthesized Selenoproteins". W Advanced Topics in Science and Technology in China, 249–58. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-22236-8_16.

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Luo, Quan, i Junqiu Liu. "Artificial Selenoproteins". W Encyclopedia of Metalloproteins, 188–95. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_487.

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Cohen, G. N. "Selenocysteine and Selenoproteins". W Microbial Biochemistry, 363–71. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-9437-7_30.

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Salinas, Gustavo, Mariana Bonilla, Lucía Otero, Alexey V. Lobanov i Vadim N. Gladyshev. "Selenoproteins in Parasites". W Selenium, 471–79. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4614-1025-6_37.

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Gladyshev, Vadim N. "Selenoproteins and Selenoproteomes". W Selenium, 109–23. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4614-1025-6_9.

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Cohen, G. N. "Selenocysteine and Selenoproteins". W Microbial Biochemistry, 405–14. Dordrecht: Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-017-8908-0_30.

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Cohen, Georges N. "Selenocysteine and Selenoproteins". W Microbial Biochemistry, 523–34. Dordrecht: Springer Netherlands, 2016. http://dx.doi.org/10.1007/978-94-017-7579-3_30.

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Huang, Kaixun, i Huibi Xu. "Selenoproteins and Atherosclerosis". W Advanced Topics in Science and Technology in China, 141–60. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-22236-8_10.

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Liu, Qiong, i Liang Jiang. "Bioinformatics of Selenoproteins". W Advanced Topics in Science and Technology in China, 125–40. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-22236-8_9.

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Rother, Michael. "Selenoproteins in Prokaryotes". W Encyclopedia of Metalloproteins, 1959–64. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_466.

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Streszczenia konferencji na temat "Selenoproteins"

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Tao, Lan, Geng Liu, Xiaoli Wang i Lei Zhang. "Prediction of Selenoproteins Based on Motif Recognition". W 2009 2nd International Conference on Biomedical Engineering and Informatics. IEEE, 2009. http://dx.doi.org/10.1109/bmei.2009.5302720.

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RoyChoudhury, Sourav, Rashmi Mukherjee i Koel Chaudhury. "Molecular characterization of selenoproteins based on decreased glutathione peroxidase activity in preeclampsia". W 2010 International Conference on Systems in Medicine and Biology (ICSMB). IEEE, 2010. http://dx.doi.org/10.1109/icsmb.2010.5735420.

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Jiang, Liang, Qiong Liu i Xiaoli Wang. "An Improved Method for the Prediction of Selenoproteins from the Genome of Anopheles Gambiae". W 2008 2nd International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2008. http://dx.doi.org/10.1109/icbbe.2008.144.

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Strauss, Ewa, Lukasz Kruszyna, Jolanta Tomczak, Marta Stelcer, Zbigniew Krasinski i Grzegorz Oszkinis. "Polymorphisms of Genes Encoding Selenoproteins Influence the Growth of Abdominal Aortic Aneurysm (AAA) - A Study in Polish Population". W 70th International Congress of the European Society for Cardiovascular and Endovascular Surgery and 7th International Meeting on Aortic Diseases. Thieme Medical Publishers, Inc., 2022. http://dx.doi.org/10.1055/s-0042-1750917.

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Galinn, Sarah E., Lindsay C. Rosenthal, Steven M. Barsotti i Petra A. Tsuji. "Abstract 4881: Influence of polyphenols on selenoprotein expression in human colon cancer cells." W Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-4881.

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Penney, Kathryn L., Haojie Li, Lorelei A. Mucci, J. Steven Morris, Howard D. Sesso, Meir J. Stampfer i Jing Ma. "Abstract A122: Genetic variation in selenoprotein P, selenium levels, and prostate cancer risk and survival". W Abstracts: AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Dec 6–9, 2009; Houston, TX. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1940-6207.prev-09-a122.

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Lin, Shih-Wen, Neal D. Freedman, Philip R. Taylor, You-Lin Qiao, Christian C. Abnet, Paula Hyland, Nan Hu i in. "Abstract A59: Selenoprotein gene variants and risk of esophageal and gastric cancer in a Chinese population". W Abstracts: AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Oct 22-25, 2011; Boston, MA. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1940-6207.prev-11-a59.

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Gopalakrishna, Rayudu, Jason E. Schiffman, Joshua Man, Lok Lei, Adela Wu i Usha Gundimeda. "Abstract 1889: Curcumin potentiates the cancer-preventive actions of selenium by inactivating selenoprotein thioredoxin reductase in prostate cancer cells". W Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-1889.

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Gopalakrishna, Rayudu, Jason Eric Schiffman, Kelley Mowatt i Usha Gundimeda. "Abstract 3687: Curcumin both inactivates and induces selenoprotein thioredoxin reductase: dual regulation influences curcumin-induced apoptosis in prostate cancer cells". W Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-3687.

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Li, Sharon, Paula L. Hyland, Neal D. Freedman, Nan Hu, Hua Su, Lemin Wang, Chaoyu Wang i in. "Abstract 2206: Genetic variants in selenoprotein genes and risk of esophageal squamous cell carcinoma and gastric cancer in a Chinese population". W Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-2206.

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Raporty organizacyjne na temat "Selenoproteins"

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Navsariwala, Veda. Selenoproteins and Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, listopad 2005. http://dx.doi.org/10.21236/ada444681.

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Diwadkar-Navsariwala, Veda. Selenoproteins and Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, listopad 2006. http://dx.doi.org/10.21236/ada463203.

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