Relevant bibliographies by topics / Spirodiazaselenuranes

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Spirodiazaselenuranes'

Author: Grafiati
Published: 6 September 2023

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Journal articles on the topic "Spirodiazaselenuranes"

1

Lamani, Devappa S., Debasish Bhowmick, and Govindasamy Mugesh. "Spirodiazaselenuranes: synthesis, structure and antioxidant activity." Organic & Biomolecular Chemistry 10, no. 39 (2012): 7933. http://dx.doi.org/10.1039/c2ob26156a.

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2

Lamani, Devappa, Debasish Bhowmick, and Govindasamy Mugesh. "Substituent Effects on the Stability and Antioxidant Activity of Spirodiazaselenuranes." Molecules 20, no. 7 (2015): 12959–78. http://dx.doi.org/10.3390/molecules200712959.

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3

Kadu, Rahul, Monojit Batabyal, Heena Kadyan, Apurba Lal Koner, and Sangit Kumar. "An efficient copper-catalyzed synthesis of symmetrical bis(N-arylbenzamide) selenides and their conversion to hypervalent spirodiazaselenuranes and hydroxy congeners." Dalton Transactions 48, no. 21 (2019): 7249–60. http://dx.doi.org/10.1039/c8dt04832k.

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4

Sarma, Bani Kanta, Debasish Manna, Mao Minoura, and Govindasamy Mugesh. "Synthesis, Structure, Spirocyclization Mechanism, and Glutathione Peroxidase-like Antioxidant Activity of Stable Spirodiazaselenurane and Spirodiazatellurane." Journal of the American Chemical Society 132, no. 15 (2010): 5364–74. http://dx.doi.org/10.1021/ja908080u.

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5

Kuzma, Dušan, Masood Parvez, and Thomas George Back. "Formation of a spirodiazaselenurane and its corresponding azaselenonium derivatives from the oxidation of 2,2′-selenobis(benzamide). Structure, properties and glutathione peroxidase activity." Organic & Biomolecular Chemistry 5, no. 19 (2007): 3213. http://dx.doi.org/10.1039/b710685h.

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Dissertations / Theses on the topic "Spirodiazaselenuranes"

1

Bhowmick, Debasish. "Structure-Activity Correlation and Mechanistic Investigations of Glutathione Peroxidase-Like Catalytic Activity of Diaryl Diselenides." Thesis, 2014. https://etd.iisc.ac.in/handle/2005/4563.

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Abstract:
Hydroperoxides are very harmful and they can oxidize several biomolecules, causing different disease states. Glutathione peroxidase (GPx) is a mammalian selenoenzyme which protects human body from oxidative damage by catalyzing the reduction of harmful peroxides using glutathione (GSH) as a cofactor. GPx contains selenocysteine in its active site. The catalytic cycle of GPx enzymes is believed to involve three steps. In the first step, the reduced selenolate moiety (E-SeH) of Sec residue reduces hydroperoxides to water (or alcohol) to form oxidized selenenic acid (E-SeOH), which upon reaction
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2

Sarma, Bani Kanta. "Antioxidant Activity Of The Anti-Inflammatory Compound Ebselen And Its Analogues : Role Of Nonbonded Interactions." Thesis, 2008. https://etd.iisc.ac.in/handle/2005/900.

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Abstract:
Although considered as a poison for long time, the importance of selenium as an essential trace element is now well recognized. In proteins, the redox active selenium moiety is incorportated as selenocysteine (Sec), the 21st amino acid. In mammals, selenium exerts its redox activities through several selenocysteine-containing enzymes, which include glutathione peroxidase (GPx), iodothyronine deiodinase (ID) and thioredoxin reductase (TrxR). Although these enzymes have Sec in their active sites, they catalyze completely different reactions and their substrate specificity and cofactor or co-subs
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3

Sarma, Bani Kanta. "Antioxidant Activity Of The Anti-Inflammatory Compound Ebselen And Its Analogues : Role Of Nonbonded Interactions." Thesis, 2008. http://hdl.handle.net/2005/900.

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Abstract:
Although considered as a poison for long time, the importance of selenium as an essential trace element is now well recognized. In proteins, the redox active selenium moiety is incorportated as selenocysteine (Sec), the 21st amino acid. In mammals, selenium exerts its redox activities through several selenocysteine-containing enzymes, which include glutathione peroxidase (GPx), iodothyronine deiodinase (ID) and thioredoxin reductase (TrxR). Although these enzymes have Sec in their active sites, they catalyze completely different reactions and their substrate specificity and cofactor or co-subs
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Book chapters on the topic "Spirodiazaselenuranes"

1

S. Lamani, Devappa. "Functional Mimics of Glutathione Peroxidase: Spirochalcogenuranes, Mechanism and Its Antioxidant Activity." In Chalcogens [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.102430.

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Abstract:
The present chapter describe a series of synthetic organoselenium compounds such as ebselen analogues, diaryl selenides, spirodioxyselenurane, spirodiazaselenuranes and its Glutathione peroxidise (GPx) catalytic activity. These ebselen related compounds either by modifying the basic structure of ebselen or incorporating some structural features of the native enzyme, a number of small-molecules of selenium compounds as functional mimics of GPx are discussed. In addition to this, spirodioxyselenuranes and spirodiazaselenuranes are important class of hypervalent selenium compounds, whose stability highly depends on the nature of the substituents attached to the nitrogen atom. The glutathione peroxidase (GPx) mimetic activity of all the selenium compounds showed significantly by facilitating the oxidation of the selenium centre. In contrast to this, ebselen analogue shows significant antioxidant activity compared with spirodiazaselenuranes and its derivatives.
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