Year |
Citation |
Score |
2020 |
Chen C, Park C. Chaperone Action of a Cofactor in Protein Folding. Protein Science : a Publication of the Protein Society. PMID 32385904 DOI: 10.1002/Pro.3880 |
0.436 |
|
2018 |
Chen C, Liu P, Park C. Chemical Chaperone Activity of NAD+ in Protein Folding Biophysical Journal. 114: 412a. DOI: 10.1016/J.Bpj.2017.11.2286 |
0.59 |
|
2017 |
Gardner NW, McGinness SM, Panchal J, Topp EM, Park C. A cooperative folding unit as the structural link for energetic coupling within a protein. Biochemistry. PMID 29166011 DOI: 10.1021/Acs.Biochem.7B00850 |
0.408 |
|
2017 |
Baek M, Park T, Heo L, Park C, Seok C. GalaxyHomomer: a web server for protein homo-oligomer structure prediction from a monomer sequence or structure. Nucleic Acids Research. PMID 28387820 DOI: 10.1093/Nar/Gkx246 |
0.332 |
|
2017 |
Zeng L, Shin WH, Zhu X, Park SH, Park C, Tao WA, Kihara D. Discovery of Nicotinamide Adenine Dinucleotide Binding Proteins in the Escherichia coli Proteome Using a Combined Energetic- and Structural-Bioinformatics-Based Approach. Journal of Proteome Research. 16: 470-480. PMID 28152599 DOI: 10.1021/Acs.Jproteome.6B00624 |
0.402 |
|
2016 |
Chen C, Yun JH, Kim JH, Park C. Effect of circular permutations on transient partial unfolding in proteins. Protein Science : a Publication of the Protein Society. PMID 27164316 DOI: 10.1002/Pro.2945 |
0.427 |
|
2016 |
Gardner NW, Monroe LK, Kihara D, Park C. Energetic Coupling between Ligand Binding and Dimerization in E. coli Phosphoglycerate Mutase. Biochemistry. PMID 26919584 DOI: 10.1021/Acs.Biochem.5B00980 |
0.397 |
|
2016 |
Hinzman MW, Essex ME, Park C. Salt bridge as a gatekeeper against partial unfolding. Protein Science : a Publication of the Protein Society. PMID 26916981 DOI: 10.1002/Pro.2908 |
0.362 |
|
2015 |
Kasper JR, Park C. Ligand binding to a high-energy partially unfolded protein. Protein Science : a Publication of the Protein Society. 24: 129-37. PMID 25367157 DOI: 10.1002/Pro.2596 |
0.598 |
|
2014 |
Schlebach JP, Woodall NB, Bowie JU, Park C. Bacteriorhodopsin folds through a poorly organized transition state. Journal of the American Chemical Society. 136: 16574-81. PMID 25369295 DOI: 10.1021/Ja508359N |
0.719 |
|
2014 |
Kasper JR, Andrews EC, Park C. Product inhibition in native-state proteolysis. Plos One. 9: e111416. PMID 25360755 DOI: 10.1371/Journal.Pone.0111416 |
0.603 |
|
2014 |
Kasper JR, Liu PF, Park C. Structure of a partially unfolded form of Escherichia coli dihydrofolate reductase provides insight into its folding pathway. Protein Science : a Publication of the Protein Society. 23: 1728-37. PMID 25252157 DOI: 10.1002/Pro.2555 |
0.69 |
|
2014 |
Schlebach JP, Woodall NB, Bowie JU, Park C. Bacteriorhodopsin folds through a poorly organized transition state Journal of the American Chemical Society. 136: 16574-16581. DOI: 10.1021/ja508359n |
0.65 |
|
2012 |
Chang Y, Schlebach JP, VerHeul RA, Park C. Simplified proteomics approach to discover protein-ligand interactions. Protein Science : a Publication of the Protein Society. 21: 1280-7. PMID 22733688 DOI: 10.1002/Pro.2112 |
0.714 |
|
2012 |
Liu PF, Park C. Selective stabilization of a partially unfolded protein by a metabolite. Journal of Molecular Biology. 422: 403-13. PMID 22684147 DOI: 10.1016/J.Jmb.2012.05.044 |
0.645 |
|
2012 |
Schlebach JP, Cao Z, Bowie JU, Park C. Revisiting the folding kinetics of bacteriorhodopsin Protein Science. 21: 97-106. PMID 22095725 DOI: 10.1002/Pro.766 |
0.719 |
|
2012 |
Cao Z, Schlebach JP, Park C, Bowie JU. Thermodynamic stability of bacteriorhodopsin mutants measured relative to the bacterioopsin unfolded state Biochimica Et Biophysica Acta - Biomembranes. 1818: 1049-1054. PMID 21880269 DOI: 10.1016/J.Bbamem.2011.08.019 |
0.719 |
|
2011 |
Liu PF, Kihara D, Park C. Energetics-based discovery of protein-ligand interactions on a proteomic scale. Journal of Molecular Biology. 408: 147-62. PMID 21338610 DOI: 10.1016/J.Jmb.2011.02.026 |
0.603 |
|
2011 |
Schlebach JP, Kim MS, Joh NH, Bowie JU, Park C. Probing membrane protein unfolding with pulse proteolysis Journal of Molecular Biology. 406: 545-551. PMID 21192947 DOI: 10.1016/J.Jmb.2010.12.018 |
0.706 |
|
2009 |
Chang Y, Park C. Mapping transient partial unfolding by protein engineering and native-state proteolysis. Journal of Molecular Biology. 393: 543-56. PMID 19683000 DOI: 10.1016/J.Jmb.2009.08.006 |
0.437 |
|
2009 |
