Natalia Oganesyan
Papers
2
Total Citations
81
H-Index
2
About
Natalia Oganesyan is a structural biologist whose work has advanced our understanding of key metabolic enzymes and protein production technologies. Her research focuses on the structure and function of nicotinate phosphoribosyltransferases (NAPRTases), enzymes critical to the NAD+ salvage pathway. In her landmark 2005 study (38 citations), she determined the crystal structure of NAPRTase from *Thermoplasma acidophilum*, revealing a three-domain architecture—including a unique C-terminal domain—that provided fundamental insights into how this enzyme recognizes substrates and catalyzes a key step in NAD+ biosynthesis. This structural work has implications for understanding metabolism in thermophilic organisms and for targeting similar pathways in pathogens. Complementing her structural studies, Oganesyan made a significant methodological contribution with her 2004 paper (43 citations) on an automated small-scale protein expression and purification screening system. This practical tool has helped researchers rapidly identify optimal conditions for producing soluble, stable proteins—a critical bottleneck in structural biology and drug discovery. Her work exemplifies how combining structural determination with innovative protein production methods can accelerate biological discovery.
Research Focus
Key Achievements
Top Papers
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