Cho, Jae Assistant Professor

academic article

• Shi, J., Shen, Q., Cho, J., & Hwang, W. (2020). Entropy Hotspots for the Binding of Intrinsically Disordered Ligands to a Receptor Domain. Biophysical Journal.  118(10), 2502-2512.
  
• Shen, Q., & Cho, J. (2019). The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus. Biochemical and Biophysical Research Communications.  518(1), 178-182.
  
• Shen, Q., Bhatt, V. S., Krieger, I., Sacchettini, J. C., & Cho, J. (2018). Structure-guided design of a potent peptide inhibitor targeting the interaction between CRK and ABL kinase. MedChemComm.  9(3), 519-524.
  
• Shen, Q., Shi, J., Zeng, D., Zhao, B., Li, P., Hwang, W., & Cho, J. (2018). Molecular Mechanisms of Tight Binding through Fuzzy Interactions. Biophysical Journal.  114(6), 1313-1320.
  
• Shen, Q., Zeng, D., Zhao, B., Bhatt, V. S., Li, P., & Cho, J. (2017). The Molecular Mechanisms Underlying the Hijack of Host Proteins by the 1918 Spanish Influenza Virus. ACS Chemical Biology.  12(5), 1199-1203.
  
• Sato, S., Cho, J., Peran, I., Soydaner-Azeloglu, R. G., & Raleigh, D. P. (2017). The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State. Biophysical Journal.  112(9), 1797-1806.
  
• Zeng, D., Shen, Q., & Cho, J. (2017). Thermodynamic contribution of backbone conformational entropy in the binding between SH3 domain and proline-rich motif. Biochemical and Biophysical Research Communications.  484(1), 21-26.
  
• Bhatt, V. S., Zeng, D., Krieger, I., Sacchettini, J. C., & Cho, J. (2016). Binding Mechanism of the N-Terminal SH3 Domain of CrkII and Proline-Rich Motifs in cAbl. Biophysical Journal.  110(12), 2630-2641.
  
• Zeng, D., Bhatt, V. S., Shen, Q., & Cho, J. (2016). Kinetic Insights into the Binding between the nSH3 Domain of CrkII and Proline-Rich Motifs in cAbl. Biophysical Journal.  111(9), 1843-1853.
  
• Cho, J., Meng, W., Sato, S., Kim, E. Y., Schindelin, H., & Raleigh, D. P. (2014). Energetically significant networks of coupled interactions within an unfolded protein. Proceedings of the National Academy of Sciences of the United States of America.  111(33), 12079-12084.
  
• Stafford, K. A., Ferrage, F., Cho, J., & Palmer, A. G. (2013). Side chain dynamics of carboxyl and carbonyl groups in the catalytic function of Escherichia coli ribonuclease H. Journal of the American Chemical Society.  135(48), 18024-18027.
  
• Cho, J., Muralidharan, V., Vila-Perello, M., Raleigh, D. P., Muir, T. W., & Palmer, A. G. (2011). Tuning protein autoinhibition by domain destabilization. Nature Structural and Molecular Biology.  18(5), 550-555.
  
• Cho, J., O'Connell, N., Raleigh, D. P., & Palmer, A. G. (2009). ϕ-Value Analysis for Ultrafast Folding Proteins by NMR Relaxation Dispersion. Journal of the American Chemical Society.  132(2), 450-451.
  
• Cho, J., & Raleigh, D. P. (2009). Experimental characterization of the denatured state ensemble of proteins. 490, 339-351.
  
• Trbovic, N., Cho, J., Abel, R., Friesner, R. A., Rance, M., & Palmer, A. G. (2008). Protein Side-Chain Dynamics and Residual Conformational Entropy. Journal of the American Chemical Society.  131(2), 615-622.
  
• Taskent, H., Cho, J., & Raleigh, D. P. (2008). Temperature-dependent Hammond behavior in a protein-folding reaction: analysis of transition-state movement and ground-state effects. Journal of Molecular Biology.  378(3), 699-706.
  
• Cho, J., Sato, S., Horng, J., Anil, B., & Raleigh, D. P. (2008). Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Archives of Biochemistry and Biophysics.  469(1), 20-28.
  
• Song, B., Cho, J., & Raleigh, D. P. (2007). Ionic-Strength-Dependent Effects in Protein Folding: Analysis of Rate Equilibrium Free-Energy Relationships and Their Interpretation †. Biochemistry.  46(49), 14206-14214.
  
• Li, Y., Gupta, R., Cho, J., & Raleigh, D. P. (2007). Mutational Analysis of the Folding Transition State of the C-Terminal Domain of Ribosomal Protein L9: A Protein with an Unusual β-Sheet Topology †. Biochemistry.  46(4), 1013-1021.
  
• Bi, Y., Cho, J., Kim, E., Shan, B., Schindelin, H., & Raleigh, D. P. (2007). Rational design, structural and thermodynamic characterization of a hyperstable variant of the villin headpiece helical subdomain. Biochemistry.  46(25), 7497-7505.
  
• Muralidharan, V., Dutta, K., Cho, J., Vila-Perello, M., Raleigh, D. P., Cowburn, D., & Muir, T. W. (2006). Solution Structure and Folding Characteristics of the C-Terminal SH3 Domain of c-Crk-II † , ‡. Biochemistry.  45(29), 8874-8884.
  
• Bi, Y., Tang, Y., Raleigh, D. P., & Cho, J. (2006). Efficient high level expression of peptides and proteins as fusion proteins with the N-terminal domain of L9: application to the villin headpiece helical subdomain. Protein Expression and Purification.  47(1), 234-240.
  
• Abedini, A., Tracz, S. M., Cho, J., & Raleigh, D. P. (2006). Characterization of the Heparin Binding Site in the N-Terminus of Human Pro-Islet Amyloid Polypeptide: Implications for Amyloid Formation †. Biochemistry.  45(30), 9228-9237.
  
• Cho, J., & Raleigh, D. P. (2006). Denatured State Effects and the Origin of Nonclassical φ Values in Protein Folding. Journal of the American Chemical Society.  128(51), 16492-16493.
  
• Cho, J., & Raleigh, D. P. (2006). Electrostatic interactions in the denatured state and in the transition state for protein folding: effects of denatured state interactions on the analysis of transition state structure. Journal of Molecular Biology.  359(5), 1437-1446.
  
• Anil, B., Li, Y., Cho, J., & Raleigh, D. P. (2006). The Unfolded State of NTL9 Is Compact in the Absence of Denaturant †. Biochemistry.  45(33), 10110-10116.
  
• Horng, J., Cho, J., & Raleigh, D. P. (2005). Analysis of the pH-dependent folding and stability of histidine point mutants allows characterization of the denatured state and transition state for protein folding. Journal of Molecular Biology.  345(1), 163-173.
  
• Anil, B., Sato, S., Cho, J., & Raleigh, D. P. (2005). Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. Journal of Molecular Biology.  354(3), 693-705.
  
• Cho, J., & Raleigh, D. P. (2005). Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins. Journal of Molecular Biology.  353(1), 174-185.
  
• Muralidharan, V., Cho, J., Trester-Zedlitz, M., Kowalik, L., Chait, B. T., Raleigh, D. P., & Muir, T. W. (2004). Domain-Specific Incorporation of Noninvasive Optical Probes into Recombinant Proteins. Journal of the American Chemical Society.  126(43), 14004-14012.
  
• Cho, J., Sato, S., & Raleigh, D. P. (2004). Thermodynamics and kinetics of non-native interactions in protein folding: a single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state. Journal of Molecular Biology.  338(4), 827-837.