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Prajwal Paudel

Researcher at University of Alabama in Huntsville

Publications -  23
Citations -  432

Prajwal Paudel is an academic researcher from University of Alabama in Huntsville. The author has contributed to research in topics: Essential oil & Internal medicine. The author has an hindex of 11, co-authored 21 publications receiving 323 citations. Previous affiliations of Prajwal Paudel include University of Delaware.

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Bioactivities and compositional analyses of Cinnamomum essential oils from Nepal: C. camphora, C. tamala, and C. glaucescens.

TL;DR: This work examines the biological activity of essential oils of Cinnamomum camphora leaves, C. glaucescens fruit, and C. tamala root from Nepal for phytotoxic activity against lettuce and perennial ryegrass, brine shrimp lethality, and antibacterial, antifungal, cytotoxic, insecticidal, and nematicidal activities.
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Mechanisms of Bond Cleavage during Manganese Oxide and UV Degradation of Glyphosate: Results from Phosphate Oxygen Isotopes and Molecular Simulations

TL;DR: The DFT results reveal that the C-P bond could be cleaved by water, OH- or •OH, with the energy barrier opposing bond dissociation being lowest in the presence of the radical species, and that C-N bond cleavage is favored by the formation of both nitrogen- and carbon-centered radicals.
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Volatile constituents of Pinus roxburghii from Nepal.

TL;DR: The bioactivity of P. roxburghii essential oil is consistent with its traditional medicinal use and exhibits anti-bacterial activity and anti-fungal activity against Aspergillus niger.
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Bioactivities of volatile components from Nepalese Artemisia species.

TL;DR: DFT calculations (B3LYP/6-31G*) revealed thermal decomposition of ascaridole to be energetically accessible at hydrodistillation and GC conditions, but these are spin-forbidden processes, so decomposition likely proceeds by way of homolytic peroxide bond cleavage rather than retro-Diels-Alder elimination of molecular oxygen.
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Crystal structure and activity-based labeling reveal the mechanisms for linkage-specific substrate recognition by deubiquitinase USP9X.

TL;DR: The structure model and biochemical data suggest that the USP9X catalytic domain harbors three Ub binding sites, and a zinc finger in the fingers subdomain and the β-hairpin insertion both play important roles in polyUb chain processing and linkage specificity.