Publications by authors named "Hima Priyanka Nadimpalli"

Background: Cellular iron homeostasis is regulated by iron regulatory proteins (IRP1 and IRP2) that sense iron levels (and other metabolic cues) and modulate mRNA translation or stability via interaction with iron regulatory elements (IREs). IRP2 is viewed as the primary regulator in the liver, yet our previous datasets showing diurnal rhythms for certain IRE-containing mRNAs suggest a nuanced temporal control mechanism. The purpose of this study is to gain insights into the daily regulatory dynamics across IRE-bearing mRNAs, specific IRP involvement, and underlying systemic and cellular rhythmicity cues in mouse liver.

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The genetic code that specifies the identity of amino acids incorporated into proteins during protein synthesis is almost universally conserved. Mitochondrial genomes feature deviations from the standard genetic code, including the reassignment of two arginine codons to stop codons. The protein required for translation termination at these noncanonical stop codons to release the newly synthesized polypeptides is not currently known.

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Cytoplasmic polyadenylation is a mechanism to promote mRNA translation in a wide variety of biological contexts. A canonical complex centered around the conserved RNA-binding protein family CPEB has been shown to be responsible for this process. We have previously reported evidence for an alternative noncanonical, CPEB-independent complex in <i>Drosophila</i>, of which the RNA-interference factor Dicer-2 is a component.

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Electronic laboratory notebooks (ELNs) will probably replace paper laboratory notebooks (PLNs) in academic research due to their advantages in data recording, sharing and security. Despite several reports describing technical characteristics of ELNs and their advantages over PLNs, no study has directly tested ELN performance among researchers. In addition, the usage of tablet-based devices or wearable technology as ELN complements has never been explored in the field.

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Article Synopsis
  • Initiator tRNAs bind directly to the ribosomal P-site due to the presence of three consecutive G-C base pairs (3GC pairs) in their structure, which is crucial for their function.
  • Mutations in mRNA or 16S rRNA that enhance interaction between Shine-Dalgarno and anti-SD sequences can compensate for the absence of 3GC pairs in the tRNA(fMet) within E. coli.
  • The study suggests that while 3GC pairs are important for tRNA(fMet) retention during ribosome transitions, certain conditions (like drugs or variations in initiation factors) can reduce reliance on these pairs for proper initiation in the 70S ribosome.
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