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Jae-Hyun Cho, Ph.D. - Publications

Affiliations: 
2006 Stony Brook University, Stony Brook, NY, United States 
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37 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2021 Dubrow A, Kim I, Topo E, Cho JH. Understanding the Binding Transition State After the Conformational Selection Step: The Second Half of the Molecular Recognition Process Between NS1 of the 1918 Influenza Virus and Host p85β. Frontiers in Molecular Biosciences. 8: 716477. PMID 34307465 DOI: 10.3389/fmolb.2021.716477  0.386
2020 Shi J, Shen Q, Cho JH, Hwang W. Entropy Hotspots for the Binding of Intrinsically Disordered Ligands to a Receptor Domain. Biophysical Journal. PMID 32311315 DOI: 10.1016/J.Bpj.2020.03.026  0.446
2020 Dubrow A, Lin S, Savage N, Shen Q, Cho JH. Molecular Basis of the Ternary Interaction between NS1 of the 1918 Influenza A Virus, PI3K, and CRK. Viruses. 12. PMID 32244879 DOI: 10.3390/V12030338  0.374
2020 Cho JH, Zhao B, Shi J, Savage N, Shen Q, Byrnes J, Yang L, Hwang W, Li P. Molecular recognition of a host protein by NS1 of pandemic and seasonal influenza A viruses. Proceedings of the National Academy of Sciences of the United States of America. PMID 32152123 DOI: 10.1073/Pnas.1920582117  0.388
2020 Shi J, Cho J, Hwang W. Calculation of Backbone and Side Chain Conformational Entropy Changes Upon Binding of Proline-Rich Motifs to SH3 Domain Biophysical Journal. 118: 48a. DOI: 10.1016/J.Bpj.2019.11.445  0.394
2019 Shen Q, Cho JH. The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus. Biochemical and Biophysical Research Communications. PMID 31420169 DOI: 10.2210/Pdb6Nu0/Pdb  0.365
2018 Shen Q, Bhatt VS, Krieger I, Sacchettini JC, Cho JH. Structure-guided design of a potent peptide inhibitor targeting the interaction between CRK and ABL kinase. Medchemcomm. 9: 519-524. PMID 30108942 DOI: 10.1039/C7Md00619E  0.303
2018 Shen Q, Shi J, Zeng D, Zhao B, Li P, Hwang W, Cho JH. Molecular Mechanisms of Tight Binding through Fuzzy Interactions. Biophysical Journal. 114: 1313-1320. PMID 29590589 DOI: 10.1016/J.Bpj.2018.01.031  0.45
2017 Sato S, Cho JH, Peran I, Soydaner-Azeloglu RG, Raleigh DP. The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State. Biophysical Journal. 112: 1797-1806. PMID 28494951 DOI: 10.1016/J.Bpj.2017.01.034  0.763
2017 Shen Q, Zeng D, Zhao B, Bhatt VS, Li P, Cho JH. The molecular mechanisms underlying the hijack of host proteins by the 1918 Spanish influenza virus. Acs Chemical Biology. PMID 28368102 DOI: 10.1021/Acschembio.7B00168  0.437
2017 Zeng D, Shen Q, Cho JH. Thermodynamic contribution of backbone conformational entropy in the binding between SH3 domain and proline-rich motif. Biochemical and Biophysical Research Communications. PMID 28111343 DOI: 10.1016/J.Bbrc.2017.01.089  0.488
2017 Shen Q, Zeng D, Cho J. Binding Mechanism between CrkII and cAbl Kinase Biophysical Journal. 112. DOI: 10.1016/J.Bpj.2016.11.1114  0.407
2016 Zeng D, Bhatt VS, Shen Q, Cho JH. Kinetic Insights into the Binding between the nSH3 Domain of CrkII and Proline-Rich Motifs in cAbl. Biophysical Journal. 111: 1843-1853. PMID 27806266 DOI: 10.1016/J.Bpj.2016.09.029  0.452
2016 Bhatt VS, Zeng D, Krieger I, Sacchettini JC, Cho JH. Binding Mechanism of the N-Terminal SH3 Domain of CrkII and Proline-Rich Motifs in cAbl. Biophysical Journal. 110: 2630-2641. PMID 27332121 DOI: 10.1016/J.Bpj.2016.05.008  0.439
2014 Cho JH, Meng W, Sato S, Kim EY, Schindelin H, Raleigh DP. Energetically significant networks of coupled interactions within an unfolded protein. Proceedings of the National Academy of Sciences of the United States of America. 111: 12079-84. PMID 25099351 DOI: 10.1073/Pnas.1402054111  0.79
2013 Stafford KA, Ferrage F, Cho JH, Palmer AG. Side chain dynamics of carboxyl and carbonyl groups in the catalytic function of Escherichia coli ribonuclease H. Journal of the American Chemical Society. 135: 18024-7. PMID 24219366 DOI: 10.1021/Ja409479Y  0.363
2011 Cho JH, Muralidharan V, Vila-Perello M, Raleigh DP, Muir TW, Palmer AG. Tuning protein autoinhibition by domain destabilization. Nature Structural & Molecular Biology. 18: 550-5. PMID 21532593 DOI: 10.1038/Nsmb.2039  0.664
