Results 21 to 30 of about 20,846 (213)

Probing the Structure of [NiFeSe] Hydrogenase with QM/MM Computations [PDF]

, 2020
The geometry and vibrational behavior of selenocysteine [NiFeSe] hydrogenase isolated from Desulfovibrio vulgaris Hildenborough have been investigated using a hybrid quantum mechanical (QM)/ molecular mechanical (MM) approach. Structural models have been
Elghobashi-Meinhardt, Nadia Said, Moubarak, Samah, Mroginski, Maria Andrea, Tombolelli, Daria   +3 more
core   +1 more source

Comparative analysis of CO2 reduction by soluble Escherichia coli formate dehydrogenase H and its selenocysteine-to-cysteine substitution variant

Journal of CO2 Utilization, 2023
Metal-dependent formate dehydrogenases (Me-FDHs) are highly active CO2-reducing enzymes operating at low redox potentials and employ either molybdenum or tungsten to reduce the bound substrate.
Feilong Li, Silvan Scheller, Michael Lienemann   +2 more
doaj   +1 more source

Selenoprotein gene nomenclature [PDF]

, 2016
The human genome contains 25 genes coding for selenocysteine-containing proteins (selenoproteins). These proteins are involved in a variety of functions, most notably redox homeostasis.
Arn\ue9r, Elias S., Berry, Marla J., Bruford, Elspeth A., Burk, Raymond F., Carlson, Bradley A., Castellano, Sergi, Chavatte, Laurent, Conrad, Marcus, Copeland, Paul R., Diamond, Alan M., Driscoll, Donna M., Ferreiro, Ana, Floh\ue9, Leopold, Gladyshev, Vadim N, Green, Fiona R., Guig\uf3, Roderic, Handy, Diane E., Hatfield, Dolph L., Hesketh, John, Hoffmann, Peter R., Holmgren, Arne, Hondal, Robert J., Howard, Michael T., Huang, Kaixun, K\uf6hrle, Josef, Kim, Hwa Young, Kim, Ick Young, Krol, Alain, Kryukov, Gregory V., Lee, Byeong Jae, Lee, Byung Cheon, Lei, Xin Gen, Lescure, Alain, Liu, Qiong, Lobanov, Alexei V., Loscalzo, Joseph, Maiorino, Matilde, Mariotti, Marco, Prabhu, K. Sandeep, Rayman, Margaret P., Regina, Brigelius Floh\ue9, Rozovsky, Sharon, Salinas, Gustavo, Schmidt, Edward E., Schomburg, Lutz, Schweizer, Ulrich, Simonovi\u107, Miljan, Sunde, Roger A., Tsuji, Petra A., Tweedie, Susan, Ursini, Fulvio, Whanger, Philip D., Zhang, Yan   +52 more
core   +3 more sources

Selenium in biology: Facts and medical perspectives [PDF]

, 2000
Several decades after the discovery of setenium as an essential trace element in vertebrates approximately 20 eukaryotic and more than 15 prokaryotic selenoproteins containing the 21(st) proteinogenic amino acid, selenocysteine, have been identified ...
Brigelius-Flohé, Regina, Böck, August, Flohé, Leopold, Gärtner, Roland, Köhrle, Josef, Meyer, Ortwin   +5 more
core   +1 more source

Selenocysteine in Trypanosoma evansi: Identification of the Genes selb, selc, seld, pstk, seltryp and the Selenophosphate Synthetase Protein

Acta Protozoologica, 2021
Selenoproteins have been described in all three domains of life and their function has been mainly associated with oxidative stress defense.
Kaio Cesar Simiano Tavares, Maria Gabriela Casagrande Dambrós, André Saraiva Leão Antunes, Pietro Martin Danziato, Patricia Hermes Stoco, Aline Daiane Schlindwein, Renato Simões Moreira, Luiz Claudio Miletti   +7 more
doaj   +1 more source

Effects of selenium biofortification on crop nutritional quality [PDF]

, 2015
Selenium (Se) at very low doses has crucial functions in humans and animals. Since plants represent the main dietary source of this element, Se-containing crops may be used as a means to deliver Se to consumers (biofortification). Several strategies have
Dall'Acqua, Stefano, Elizabeth A. H., Pilon Smits, Malagoli, Mario, Schiavon, Michela   +3 more
core   +1 more source

Delivery of the selenoprotein thioredoxin reductase 1 to mammalian cells

Frontiers in Molecular Biosciences, 2022
Over-expression of genetically encoded thioredoxin reductase 1 (TrxR1) TrxR1 can be toxic to cells due to the formation of a truncated version of the enzyme. We developed a new mammalian cell-based model to investigate TrxR1 activity.
David E. Wright, Tarana Siddika, Ilka U. Heinemann, Patrick O’Donoghue   +3 more
doaj   +1 more source

Review

, 2020
The chalcogen elements oxygen, sulfur, and selenium are essential constituents of side chain functions of natural amino acids. Conversely, no structural and biological function has been discovered so far for the heavier and more metallic tellurium ...
Agh R, Arai K, Baskakov IV, Creighton TE, Dittmer K, Du Vigneaud V, Janeček J, Metanis N, Musiol HJ, Muttenthaler M, Nygard B, O'Donnell ME, Welch M, Yang F   +13 more
core   +1 more source

Human selenoprotein P and S variant mRNAs with different numbers of SECIS elements and inferences from mutant mice of the roles of multiple SECIS elements [PDF]

Open Biology, 2016
Dynamic redefinition of the 10 UGAs in human and mouse selenoprotein P (Sepp1) mRNAs to specify selenocysteine instead of termination involves two 3′ UTR structural elements (SECIS) and is regulated by selenium availability. In addition to the previously
Sen Wu, Marco Mariotti, Didac Santesmasses, Kristina E. Hill, Janinah Baclaocos, Estel Aparicio-Prat, Shuping Li, John Mackrill, Yuanyuan Wu, Michael T. Howard, Mario Capecchi, Roderic Guigó, Raymond F. Burk, John F. Atkins   +13 more
doaj   +1 more source

Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation

Nature Communications, 2016
Specialized translation elongation factors (eEFSec and SelB) promote selenocysteine incorporation into proteins. Here, the authors report the structure of human eEFSec, examine its interactions with guanine nucleotides, and propose a non-canonical ...
Malgorzata Dobosz-Bartoszek, Mark H. Pinkerton, Zbyszek Otwinowski, Srinivas Chakravarthy, Dieter Söll, Paul R. Copeland, Miljan Simonović   +6 more
doaj   +1 more source