| Year |
Citation |
Score |
| 2011 |
Auton M, Rösgen J, Sinev M, Holthauzen LM, Bolen DW. Osmolyte effects on protein stability and solubility: a balancing act between backbone and side-chains. Biophysical Chemistry. 159: 90-9. PMID 21683504 DOI: 10.1016/J.Bpc.2011.05.012 |
0.432 |
|
| 2010 |
Holthauzen LM, Rösgen J, Bolen DW. Hydrogen bonding progressively strengthens upon transfer of the protein urea-denatured state to water and protecting osmolytes. Biochemistry. 49: 1310-8. PMID 20073511 DOI: 10.1021/bi9015499 |
0.319 |
|
| 2010 |
Street TO, Krukenberg KA, Rosgen J, Bolen DW, Agard DA. Osmolyte-induced conformational changes in the Hsp90 molecular chaperone. Protein Science : a Publication of the Protein Society. 19: 57-65. PMID 19890989 DOI: 10.1002/Pro.282 |
0.387 |
|
| 2008 |
Bolen DW, Rose GD. Structure and energetics of the hydrogen-bonded backbone in protein folding. Annual Review of Biochemistry. 77: 339-62. PMID 18518824 DOI: 10.1146/Annurev.Biochem.77.061306.131357 |
0.364 |
|
| 2008 |
Auton M, Bolen DW, Rösgen J. Structural thermodynamics of protein preferential solvation: osmolyte solvation of proteins, aminoacids, and peptides. Proteins. 73: 802-13. PMID 18498104 DOI: 10.1002/Prot.22103 |
0.31 |
|
| 2007 |
Auton M, Holthauzen LM, Bolen DW. Anatomy of energetic changes accompanying urea-induced protein denaturation. Proceedings of the National Academy of Sciences of the United States of America. 104: 15317-22. PMID 17878304 DOI: 10.1073/Pnas.0706251104 |
0.443 |
|
| 2007 |
Auton M, Bolen DW. Application of the transfer model to understand how naturally occurring osmolytes affect protein stability. Methods in Enzymology. 428: 397-418. PMID 17875431 DOI: 10.1016/S0076-6879(07)28023-1 |
0.318 |
|
| 2007 |
Rösgen J, Pettitt BM, Bolen DW. An analysis of the molecular origin of osmolyte-dependent protein stability. Protein Science : a Publication of the Protein Society. 16: 733-43. PMID 17327389 DOI: 10.1110/Ps.062671607 |
0.479 |
|
| 2007 |
Holthauzen LM, Bolen DW. Mixed osmolytes: the degree to which one osmolyte affects the protein stabilizing ability of another. Protein Science : a Publication of the Protein Society. 16: 293-8. PMID 17189473 DOI: 10.1110/Ps.062610407 |
0.554 |
|
| 2007 |
Ferreon AC, Ferreon JC, Bolen DW, Rösgen J. Protein phase diagrams II: nonideal behavior of biochemical reactions in the presence of osmolytes. Biophysical Journal. 92: 245-56. PMID 17028144 DOI: 10.1529/Biophysj.106.092262 |
0.691 |
|
| 2006 |
Street TO, Bolen DW, Rose GD. A molecular mechanism for osmolyte-induced protein stability. Proceedings of the National Academy of Sciences of the United States of America. 103: 13997-4002. PMID 16968772 DOI: 10.1073/Pnas.0606236103 |
0.41 |
|
| 2006 |
Auton M, Ferreon AC, Bolen DW. Metrics that differentiate the origins of osmolyte effects on protein stability: a test of the surface tension proposal. Journal of Molecular Biology. 361: 983-92. PMID 16889793 DOI: 10.1016/J.Jmb.2006.07.003 |
0.71 |
|
| 2006 |
Wu P, Bolen DW. Osmolyte-induced protein folding free energy changes. Proteins. 63: 290-6. PMID 16453342 DOI: 10.1002/prot.20868 |
0.433 |
|
| 2005 |
Auton M, Bolen DW. Predicting the energetics of osmolyte-induced protein folding/unfolding. Proceedings of the National Academy of Sciences of the United States of America. 102: 15065-8. PMID 16214887 DOI: 10.1073/Pnas.0507053102 |
0.328 |
|
| 2005 |
Rajagopalan L, Rösgen J, Bolen DW, Rajarathnam K. Novel use of an osmolyte to dissect multiple thermodynamic linkages in a chemokine ligand-receptor system. Biochemistry. 44: 12932-9. PMID 16185062 DOI: 10.1021/Bi051219Z |
