Publications by authors named "Gaurab Sarangi"
Article Synopsis
- Selenocysteine, a unique selenium-containing amino acid, is critical for the function of certain enzymes called selenoprotein oxidoreductases but has been lost in some mammalian lineages, particularly in glutathione peroxidase 6 (GPX6).
- The loss of selenocysteine in GPX6 occurred through strong evolutionary changes while also introducing new mutations that altered the enzyme's catalytic properties.
- This case of adaptive convergence suggests that these modifications led to novel enzymatic functions rather than merely compensating for the loss of selenocysteine, highlighting an interesting aspect of evolution in mammalian selenoproteins.
Selenium (Se), a sparse element on earth, is an essential micronutrient in the vertebrate diet and its intake depends on its content in soils and waters worldwide. Selenium is required due to its function in selenoproteins, which contain selenocysteine (Sec), the 21st amino acid in the genetic code, as one of their constituent residues. Selenocysteine is analogous to the amino acid cysteine (Cys), which uses the abounding element sulfur instead.
View Article and Find Full Text PDFSelenoDB (http://www.selenodb.org) aims to provide high-quality annotations of selenoprotein genes, proteins and SECIS elements.
View Article and Find Full Text PDFWe apply a model-independent, agnostic approach to the collider phenomenology of supersymmetry, in which all mass parameters are taken as free inputs at the weak scale. We consider the gauginos, Higgsinos, and the first two generations of sleptons and squarks, and analyze all possible mass hierarchies among them (4×8!=161,280 in total) in which the lightest superpartner is neutral, leading to missing energy. In each case, we identify the full set of the dominant decay chains originating from the lightest colored superpartner.
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