Ragunathan Priya

Employment

• Nanyang Technological University Research fellow
  2013 - Present

Education

• Nanyang Technological University Ph.D
  2007 - 2010

Projects & Funding

Projects & funding information is unavailable.

Publications (13)

• Variations of the Mycobacterium abscessus F-ATP synthase subunit a-c interface alter binding and potency of the anti-TB drug bedaquiline
  Biochemical and Biophysical Research Communications 2024 DOI: 10.1016/j.bbrc.2023.149249
  +Save
• Mycobacterial F-ATP Synthase: From Structures to Target Sites to Inhibitors
  Amaravadhi Harikishore, Chui Fann Wong, Priya Ragunathan +3 more
  2024 DOI: 10.1007/978-981-97-1777-4_5
  +Save
• GaMF1.39’s antibiotic efficacy and its enhanced antitubercular activity in combination with clofazimine, Telacebec, ND-011992, or TBAJ-876
  Priya Ragunathan, Pearly Shuyi Ng, Samsher Singh +13 more
  Microbiology Spectrum 2023 DOI: 10.1128/spectrum.02282-23
  +Save
• Structural and Mechanistic Insights into Mycobacterium abscessus Aspartate Decarboxylase PanD and a Pyrazinoic Acid-Derived Inhibitor
  Wuan Geok Saw, Chen Yen Leow, Amaravadhi Harikishore +8 more
  ACS Infectious Diseases 2022 DOI: 10.1021/acsinfecdis.2c00133
  +Save
• Atomic structure of and valine binding to the regulatory ACT domain of the Mycobacterium tuberculosis Rel protein
  Joon Su Shin, Bharti Singal, Malathy Sony Subramanian Manimekalai +3 more
  The FEBS Journal 2021 DOI: 10.1111/febs.15600
  +Save
• A systematic assessment of mycobacterial F1‐ATPase subunit ε’s role in latent ATPase hydrolysis
  The FEBS Journal 2021 DOI: 10.1111/febs.15440
  +Save
• Discovery of a Novel Mycobacterial F‐ATP Synthase Inhibitor and its Potency in Combination with Diarylquinolines
  Adam Hotra, Priya Ragunathan, Pearly Shuyi Ng +20 more
  Angewandte Chemie International Edition 2020 DOI: 10.1002/anie.202002546
  +Save
• Discovery of a Novel Mycobacterial F‐ATP Synthase Inhibitor and its Potency in Combination with Diarylquinolines
  Angewandte Chemie 2020 DOI: 10.1002/ange.202002546
  +Save
• Solution structure of subunit γ (γ(1-204)) of the Mycobacterium tuberculosis F-ATP synthase and the unique loop of γ(165-178), representing a novel TB drug target.
  Journal of Bioenergitics and Biomembranes 2013
  +Save
• Conserved glycine residues in the P-loop of ATP synthases form a doorframe for nucleotide entrance.
  Journal of molecular biology 2011
  +Save
• The critical roles of residues P235 and F236 of subunit A of the motor protein A-ATP synthase in P-loop formation and nucleotide binding.
  Journal of Molecular Biology 2010
  +Save
• Solution structure, determined by nuclear magnetic resonance, of the b30-82 domain of subunit b of Escherichia coli F1Fo ATP synthase.
  Journal of Bacteriology 2009
  +Save
• Low resolution structure of subunit b (b (22-156)) of Escherichia coli F(1)F(O) ATP synthase in solution and the b-delta assembly.
  Journal of Bioenergitics Biomembranes 2008
  +Save