0.308 |
|
| 2005 |
Rösgen J, Pettitt BM, Bolen DW. Protein folding, stability, and solvation structure in osmolyte solutions. Biophysical Journal. 89: 2988-97. PMID 16113118 DOI: 10.1529/Biophysj.105.067330 |
0.444 |
|
| 2004 |
Rösgen J, Pettitt BM, Bolen DW. Uncovering the basis for nonideal behavior of biological molecules. Biochemistry. 43: 14472-84. PMID 15533052 DOI: 10.1021/Bi048681O |
0.337 |
|
| 2004 |
Ferreon AC, Bolen DW. Thermodynamics of denaturant-induced unfolding of a protein that exhibits variable two-state denaturation. Biochemistry. 43: 13357-69. PMID 15491142 DOI: 10.1021/bi048666j |
0.693 |
|
| 2004 |
Bolen DW. Effects of naturally occurring osmolytes on protein stability and solubility: issues important in protein crystallization. Methods (San Diego, Calif.). 34: 312-22. PMID 15325649 DOI: 10.1016/j.ymeth.2004.03.022 |
0.407 |
|
| 2004 |
Rösgen J, Pettitt BM, Perkyns J, Bolen DW. Statistical Thermodynamic Approach to the Chemical Activities in Two-Component Solutions Journal of Physical Chemistry B. 108: 2048-2055. DOI: 10.1021/Jp036325U |
0.306 |
|
| 2003 |
Russo AT, Rösgen J, Bolen DW. Osmolyte effects on kinetics of FKBP12 C22A folding coupled with prolyl isomerization. Journal of Molecular Biology. 330: 851-66. PMID 12850152 DOI: 10.1016/S0022-2836(03)00626-0 |
0.425 |
|
| 2003 |
Qu Y, Bolen DW. Hydrogen exchange kinetics of RNase A and the urea:TMAO paradigm. Biochemistry. 42: 5837-49. PMID 12741842 DOI: 10.1021/bi0206457 |
0.39 |
|
| 2002 |
Qu Y, Bolen DW. Efficacy of macromolecular crowding in forcing proteins to fold. Biophysical Chemistry. 101: 155-65. PMID 12487997 DOI: 10.1016/S0301-4622(02)00148-5 |
0.376 |
|
| 2001 |
Bolen DW, Baskakov IV. The osmophobic effect: natural selection of a thermodynamic force in protein folding. Journal of Molecular Biology. 310: 955-63. PMID 11502004 DOI: 10.1006/Jmbi.2001.4819 |
0.632 |
|
| 2001 |
Bolen DW. Protein stabilization by naturally occurring osmolytes. Methods in Molecular Biology (Clifton, N.J.). 168: 17-36. PMID 11357625 DOI: 10.1385/1-59259-193-0:017 |
0.335 |
|
| 2001 |
Kumar R, Lee JC, Bolen DW, Thompson EB. The conformation of the glucocorticoid receptor af1/tau1 domain induced by osmolyte binds co-regulatory proteins. The Journal of Biological Chemistry. 276: 18146-52. PMID 11279138 DOI: 10.1074/jbc.M100825200 |
0.332 |
|
| 2000 |
Bolen DW, Yang M. Effects of guanidine hydrochloride on the proton inventory of proteins: implications on interpretations of protein stability. Biochemistry. 39: 15208-16. PMID 11106500 DOI: 10.1021/bi001071d |
0.309 |
|
| 2000 |
Yang M, Ferreon AC, Bolen DW. Structural thermodynamics of a random coil protein in guanidine hydrochloride. Proteins. 44-9. PMID 11013399 DOI: 10.1002/1097-0134(2000)41:4+<44::AID-PROT40>3.0.CO;2-7 |
0.731 |
|
| 2000 |
Jamin M, Antalik M, Loh SN, Bolen DW, Baldwin RL. The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry Protein Science. 9: 1340-1346. PMID 10933499 DOI: 10.1110/Ps.9.7.1340 |
0.365 |
|
| 2000 |
Bolen D. Solvent properties, the osmophobic effect, and natural selection in protein folding Comparative Biochemistry and Physiology Part a: Molecular & Integrative Physiology. 126: 16. DOI: 10.1016/S1095-6433(00)80029-X |
0.321 |
|
| 1999 |
Yang M, Liu D, Bolen DW. The peculiar nature of the guanidine hydrochloride-induced two-state denaturation of staphylococcal nuclease: a calorimetric study. Biochemistry. 38: 11216-22. PMID 10460179 DOI: 10.1021/Bi9909400 |
0.418 |
|
| 1999 |
