Rahul Yadav
Affiliation confirmed via AI analysis of OpenAlex, ORCID, and web sources.
Assistant Professor Chemistry/Biochemistry
Also affiliated: University of Kansas (2016); Central Drug Research Institute (2011–2020); University of Michigan (2017–2021); Indian Institute of Science Education and Research, Bhopal (2021–2025); Wichita State University (2005–2025); Vellore Institute of Technology University (2025–2026); Banaras Hindu University (2025–2026); Mississippi State University (2020–2026)
Research Areas
Biomedical Subjects
Links
Biography and Research Information
OverviewAI-generated summary
Rahul Yadav's research investigates the structural and functional aspects of steroidogenic cytochrome P450 enzymes, particularly CYP17A1. His work includes the structure-based design of inhibitors to improve selectivity for CYP17A1 over related enzymes like CYP21A2. He also explores the application of biomolecular NMR spectroscopy and molecular docking simulations to understand protein binding and dynamics, as evidenced by his studies on bacterial proteins and the solution structure of ADF from *Toxoplasma gondii*. Further research interests include the development of novel materials, such as copper nanoclusters for white light generation and Al2O3 nanofluids for grinding applications. Yadav has published over 120 works, with an h-index of 18 and more than 1,000 citations. He has collaborated with researchers at the University of Arkansas – Fort Smith, including Luke Jodoin and Archana Mishra.
Metrics
- h-index: 15
- Publications: 64
- Citations: 586
Positions
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Assistant Professor Chemistry/Biochemistry 2022–presentUniversity of Arkansas – Fort Smith Chemistry ORCID
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Mississippi State University 2019–2022Chemistry ORCID
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Postdoc 2016–2019University of Michigan Medicinal Chemistry ORCID
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Postdoc 2015–2016University of Kansas Medicinal chemistry ORCID
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Postdoc 2013–2015Wichita State University Chemistry ORCID
Selected Publications
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The Mechanism of R2ab-mediated Attachment to Polystyrene Surfaces in Staphylococcus epidermidis (2026)
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Investigating Quinclorac Binding to Human Serum Albumin using Spectroscopy and Molecular Docking (2026)
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Human Serum Albumin Interaction with Organochlorine Pesticides (2026)
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DATASET: The S. epidermidis Amidase Domain Uses Distinct Interfaces to Mediate Surface Attachment in Biofilm Formation (2026)
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DATASET: The S. epidermidis Amidase Domain Uses Distinct Interfaces to Mediate Surface Attachment in Biofilm Formation (2026)
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Investigating Quinclorac Binding to Human Serum Albumin using Spectroscopy and Molecular Docking (2026)
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Human Serum Albumin Interaction with Organochlorine Pesticides (2025)Journal of the Arkansas Academy of Science OpenAlex
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Integrated structural model of the palladin–actin complex using XL ‐ MS , docking, NMR , and SAXS (2025)
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Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS (2024)
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NMR Experiments for Measuring RDCs in Biomolecules (2024)
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1H, 15N, and 13C chemical shift backbone resonance NMR assignment of the accumulation-associated protein (Aap) lectin domain from Staphylococcus epidermidis (2023)
Collaboration Network
Top Collaborators
- 1H, 15N, and 13C chemical shift backbone resonance NMR assignment of the accumulation-associated protein (Aap) lectin domain from Staphylococcus epidermidis
- NMR Experiments for Measuring RDCs in Biomolecules
- DATASET: The S. epidermidis Amidase Domain Uses Distinct Interfaces to Mediate Surface Attachment in Biofilm Formation
- DATASET: The S. epidermidis Amidase Domain Uses Distinct Interfaces to Mediate Surface Attachment in Biofilm Formation
- The Mechanism of R2ab-mediated Attachment to Polystyrene Surfaces in Staphylococcus epidermidis
- DATASET: The S. epidermidis Amidase Domain Uses Distinct Interfaces to Mediate Surface Attachment in Biofilm Formation
- DATASET: The S. epidermidis Amidase Domain Uses Distinct Interfaces to Mediate Surface Attachment in Biofilm Formation
- The Mechanism of R2ab-mediated Attachment to Polystyrene Surfaces in Staphylococcus epidermidis
- Integrated structural model of the palladin–actin complex using XL ‐ MS , docking, NMR , and SAXS
- Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS
- Integrated structural model of the palladin–actin complex using XL ‐ MS , docking, NMR , and SAXS
- Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS
- Integrated structural model of the palladin–actin complex using XL ‐ MS , docking, NMR , and SAXS
- Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS
- Integrated structural model of the palladin–actin complex using XL ‐ MS , docking, NMR , and SAXS
- Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS
- Integrated structural model of the palladin–actin complex using XL ‐ MS , docking, NMR , and SAXS
- Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS
- Integrated structural model of the palladin–actin complex using XL ‐ MS , docking, NMR , and SAXS
- Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS
- Investigating Quinclorac Binding to Human Serum Albumin using Spectroscopy and Molecular Docking
- The Mechanism of R2ab-mediated Attachment to Polystyrene Surfaces in Staphylococcus epidermidis
- DATASET: The S. epidermidis Amidase Domain Uses Distinct Interfaces to Mediate Surface Attachment in Biofilm Formation
- DATASET: The S. epidermidis Amidase Domain Uses Distinct Interfaces to Mediate Surface Attachment in Biofilm Formation
- DATASET: The S. epidermidis Amidase Domain Uses Distinct Interfaces to Mediate Surface Attachment in Biofilm Formation
- DATASET: The S. epidermidis Amidase Domain Uses Distinct Interfaces to Mediate Surface Attachment in Biofilm Formation
- DATASET: The S. epidermidis Amidase Domain Uses Distinct Interfaces to Mediate Surface Attachment in Biofilm Formation
- DATASET: The S. epidermidis Amidase Domain Uses Distinct Interfaces to Mediate Surface Attachment in Biofilm Formation
- DATASET: The S. epidermidis Amidase Domain Uses Distinct Interfaces to Mediate Surface Attachment in Biofilm Formation
- DATASET: The S. epidermidis Amidase Domain Uses Distinct Interfaces to Mediate Surface Attachment in Biofilm Formation
- DATASET: The S. epidermidis Amidase Domain Uses Distinct Interfaces to Mediate Surface Attachment in Biofilm Formation
- DATASET: The S. epidermidis Amidase Domain Uses Distinct Interfaces to Mediate Surface Attachment in Biofilm Formation
- 1H, 15N, and 13C chemical shift backbone resonance NMR assignment of the accumulation-associated protein (Aap) lectin domain from Staphylococcus epidermidis
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