2010 Cho JH, O'Connell N, Raleigh DP, Palmer AG. Phi-value analysis for ultrafast folding proteins by NMR relaxation dispersion. Journal of the American Chemical Society. 132: 450-1. PMID 20028088 DOI: 10.1021/Ja909052H  0.622
2009 Cho JH, Raleigh DP. Experimental characterization of the denatured state ensemble of proteins. Methods in Molecular Biology (Clifton, N.J.). 490: 339-51. PMID 19157090 DOI: 10.1007/978-1-59745-367-7_14  0.708
2009 Trbovic N, Cho JH, Abel R, Friesner RA, Rance M, Palmer AG. Protein side-chain dynamics and residual conformational entropy. Journal of the American Chemical Society. 131: 615-22. PMID 19105660 DOI: 10.1021/Ja806475K  0.387
2009 Raleigh DP, Shan B, Meng W, Cho J, Taskent H. Characterization of the Unfolded State Under Native Conditions: A Missing Piece of the Protein Folding Puzzle Biophysical Journal. 96: 220a. DOI: 10.1016/J.Bpj.2008.12.1921  0.781
2008 Taskent H, Cho JH, Raleigh DP. Temperature-dependent Hammond behavior in a protein-folding reaction: analysis of transition-state movement and ground-state effects. Journal of Molecular Biology. 378: 699-706. PMID 18384809 DOI: 10.1016/J.Jmb.2008.02.024  0.627
2008 Cho JH, Sato S, Horng JC, Anil B, Raleigh DP. Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Archives of Biochemistry and Biophysics. 469: 20-8. PMID 17900519 DOI: 10.1016/J.Abb.2007.08.004  0.783
2007 Song B, Cho JH, Raleigh DP. Ionic-strength-dependent effects in protein folding: analysis of rate equilibrium free-energy relationships and their interpretation. Biochemistry. 46: 14206-14. PMID 18001140 DOI: 10.1021/Bi701645G  0.662
2007 Bi Y, Cho JH, Kim EY, Shan B, Schindelin H, Raleigh DP. Rational design, structural and thermodynamic characterization of a hyperstable variant of the villin headpiece helical subdomain. Biochemistry. 46: 7497-505. PMID 17536785 DOI: 10.1021/Bi6026314  0.693
2007 Li Y, Gupta R, Cho JH, Raleigh DP. Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology. Biochemistry. 46: 1013-21. PMID 17240985 DOI: 10.1021/Bi061516J  0.685
2006 Cho JH, Raleigh DP. Denatured state effects and the origin of nonclassical phi values in protein folding. Journal of the American Chemical Society. 128: 16492-3. PMID 17177385 DOI: 10.1021/Ja0669878  0.609
2006 Anil B, Li Y, Cho JH, Raleigh DP. The unfolded state of NTL9 is compact in the absence of denaturant. Biochemistry. 45: 10110-6. PMID 16906769 DOI: 10.1021/Bi060636O  0.792
2006 Abedini A, Tracz SM, Cho JH, Raleigh DP. Characterization of the heparin binding site in the N-terminus of human pro-islet amyloid polypeptide: implications for amyloid formation. Biochemistry. 45: 9228-37. PMID 16866369 DOI: 10.1021/Bi0510936  0.704
2006 Muralidharan V, Dutta K, Cho J, Vila-Perello M, Raleigh DP, Cowburn D, Muir TW. Solution structure and folding characteristics of the C-terminal SH3 domain of c-Crk-II. Biochemistry. 45: 8874-84. PMID 16846230 DOI: 10.1021/Bi060590Z  0.608
2006 Cho JH, Raleigh DP. 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: 1437-46. PMID 16787780 DOI: 10.1016/J.Jmb.2006.04.038  0.684
2006 Bi Y, Tang Y, Raleigh DP, Cho JH. 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: 234-40. PMID 16325421 DOI: 10.1016/J.Pep.2005.10.023  0.704
2005 Anil B, Sato S, Cho JH, Raleigh DP. Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. Journal of Molecular Biology. 354: 693-705. PMID 16246369 DOI: 10.1016/J.Jmb.2005.08.054  0.782
2005 Cho JH, Raleigh DP. Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins. Journal of Molecular Biology. 353: 174-85. PMID 16165156 DOI: 10.1016/J.Jmb.2005.08.019  0.705
2005 Horng JC, Cho JH, Raleigh DP. 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: 163-73. PMID 15567419 DOI: 10.1016/J.Jmb.2004.10.023  0.716
2004 Muralidharan V, Cho J, Trester-Zedlitz M, Kowalik L, Chait BT, Raleigh DP, Muir TW. Domain-specific incorporation of noninvasive optical probes into recombinant proteins. Journal of the American Chemical Society. 126: 14004-12. PMID 15506763 DOI: 10.1021/Ja0466199  0.602
2004 Cho JH, Sato S, Raleigh DP. 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: 827-37. PMID 15099748 DOI: 10.1016/J.Jmb.2004.02.073  0.77
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