Kumar R, Baskakov IV, Srinivasan G, Bolen DW, Lee JC, Thompson EB. Interdomain signaling in a two-domain fragment of the human glucocorticoid receptor. The Journal of Biological Chemistry. 274: 24737-41. PMID 10455143 DOI: 10.1074/Jbc.274.35.24737 |
0.591 |
|
| 1999 |
Baskakov IV, Bolen DW. The paradox between m values and deltaCp's for denaturation of ribonuclease T1 with disulfide bonds intact and broken. Protein Science : a Publication of the Protein Society. 8: 1314-9. PMID 10386881 DOI: 10.1110/Ps.8.6.1314 |
0.601 |
|
| 1999 |
Baskakov IV, Kumar R, Srinivasan G, Ji YS, Bolen DW, Thompson EB. Trimethylamine N-oxide-induced cooperative folding of an intrinsically unfolded transcription-activating fragment of human glucocorticoid receptor. The Journal of Biological Chemistry. 274: 10693-6. PMID 10196139 DOI: 10.1074/Jbc.274.16.10693 |
0.646 |
|
| 1998 |
Baskakov IV, Bolen DW. Monitoring the sizes of denatured ensembles of staphylococcal nuclease proteins: implications regarding m values, intermediates, and thermodynamics. Biochemistry. 37: 18010-7. PMID 9922169 DOI: 10.1021/Bi981849J |
0.675 |
|
| 1998 |
Qu Y, Bolen CL, Bolen DW. Osmolyte-driven contraction of a random coil protein. Proceedings of the National Academy of Sciences of the United States of America. 95: 9268-73. PMID 9689069 DOI: 10.1073/pnas.95.16.9268 |
0.387 |
|
| 1998 |
Baskakov I, Wang A, Bolen DW. Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: a test of the counteraction hypothesis. Biophysical Journal. 74: 2666-73. PMID 9591690 DOI: 10.1016/S0006-3495(98)77972-X |
0.638 |
|
| 1998 |
Baskakov I, Bolen DW. Time-dependent effects of trimethylamine-N-oxide/urea on lactate dehydrogenase activity: an unexplored dimension of the adaptation paradigm. Biophysical Journal. 74: 2658-65. PMID 9591689 DOI: 10.1016/S0006-3495(98)77971-8 |
0.604 |
|
| 1998 |
Baskakov I, Bolen DW. Forcing thermodynamically unfolded proteins to fold. The Journal of Biological Chemistry. 273: 4831-4. PMID 9478922 DOI: 10.1074/jbc.273.9.4831 |
0.668 |
|
| 1997 |
Wang A, Bolen DW. A naturally occurring protective system in urea-rich cells: mechanism of osmolyte protection of proteins against urea denaturation. Biochemistry. 36: 9101-8. PMID 9230042 DOI: 10.1021/bi970247h |
0.429 |
|
| 1996 |
Wang A, Bolen DW. Effect of proline on lactate dehydrogenase activity: testing the generality and scope of the compatibility paradigm. Biophysical Journal. 71: 2117-22. PMID 8889186 DOI: 10.1016/S0006-3495(96)79410-9 |
0.381 |
|
| 1995 |
Yao M, Bolen DW. How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability. Biochemistry. 34: 3771-81. PMID 7893674 |
0.314 |
|
| 1995 |
Wang A, Robertson AD, Bolen DW. Effects of a naturally occurring compatible osmolyte on the internal dynamics of ribonuclease A. Biochemistry. 34: 15096-104. PMID 7578123 |
0.384 |
|
| 1992 |
Santoro MM, Liu Y, Khan SM, Hou LX, Bolen DW. Increased thermal stability of proteins in the presence of naturally occurring osmolytes. Biochemistry. 31: 5278-83. PMID 1376620 |
0.397 |
|
| 1988 |
Bolen DW, Santoro MM. Unfolding free energy changes determined by the linear extrapolation method. 2. Incorporation of delta G degrees N-U values in a thermodynamic cycle. Biochemistry. 27: 8069-74. PMID 3233196 |
0.305 |
|
| 1971 |
Bolen DW, Flögel M, Biltonen R. Calorimetric studies of protein--inhibitor interaction. I. Binding of 3'-cytidine monophosphate to ribonuclease A at pH 5.5. Biochemistry. 10: 4136-40. PMID 5161033 DOI: 10.1021/bi00798a019 |
0.582 |
|
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