Molecular machines and their assemblies range 10-100 nm in size and perform extremely complex but critical actions within the cell. Cryo-Electron microscopy (Cryo-EM) has now overcome many biophysical hurdles and finally become a major strategy in structural biology. Our research focus is driven by a diverse spectrum of challenging biological topics and to explore functional mechanism of molecular machines by achieving high resolution structures.
- Walsh RW Jr*., Roh SH*, Gharpure A, Morales-Perez CL, Hibbs RE. “Structural principles of distinct assemblies of the human α4β2 nicotinic receptor.” Nature 2018. doi:10.1038/s41586-018-0081-7. PMID:29720657
- Roh SH, Stam NJ, Hryc CF, Couoh-Cardel S, Pintilie G, Chiu W, Wilkens S. “The 3.5-Å Cryo-EM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase Vo Proton Channel.” Molecular Cell. 2018. S1097-2765(18)30104-7. PMID:29526695
- Roh SH, Hryc CF, Jeong HH, Fei X, Jakana J, Lorimer GH, Chiu W. “Subunit conformational variation within individual GroEL oligomers resolved by Cryo-EM.” Proceedings of the National Academy of Sciences of the United States of America. 2017; 114(31):8259-8264. PMID: 28710336
- Roh SH, Kasembeli MM, Galaz-Montoya JG, Chiu W, Tweardy DJ. “Chaperonin TRiC/CCT Recognizes Fusion Oncoprotein AML1-ETO through Subunit-Specific Interactions.” Biophysical journal. 2016; 110(11):2377-2385. PMID: 27276256
- Roh SH, Kasembeli M, Galaz-Montoya JG, Trnka M, Lau WC, Burlingame A, Chiu W, Tweardy DJ. “Chaperonin TRiC/CCT Modulates the Folding and Activity of Leukemogenic Fusion Oncoprotein AML1-ETO.” The Journal of biological chemistry. 2016; 291(9):4732-41. PMID: 26706127