| Year |
Citation |
Score |
| 1996 |
Xie Y, Wetlaufer DB. Control of aggregation in protein refolding: the temperature-leap tactic. Protein Science : a Publication of the Protein Society. 5: 517-23. PMID 8868489 DOI: 10.1002/pro.5560050314 |
0.3 |
|
| 1995 |
Wetlaufer DB, Xie Y. Control of aggregation in protein refolding: a variety of surfactants promote renaturation of carbonic anhydrase II. Protein Science : a Publication of the Protein Society. 4: 1535-43. PMID 8520479 DOI: 10.1002/pro.5560040811 |
0.335 |
|
| 1991 |
Buckley JJ, Wetlaufer DB. Use of the surfactant 3-(3-cholamidopropyl)-dimethyl-ammoniapropane sulfonate in hydrophobic interaction chromatography of proteins Journal of Chromatography A. 464: 61-71. DOI: 10.1016/S0021-9673(00)94223-7 |
0.367 |
|
| 1990 |
Wetlaufer DB. Nucleation in protein folding--confusion of structure and process. Trends in Biochemical Sciences. 15: 414-5. PMID 2278098 DOI: 10.1016/0968-0004(90)90275-g |
0.287 |
|
| 1990 |
Buckley JJ, Wetlaufer DB. Surfactant-mediated hydrophobic interaction chromatography of proteins: gradient elution Journal of Chromatography A. 518: 99-110. PMID 2258414 DOI: 10.1016/S0021-9673(01)93165-6 |
0.313 |
|
| 1990 |
Wetlaufer DB. Experimental approaches to protein folding. Biotechnology (Reading, Mass.). 14: 21-35. PMID 2183898 DOI: 10.1016/b978-0-409-90116-0.50010-8 |
0.348 |
|
| 1990 |
Gehas J, Wetlaufer DB. Isocratic hydrophobi interaction chromatography of dansyl amino acids Journal of Chromatography A. 511: 123-130. DOI: 10.1016/S0021-9673(01)93277-7 |
0.263 |
|
| 1990 |
Wetlaufer DB. A biochemistry textbook for assorted undergraduates Trends in Biochemical Sciences. 15: 337. DOI: 10.1016/0968-0004(90)90069-N |
0.175 |
|
| 1989 |
Buckley JJ, Wetlaufer DB. Use of the surfactant 3-(3-cholamidopropyl)-dimethyl-ammoniopropane sulfonate in hydrophobic interaction chromatography of proteins Journal of Chromatography. 464: 61-71. PMID 2715250 |
0.329 |
|
| 1989 |
Gehas J, Wetlaufer D. Hydrophobic interaction chromatography of small molecules: characterization of the retention of acyl coenzyme a homologues Journal of Chromatography A. 477: 249-258. DOI: 10.1016/S0021-9673(01)89634-5 |
0.243 |
|
| 1988 |
Wetlaufer D. Reversible and irreversible denaturation of proteins in chromatographic systems Makromolekulare Chemie. Macromolecular Symposia. 17: 17-28. DOI: 10.1002/MASY.19880170104 |
0.344 |
|
| 1987 |
Wetlaufer DB, Branca PA, Chen GX. The oxidative folding of proteins by disulfide plus thiol does not correlate with redox potential. Protein Engineering. 1: 141-6. PMID 3507696 DOI: 10.1093/protein/1.2.141 |
0.297 |
|
| 1986 |
Wetlaufer DB. Protein structure. Science (New York, N.Y.). 233: 1027. PMID 17746568 DOI: 10.1126/science.233.4768.1027-c |
0.375 |
|
| 1986 |
Wetlaufer DB, Koenigbauer MR. Surfactant-mediated protein hydrophobic-interaction chromatography. Journal of Chromatography. 359: 55-60. PMID 3733942 DOI: 10.1016/0021-9673(86)80061-9 |
0.357 |
|
| 1986 |
Parente ES, Wetlaufer DB. Relationship between isocratic and gradient retention times in the high-performance ion-exchange chromatography of proteins. Theory and experiment. Journal of Chromatography. 355: 29-40. PMID 3700543 DOI: 10.1016/s0021-9673(01)97301-7 |
0.331 |
|
| 1985 |
Haeffner-Gormley L, Parente L, Wetlaufer DB. Use of proline-specific endopeptidase in the isolation of all four "native" disulfides of hen egg white lysozyme. International Journal of Peptide and Protein Research. 26: 83-91. PMID 3902690 DOI: 10.1111/j.1399-3011.1985.tb03181.x |
