Suman Mishra, PhD
MRC Laboratory of Molecular Biology, Indian Institute of Science Bangalore, D.Y. Patil University, Navi Mumbai
About
I am a structural biologist interested in understanding different aspects of protein folding in pathology. Currently, I am a postdoctoral scientist working with Dr. Benjamin Ryskeldi-Falcon at MRC-Laboratory of Molecular Biology, where I am developing better in vitro models for amyloidogenic proteins in disease. I did my PhD from the Molecular Biophysics Unit at the Indian Institute of Science, Bangalore where I employed single-particle cryo-EM to investigate mechanistic aspects of several bacterial pore-forming toxins from the Staphylococcus and Vibrio genera in a lipid membrane environment.
Employment
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MRC Laboratory of Molecular Biology MRC Career Development Fellow2025 - Present
Education
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Indian Institute of Science Bangalore Master of Science- Research, MS(Res)2019 - 2024
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Indian Institute of Science Bangalore Doctor of Philosophy, PhD2019 - 2024
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D.Y. Patil University, Navi Mumbai Bachelor of Technology (B.Tech) in Biotechnology2015 - 2019
Projects & Funding
Projects & funding information is unavailable.
Publications (9)
- Membrane Curvature During Membrane Rupture and Formation of Pentagonal Pyramidal Superassemblies by a Pore‐Forming Toxin, Vibrio cholerae Cytolysin, Using Single Particle Cryo‐EM Save
- Membrane curvature during membrane rupture and formation of pentagonal pyramidal superassemblies by a pore-forming toxin, Vibrio cholerae Cytolysin, using single particle cryo-EM Save
- Membrane Rupture and Lipid–Protein Interaction of γ-Hemolysin from Staphylococcus aureus Using Cryo-EM Save
- Emerging Trends in Cryo-EM-based Structural Studies of Neuropathological Amyloids Save
- Cryo-EM-based structural insights into supramolecular assemblies of γ-hemolysin from S. aureus reveal the pore formation mechanism Save
- Structural insights into thermostable direct hemolysin of Vibrio parahaemolyticus using single‐particle cryo‐EM Save
- Cryo-EM-based structural insights into supramolecular assemblies of γ-Hemolysin from Staphylococcus aureus reveal the pore formation mechanism Save
- Single-particle cryo-EM reveals conformational variability of the oligomeric VCC β-barrel pore in a lipid bilayer Save
- Conformational flexibility and structural variability of SARS-CoV2 S protein Save