Youn K, Park C. Investigating the effect of temperature on transient partial unfolding by proteolysis. Protein and Peptide Letters. 16: 1093-7. PMID 19508205 DOI: 10.2174/092986609789055287 |
0.344 |
|
2009 |
Kim MS, Song J, Park C. Determining protein stability in cell lysates by pulse proteolysis and Western blotting. Protein Science : a Publication of the Protein Society. 18: 1051-9. PMID 19388050 DOI: 10.1002/Pro.115 |
0.406 |
|
2009 |
Liu PF, Avramova LV, Park C. Revisiting absorbance at 230nm as a protein unfolding probe. Analytical Biochemistry. 389: 165-70. PMID 19318083 DOI: 10.1016/J.Ab.2009.03.028 |
0.631 |
|
2009 |
Na YR, Park C. Investigating protein unfolding kinetics by pulse proteolysis. Protein Science : a Publication of the Protein Society. 18: 268-76. PMID 19177560 DOI: 10.1002/Pro.29 |
0.452 |
|
2007 |
Park C, Zhou S, Gilmore J, Marqusee S. Energetics-based protein profiling on a proteomic scale: identification of proteins resistant to proteolysis. Journal of Molecular Biology. 368: 1426-37. PMID 17400245 DOI: 10.1016/J.Jmb.2007.02.091 |
0.623 |
|
2006 |
Park C, Marqusee S. Quantitative determination of protein stability and ligand binding by pulse proteolysis. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit 20.11. PMID 18429306 DOI: 10.1002/0471140864.Ps2011S46 |
0.618 |
|
2005 |
Park C, Marqusee S. Pulse proteolysis: a simple method for quantitative determination of protein stability and ligand binding. Nature Methods. 2: 207-12. PMID 15782190 DOI: 10.1038/Nmeth740 |
0.641 |
|
2004 |
Park C, Marqusee S. Probing the high energy states in proteins by proteolysis. Journal of Molecular Biology. 343: 1467-76. PMID 15491624 DOI: 10.1016/J.Jmb.2004.08.085 |
0.636 |
|
2004 |
Park C, Marqusee S. Analysis of the stability of multimeric proteins by effective DeltaG and effective m-values. Protein Science : a Publication of the Protein Society. 13: 2553-8. PMID 15322294 DOI: 10.1110/Ps.04811004 |
0.636 |
|
2003 |
Park C, Raines RT. Catalysis by ribonuclease A is limited by the rate of substrate association. Biochemistry. 42: 3509-18. PMID 12653555 DOI: 10.1021/Bi026076K |
0.555 |
|
2002 |
Abel RL, Haigis MC, Park C, Raines RT. Fluorescence assay for the binding of ribonuclease A to the ribonuclease inhibitor protein. Analytical Biochemistry. 306: 100-7. PMID 12069420 DOI: 10.1006/Abio.2002.5678 |
0.678 |
|
2002 |
Leland PA, Staniszewski KE, Park C, Kelemen BR, Raines RT. The ribonucleolytic activity of angiogenin. Biochemistry. 41: 1343-50. PMID 11802736 DOI: 10.1021/Bi0117899 |
0.715 |
|
2001 |
Park C, Raines RT. Adjacent cysteine residues as a redox switch. Protein Engineering. 14: 939-42. PMID 11742114 DOI: 10.1093/Protein/14.11.939 |
0.511 |
|
2001 |
Park C, Raines RT. Quantitative analysis of the effect of salt concentration on enzymatic catalysis. Journal of the American Chemical Society. 123: 11472-9. PMID 11707126 DOI: 10.1021/Ja0164834 |
0.533 |
|
2001 |
Park C, Kelemen BR, Klink TA, Sweeney RY, Behlke MA, Eubanks SR, Raines RT. Fast, facile, hypersensitive assays for ribonucleolytic activity. Methods in Enzymology. 341: 81-94. PMID 11582813 DOI: 10.1016/S0076-6879(01)41146-3 |
0.674 |
|
2001 |
Jardine AM, Leonidas DD, Jenkins JL, Park C, Raines RT, Acharya KR, Shapiro R. Cleavage of 3',5'-pyrophosphate-linked dinucleotides by ribonuclease A and angiogenin. Biochemistry. 40: 10262-72. PMID 11513604 DOI: 10.1021/Bi010888J |
0.546 |
|
2001 |
Park C, Schultz LW, Raines RT. Contribution of the active site histidine residues of ribonuclease A to nucleic acid binding. Biochemistry. 40: 4949-56. PMID 11305910 DOI: 10.1021/bi0100182 |
0.612 |
|
2000 |
Park C, Raines RT. Dimer formation by a "monomeric" protein. Protein Science : a Publication of the Protein Society. 9: 2026-33. PMID 11106177 DOI: 10.1110/Ps.9.10.2026 |
0.591 |
|
2000 |
Park C, Raines RT. Origin of the 'inactivation' of ribonuclease A at low salt concentration. Febs Letters. 468: 199-202. PMID 10692586 DOI: 10.1016/S0014-5793(00)01227-8 |
0.512 |
|
1998 |
Quirk DJ, Park C, Thompson JE, Raines RT. His...Asp catalytic dyad of ribonuclease A: conformational stability of the wild-type, D121N, D121A, and H119A enzymes. Biochemistry. 37: 17958-64. PMID 9922164 DOI: 10.1021/Bi981688J |
0.751 |
|
1995 |
Song T, Park C. Effect of folding on the export of ribose-binding protein studied with the genetically isolated suppressors for the signal sequence mutation Journal of Molecular Biology. 253: 304-312. PMID 7563091 DOI: 10.1006/jmbi.1995.0554 |
0.301 |
|
Show low-probability matches. |