0.27 |
|
| 1985 |
Wetlaufer DB. Prolyl isomerization: How significant forin vivo protein folding? Biopolymers. 24: 251-255. DOI: 10.1002/BIP.360240119 |
0.393 |
|
| 1984 |
Parente ES, Wetlaufer DB. Influence of urea on the high-performance cation-exchange chromatography of hen egg white lysozyme. Journal of Chromatography. 288: 389-98. PMID 6736147 DOI: 10.1016/s0021-9673(01)93715-x |
0.284 |
|
| 1984 |
Parente ES, Wetlaufer DB. Effects of urea-thermal denaturation on the high-performance cation-exchange chromatography of alpha-chymotrypsinogen-A. Journal of Chromatography. 314: 337-47. PMID 6526886 DOI: 10.1016/s0021-9673(01)97747-7 |
0.369 |
|
| 1984 |
Wetlaufer DB. Nonenzymatic formation and isomerization of protein disulfides. Methods in Enzymology. 107: 301-4. PMID 6503715 DOI: 10.1016/0076-6879(84)07020-8 |
0.392 |
|
| 1984 |
Brantley RK, Haeffner-Gormley L, Wetlaufer DB. Preparation of a positively charged maleimide and its application to the high-performance liquid chromatographic separation of the tryptic peptides of lysozyme. Journal of Chromatography. 295: 220-5. PMID 6470085 DOI: 10.1016/s0021-9673(01)87615-9 |
0.228 |
|
| 1983 |
Perraudin JP, Torchia TE, Wetlaufer DB. Multiple parameter kinetic studies of the oxidative folding of reduced lysozyme. The Journal of Biological Chemistry. 258: 11834-9. PMID 6619147 |
0.301 |
|
| 1981 |
Wetlaufer DB. Folding of protein fragments. Advances in Protein Chemistry. 34: 61-92. PMID 6266231 DOI: 10.1016/s0065-3233(08)60518-5 |
0.397 |
|
| 1981 |
Johanson KO, Wetlaufer DB, Reed RG, Peters T. Refolding of bovine serum albumin and its proteolytic fragments. Regain of disulfide bonds, secondary structure, and ligand-binding ability. The Journal of Biological Chemistry. 256: 445-50. PMID 6161123 |
0.236 |
|
| 1981 |
Haeffner-Gormley L, Poludniak N, Wetlaufer D. Separation of the tryptic peptides from reduced, alkylated hen egg white lysozyme by high-performance liquid chromatography Journal of Chromatography A. 214: 185-196. DOI: 10.1016/S0021-9673(00)98523-6 |
0.241 |
|
| 1978 |
Johnson ER, Anderson WL, Wetlaufer DB. Formation of three-dimensional structure in protein fragments. Reoxidation of reduced hen egg lysozyme fragment 13-105 Journal of Biological Chemistry. 253: 3408-3414. PMID 565770 |
0.355 |
|
| 1977 |
Rose GD, Wetlaufer DB. The number of turns in globular proteins Nature. 268: 769-770. PMID 895883 DOI: 10.1038/268769A0 |
0.347 |
|
| 1977 |
Wetlaufer DB, Saxena VP, Ahmed AK, Schaffer SW, Pick PW, Oh KJ, Peterson JD. Protein thiol-disulfide interchange and interfacing with biological systems Advances in Experimental Medicine and Biology. 86: 43-50. PMID 335840 DOI: 10.1007/978-1-4684-3282-4_3 |
0.329 |
|
| 1977 |
Wetlaufer DB. Thermodynamics of the Polymerization of Protein. Fumio Oosawa , Sho Asakura The Quarterly Review of Biology. 52: 398-398. DOI: 10.1086/410149 |
0.39 |
|
| 1976 |
Johnson ER, Oh KJ, Wetlaufer DB. Formation of three-dimensional structure in protein fragments. Reactivation of reduced hen egg lysozyme fragment 1-127. The Journal of Biological Chemistry. 251: 3154-7. PMID 1270441 |
0.342 |
|
| 1976 |
Anderson WL, Wetlaufer DB. The folding pathway of reduced lysozyme Journal of Biological Chemistry. 251: 3147-3153. PMID 1270440 |
0.292 |
|
| 1976 |
Rose GD, Winters RH, Wetlaufer DB. A testable model for protein folding. Febs Letters. 63: 10-16. PMID 1261670 DOI: 10.1016/0014-5793(76)80184-6 |
