Publications by authors named "Y P Venkatesh"

Certain volatile organic compounds (VOCs), such as formaldehyde, acetone, and ethanol, are overexpressed in some terminal diseases like cancer, diabetes, Alzheimer's, etc. Therefore, high-precision detection and quantification of VOCs is imperative for early diagnosis of such detrimental diseases. Non-invasive and accurate fluorescence-based detection of such analytes has garnered widespread attention.

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  • - The synthesis of crystallizable unnatural amino acid acridon-2-ylalanine (Acd) is refined for large-scale production, allowing its incorporation into proteins through genetic code expansion (GCE) and preparation for solid-phase peptide synthesis (SPPS).
  • - Acd is utilized in designing fluorescent protease sensors by leveraging its ability to quench fluorescence when near tyrosine (Tyr) residues, showcasing its application in biochemistry.
  • - The study also explores Acd's role in a lanthanide-binding peptide and its insertion into the protein α-synuclein, revealing its effectiveness in studying ion binding and aggregation properties in proteins.
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Background: Myotonic dystrophy type 1 (DM1) is a multisystem genetic disorder that classically presents with symptoms associated with myotonia, early onset cataracts, and muscular weakness, although the presentation and pattern of disease progression is quite varied. Presenting symptoms are well documented among adults with DM1. However, less is known about the co-occurrence of symptoms over time.

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Preeclampsia is a multisystem disorder associated with defective trophoblast invasion, maternal syndrome, and capillary endothelial leak. The presence of ascites/third space fluid accumulation increases the risk of maternal morbidity and mortality. The current criteria/guidelines of preeclampsia do not establish the presence of ascites as a marker of severity or recognize the timing and need for early delivery despite associated complications.

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  • - The bacterial SOS response helps bacteria adapt to DNA damage, including stress from antibiotics, by activating the protein RecA*, which triggers the breakdown of the repressor LexA.
  • - Researchers have determined the structure of the full SOS signal complex in E. coli, revealing how LexA interacts with RecA* at an unexpected interface involving its DNA-binding domain.
  • - The findings highlight a specific residue in RecA that acts as a molecular key for LexA cleavage, shedding light on the SOS response's pro-mutagenic effects and aiding in potential therapeutic strategies against antibiotic resistance.
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