Publications by authors named "I Yu Oganesyan"

Article Synopsis
  • Investigating snake venom is crucial for creating new treatments and leveraging the benefits of venom toxins, despite challenges in analyzing their complex mixtures.
  • This study introduces advanced techniques like ion mobility spectrometry and top-down mass spectrometry to effectively analyze individual venom proteins from King cobra venom.
  • The research successfully identifies and characterizes various proteins, including a glycan-containing toxin and a β-cardiotoxin, demonstrating the potential of these cutting-edge methodologies in venom analysis.
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Background: Brazil is home to a multitude of venomous snakes; perhaps the most medically relevant of which belong to the Bothrops genus. Bothrops spp. are responsible for roughly 70% of all snakebites in Brazil, and envenomings caused by their bites can be treated with three types of antivenom: bothropic antivenom, bothro-lachetic antivenom, and bothro-crotalic antivenom.

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Snakebite envenoming continues to claim many lives across the globe, necessitating the development of improved therapies. To this end, broadly-neutralizing human monoclonal antibodies may possess advantages over current plasma-derived antivenoms by offering superior safety and high neutralization capacity. Here, we report the establishment of a pipeline based on phage display technology for the discovery and optimization of high affinity broadly-neutralizing human monoclonal antibodies.

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Metformin is a first-line antidiabetic drug for the treatment of type 2 diabetes mellitus (DM2); its molecular target is AMP-activated protein kinase (AMPK), which is involved in many metabolic processes. Metformin not only reduces blood glucose levels and improves insulin sensitivity, but also inhibits lipolysis and reduces cardiovascular risk in patients with DM2. In recent years, it has been proven that metformin slows down the aging process, stimulates hair growth, eliminates cognitive impairment, and also has an antitumor effect.

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Structural isomers of -glycans that are identical in mass and atomic composition provide a great challenge to conventional mass spectrometry (MS). This study employs additional dimensions of structural elucidation including ion mobility (IM) spectroscopy coupled to hydrogen/deuterium exchange (HDX) and electron capture dissociation (ECD) to characterize three main A2 -glycans and their conformers. A series of IM-MS experiments were able to separate the low abundance -glycans and their linkage-based isomers (α1-3 and α1-6 for A2G1).

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