0.362 |
|
| 1976 |
Wetlaufer DB, Rose GD, Taaffe L. Orientation of structural segments in globular proteins. Biochemistry. 15: 5154-5157. PMID 990271 DOI: 10.1021/Bi00668A031 |
0.307 |
|
| 1975 |
Ahmed AK, Schaffer SW, Wetlaufer DB. Nonenzymic reactivation of reduced bovine pancreatic ribonuclease by air oxidation and by glutathione oxidoreduction buffers. The Journal of Biological Chemistry. 250: 8477-82. PMID 1194263 |
0.245 |
|
| 1975 |
Goldberg D, Saliterman S, Wetlaufer DB, Rose G, Hopkins TE. Minimization of construction errors in bent-wire protein models. Biopolymers. 14: 633-640. PMID 1174683 DOI: 10.1002/Bip.1975.360140315 |
0.211 |
|
| 1975 |
Anderson WL, Wetlaufer DB. A new method for disulfide analysis of peptides Analytical Biochemistry. 67: 493-502. PMID 1172386 DOI: 10.1016/0003-2697(75)90323-1 |
0.27 |
|
| 1975 |
Schaffer SW, Ahmed AK, Wetlaufer DB. Salt effects in the glutathione-facilitated reactivation of reduced bovine pancreatic ribonuclease. The Journal of Biological Chemistry. 250: 8483-6. PMID 1104605 |
0.287 |
|
| 1974 |
Wetlaufer D, Kwok E, Anderson WL, Johnson ER. Kinetic determinism of lysozyme folding at high temperatures Biochemical and Biophysical Research Communications. 56: 380-385. PMID 4823872 DOI: 10.1016/0006-291X(74)90853-5 |
0.308 |
|
| 1974 |
Hsiao CY, Ottaway CA, Wetlaufer DB. Preparation of fully deuterated fatty acids by simple method. Lipids. 9: 913-5. PMID 4437321 DOI: 10.1007/BF02532618 |
0.221 |
|
| 1973 |
Moore WV, Wetlaufer DB. Circular dichroism of nerve membrane fractions: effects of temperature, pH and electrolytes. Journal of Neurochemistry. 20: 135-49. PMID 4687197 DOI: 10.1111/j.1471-4159.1973.tb12111.x |
0.21 |
|
| 1973 |
Wetlaufer DB, Ristow S. Acquisition of three-dimensional structure of proteins. Annual Review of Biochemistry. 42: 135-58. PMID 4581224 DOI: 10.1146/annurev.bi.42.070173.001031 |
0.356 |
|
| 1973 |
Ristow SS, Wetlaufer DB. Evidence for nucleation in the folding of reduced hen egg lysozyme. Biochemical and Biophysical Research Communications. 50: 544-50. PMID 4569880 DOI: 10.1016/0006-291x(73)90874-7 |
0.249 |
|
| 1973 |
Wetlaufer DB. Nucleation, rapid folding, and globular intrachain regions in proteins. Proceedings of the National Academy of Sciences of the United States of America. 70: 697-701. PMID 4351801 DOI: 10.1073/pnas.70.3.697 |
0.325 |
|
| 1973 |
WETLAUFER DB. Protein Structure and Stability: Conventional Wisdom and New Perspectives Journal of Food Science. 38: 740-743. DOI: 10.1111/J.1365-2621.1973.TB02068.X |
0.338 |
|
| 1971 |
Saxena VP, Wetlaufer DB. A new basis for interpreting the circular dichroic spectra of proteins. Proceedings of the National Academy of Sciences of the United States of America. 68: 969-72. PMID 5280530 DOI: 10.1073/pnas.68.5.969 |
0.305 |
|
| 1971 |
Bjorksten J, Acharya PV, Ashman S, Wetlaufer DB. Gerogenic fractions in the tritiated rat. Journal of the American Geriatrics Society. 19: 561-74. PMID 5106728 DOI: 10.1111/j.1532-5415.1971.tb02577.x |
0.179 |
|
| 1971 |
Moore WV, Wetlaufer DB. The circular dichroism of synaptosomal membranes: studies of interactions with neuropharmacological agents. Journal of Neurochemistry. 18: 1167-78. PMID 4330287 DOI: 10.1111/j.1471-4159.1971.tb00215.x |
0.201 |
|
| 1970 |
Ottaway CA, Wetlaufer DB. Light-scattering contributions to the circular dichroism of particulate systems. Archives of Biochemistry and Biophysics. 139: 257-64. PMID 5501625 DOI: 10.1016/0003-9861(70)90476-5 |
