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Satoshi Sato, Ph.D. - Publications

Affiliations: 
2002 Stony Brook University, Stony Brook, NY, United States 
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24 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
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  0.76
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  0.767
2009 Huang F, Lerner E, Sato S, Amir D, Haas E, Fersht AR. Time-resolved fluorescence resonance energy transfer study shows a compact denatured state of the b domain of protein A Biochemistry. 48: 3468-3476. PMID 19222162 DOI: 10.1021/Bi801890W  0.403
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  0.736
2007 Sato S, Fersht AR. Searching for Multiple Folding Pathways of a Nearly Symmetrical Protein: Temperature Dependent Φ-Value Analysis of the B Domain of Protein A Journal of Molecular Biology. 372: 254-267. PMID 17628591 DOI: 10.1016/J.Jmb.2007.06.043  0.427
2007 Sato S, Raleigh DP. Kinetic isotope effects reveal the presence of significant secondary structure in the transition state for the folding of the N-terminal domain of L9. Journal of Molecular Biology. 370: 349-55. PMID 17512540 DOI: 10.1016/J.Jmb.2007.02.084  0.655
2007 Scott KA, Alonso DO, Sato S, Fersht AR, Daggett V. Conformational entropy of alanine versus glycine in protein denatured states. Proceedings of the National Academy of Sciences of the United States of America. 104: 2661-6. PMID 17307875 DOI: 10.1073/Pnas.0611182104  0.425
2007 Huang F, Sato S, Sharpe TD, Ying L, Fersht AR. Distinguishing between cooperative and unimodal downhill protein folding. Proceedings of the National Academy of Sciences of the United States of America. 104: 123-7. PMID 17200301 DOI: 10.1073/pnas.0609717104  0.445
2006 Sato S, Religa TL, Fersht AR. Phi-analysis of the folding of the B domain of protein A using multiple optical probes. Journal of Molecular Biology. 360: 850-64. PMID 16782128 DOI: 10.1016/J.Jmb.2006.05.051  0.482
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  0.756
2005 Ferguson N, Sharpe TD, Schartau PJ, Sato S, Allen MD, Johnson CM, Rutherford TJ, Fersht AR. Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family. Journal of Molecular Biology. 353: 427-46. PMID 16168437 DOI: 10.1016/J.Jmb.2005.08.031  0.439
2004 Sato S. [Analysing protein folding transition state using protein engineering]. Tanpakushitsu Kakusan Koso. Protein, Nucleic Acid, Enzyme. 49: 2230-4. PMID 15559307  0.354
2004 Ferguson N, Schartau PJ, Sharpe TD, Sato S, Fersht AR. One-state downhill versus conventional protein folding. Journal of Molecular Biology. 344: 295-301. PMID 15522284 DOI: 10.1016/J.Jmb.2004.09.069  0.455
2004 Fersht AR, Sato S. Phi-value analysis and the nature of protein-folding transition states. Proceedings of the National Academy of Sciences of the United States of America. 101: 7976-81. PMID 15150406 DOI: 10.1073/Pnas.0402684101  0.408
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  0.762
2004 Sato S, Religa TL, Daggett V, Fersht AR. Testing protein-folding simulations by experiment: B domain of protein A. Proceedings of the National Academy of Sciences of the United States of America. 101: 6952-6. PMID 15069202 DOI: 10.1073/Pnas.0401396101  0.474
2003 Wang M, Tang Y, Sato S, Vugmeyster L, McKnight CJ, Raleigh DP. Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale. Journal of the American Chemical Society. 125: 6032-3. PMID 12785814 DOI: 10.1021/Ja028752B  0.741
2003 Mayor U, Guydosh NR, Johnson CM, Grossmann JG, Sato S, Jas GS, Freund SM, Alonso DO, Daggett V, Fersht AR. The complete folding pathway of a protein from nanoseconds to microseconds. Nature. 421: 863-7. PMID 12594518 DOI: 10.1038/Nature01428  0.444
2002 Sato S, Raleigh DP. pH-dependent stability and folding kinetics of a protein with an unusual alpha-beta topology: the C-terminal domain of the ribosomal protein L9. Journal of Molecular Biology. 318: 571-82. PMID 12051860 DOI: 10.1016/S0022-2836(02)00015-3  0.682
2001 Sato S, Xiang S, Raleigh DP. On the relationship between protein stability and folding kinetics: a comparative study of the N-terminal domains of RNase HI, E. coli and Bacillus stearothermophilus L9. Journal of Molecular Biology. 312: 569-77. PMID 11563917 DOI: 10.1006/Jmbi.2001.4968  0.707
2001 Camarero JA, Fushman D, Sato S, Giriat I, Cowburn D, Raleigh DP, Muir TW. Rescuing a destabilized protein fold through backbone cyclization. Journal of Molecular Biology. 308: 1045-62. PMID 11352590 DOI: 10.1006/Jmbi.2001.4631  0.689
2000 Sato S, Sayid CJ, Raleigh DP. The failure of simple empirical relationships to predict the viscosity of mixed aqueous solutions of guanidine hydrochloride and glucose has important implications for the study of protein folding. Protein Science : a Publication of the Protein Society. 9: 1601-3. PMID 10975582 DOI: 10.1110/Ps.9.8.1601  0.517
2000 Sato S, Luisi DL, Raleigh DP. pH jump studies of the folding of the multidomain ribosomal protein L9: the structural organization of the N-terminal domain does not affect the anomalously slow folding of the C-terminal domain. Biochemistry. 39: 4955-62. PMID 10769155 DOI: 10.1021/Bi992608U  0.709
1999 Sato S, Kuhlman B, Wu WJ, Raleigh DP. Folding of the multidomain ribosomal protein L9: the two domains fold independently with remarkably different rates. Biochemistry. 38: 5643-50. PMID 10220353 DOI: 10.1021/Bi9830314  0.643
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