0.187 |
|
| 1970 |
Dearborn DG, Wetlaufer DB. Circular dichroism of putative unordered polypeptides and proteins. Biochemical and Biophysical Research Communications. 39: 314-20. PMID 5421933 DOI: 10.1016/0006-291x(70)90578-4 |
0.401 |
|
| 1970 |
Saxena VP, Wetlaufer DB. Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme. Biochemistry. 9: 5015-23. PMID 4991411 DOI: 10.1021/bi00827a028 |
0.367 |
|
| 1969 |
Dearborn DG, Wetlaufer DB. Reversible thermal conformation changes in human serum low-density lipoprotein. Proceedings of the National Academy of Sciences of the United States of America. 62: 179-85. PMID 5253655 DOI: 10.1073/pnas.62.1.179 |
0.297 |
|
| 1966 |
Balasubramanian D, Wetlaufer DB. Reversible alteration of the structure of globular proteins by anesthetic agents. Proceedings of the National Academy of Sciences of the United States of America. 55: 762-5. PMID 5219683 |
0.337 |
|
| 1966 |
Balasubramanian D, Wetlaufer DB. Optical Rotatory Properties of Diketopiperazines Journal of the American Chemical Society. 88: 3449-3450. DOI: 10.1021/JA00966A059 |
0.166 |
|
| 1964 |
WETLAUFER DB, LOVRIEN R. INDUCTION OF REVERSIBLE STRUCTURAL CHANGES IN PROTEINS BY NONPOLAR SUBSTANCES. The Journal of Biological Chemistry. 239: 596-603. PMID 14169166 |
0.356 |
|
| 1964 |
Coffin RL, Stoller L, Wetlaufer DB. A Versatile Solubility Apparatus. Analytical Chemistry. 36: 699-699. DOI: 10.1021/AC60209A081 |
0.255 |
|
| 1961 |
WETLAUFER DB. Terminology of protein structure. Nature. 190: 1113. PMID 13784651 DOI: 10.1038/1901113a0 |
0.374 |
|
| 1961 |
WETLAUFER DB. Osmometry and general characterization of alpha-lactalbumin. Comptes-Rendus Des Travaux Du Laboratoire Carlsberg. 32: 125-38. PMID 13784650 |
0.181 |
|
| 1961 |
Simmons NS, Cohen C, Szent-Gyorgyi AG, Wetlaufer DB, Blout ER. A Conformation-dependent Cotton Effect in α-Helical Polypeptides and Proteins1,2 Journal of the American Chemical Society. 83: 4766-4769. DOI: 10.1021/JA01484A017 |
0.482 |
|
| 1960 |
WETLAUFER DB, EDSALL JT. Sedimentation of myosin in urea solutions. Biochimica Et Biophysica Acta. 43: 132-4. PMID 13784649 DOI: 10.1016/0006-3002(60)90417-0 |
0.568 |
|
| 1958 |
MARTIN RB, EDSALL JT, WETLAUFER DB, HOLLINGWORTH BR. A complete ionization scheme for tyrosine, and the ionization constants of some tyrosine derivatives. The Journal of Biological Chemistry. 233: 1429-35. PMID 13610853 |
0.561 |
|
| 1958 |
WETLAUFER DB, EDSALL JT, HOLLINGWORTH BR. Ultraviolet difference spectra of tyrosine groups in proteins and amino acids. The Journal of Biological Chemistry. 233: 1421-8. PMID 13610852 |
0.611 |
|
| 1958 |
Wetlaufer DB, Stahmann MA. Solubility and mechanism of dye-uptake in protein-dye salts Journal of the American Chemical Society. 80: 1493-1500. DOI: 10.1021/Ja01539A054 |
0.571 |
|
| 1957 |
WETLAUFER DB. A Simple Device for forming Solution Concentration-gradients Nature. 180: 1122-1123. DOI: 10.1038/1801122A0 |
0.239 |
|
| 1956 |
WETLAUFER DB. The strength of tyrosyl-carboxylate hydrogen bonds. Comptes Rendus Des Travaux Du Laboratoire Carlsberg. Serie Chimique. 30: 135-46. PMID 13437608 |
0.187 |
|
| 1953 |
WETLAUFER DB, STAHMANN MA. The interaction of methyl orange anions with lysine polypeptides. The Journal of Biological Chemistry. 203: 117-26. PMID 13069494 |
0.504 |
|
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