| Year |
Citation |
Score |
| 2007 |
Arakawa T, Kita Y, Timasheff SN. Protein precipitation and denaturation by dimethyl sulfoxide. Biophysical Chemistry. 131: 62-70. PMID 17904724 DOI: 10.1016/J.Bpc.2007.09.004 |
0.445 |
|
| 2007 |
Arakawa T, Ejima D, Tsumoto K, Obeyama N, Tanaka Y, Kita Y, Timasheff SN. Suppression of protein interactions by arginine: a proposed mechanism of the arginine effects. Biophysical Chemistry. 127: 1-8. PMID 17257734 DOI: 10.1016/J.Bpc.2006.12.007 |
0.4 |
|
| 2003 |
Doi H, Kawaguchi M, Timasheff SN. Polymerization and calcium binding of the tubulin-colchicine complex in the GDP state. Bioscience, Biotechnology, and Biochemistry. 67: 1643-52. PMID 12951495 DOI: 10.1271/Bbb.67.1643 |
0.307 |
|
| 2002 |
TIMASHEFF SN, TINOCO I. Light scattering of isoionic conalbumin. Archives of Biochemistry and Biophysics. 66: 427-37. PMID 13403690 DOI: 10.1016/S0003-9861(57)80019-8 |
0.486 |
|
| 2002 |
Timasheff SN. Protein hydration, thermodynamic binding, and preferential hydration. Biochemistry. 41: 13473-82. PMID 12427007 DOI: 10.1021/Bi020316E |
0.385 |
|
| 1997 |
Xie G, Timasheff SN. The thermodynamic mechanism of protein stabilization by trehalose. Biophysical Chemistry. 64: 25-43. PMID 9127936 DOI: 10.1016/S0301-4622(96)02222-3 |
0.402 |
|
| 1997 |
Xie G, Timasheff SN. Temperature dependence of the preferential interactions of ribonuclease A in aqueous co-solvent systems: thermodynamic analysis. Protein Science : a Publication of the Protein Society. 6: 222-32. PMID 9007994 DOI: 10.1002/Pro.5560060124 |
0.357 |
|
| 1997 |
Xie G, Timasheff SN. Mechanism of the stabilization of ribonuclease A by sorbitol: preferential hydration is greater for the denatured then for the native protein. Protein Science : a Publication of the Protein Society. 6: 211-21. PMID 9007993 DOI: 10.1002/Pro.5560060123 |
0.391 |
|
| 1996 |
Lin TY, Timasheff SN. On the role of surface tension in the stabilization of globular proteins. Protein Science : a Publication of the Protein Society. 5: 372-81. PMID 8745416 DOI: 10.1002/Pro.5560050222 |
0.386 |
|
| 1996 |
Perez-Ramirez B, Andreu JM, Gorbunoff MJ, Timasheff SN. Stoichiometric and substoichiometric inhibition of tubulin self-assembly by colchicine analogues. Biochemistry. 35: 3277-85. PMID 8605164 DOI: 10.1021/Bi950523X |
0.338 |
|
| 1995 |
Timasheff SN. Solvent stabilization of protein structure. Methods in Molecular Biology (Clifton, N.J.). 40: 253-69. PMID 7633525 DOI: 10.1385/0-89603-301-5:253 |
0.334 |
|
| 1994 |
Shearwin KE, Timasheff SN. Effect of colchicine analogues on the dissociation of alpha beta tubulin into subunits: the locus of colchicine binding. Biochemistry. 33: 894-901. PMID 8305437 DOI: 10.1021/Bi00170A007 |
0.637 |
|
| 1994 |
Shearwin KE, Perez-Ramirez B, Timasheff SN. Linkages between the dissociation of alpha beta tubulin into subunits and ligand binding: the ground state of tubulin is the GDP conformation. Biochemistry. 33: 885-93. PMID 8305436 |
0.593 |
|
| 1994 |
Perez-Ramirez B, Timasheff SN. Cosolvent modulation of the tubulin-colchicine GTPase-activating conformational change: strength of the enzymatic activity. Biochemistry. 33: 6262-7. PMID 8193141 DOI: 10.1021/Bi00186A028 |
0.332 |
|
| 1994 |
Perez-Ramirez B, Shearwin KE, Timasheff SN. The colchicine-induced GTPase activity of tubulin: state of the product. Activation by microtubule-promoting cosolvents. Biochemistry. 33: 6253-61. PMID 8193140 DOI: 10.1021/Bi00186A027 |
0.64 |
|
| 1994 |
Kita Y, Arakawa T, Lin TY, Timasheff SN. Contribution of the surface free energy perturbation to protein-solvent interactions. Biochemistry. 33: 15178-89. PMID 7999778 DOI: 10.1021/Bi00254A029 |
0.399 |
|
| 1994 |
Lin TY, Timasheff SN. Why do some organisms use a urea-methylamine mixture as osmolyte? Thermodynamic compensation of urea and trimethylamine N-oxide interactions with protein. Biochemistry. 33: 12695-701. PMID 7918496 DOI: 10.1021/Bi00208A021 |
0.374 |
|
| 1994 |
Ward LD, Timasheff SN. Cooperative multiple binding of bisANS and daunomycin to tubulin. Biochemistry. 33: 11891-9. PMID 7918408 DOI: 10.1021/Bi00205A027 |
0.352 |
|
| 1993 |
Timasheff SN. The control of protein stability and association by weak interactions with water: how do solvents affect these processes? Annual Review of Biophysics and Biomolecular Structure. 22: 67-97. PMID 8347999 DOI: 10.1146/Annurev.Bb.22.060193.000435 |
0.358 |
|
| 1992 |
Prakash V, Timasheff SN. Aging of tubulin at neutral pH: stabilization by colchicine and its analogues. Archives of Biochemistry and Biophysics. 295: 146-52. PMID 1575511 DOI: 10.1016/0003-9861(92)90500-V |
0.373 |
|
| 1992 |
Prakash V, Timasheff SN. Aging of tubulin at neutral pH: the destabilizing effect of vinca alkaloids. Archives of Biochemistry and Biophysics. 295: 137-45. PMID 1575510 DOI: 10.1016/0003-9861(92)90499-M |
0.362 |
|
| 1992 |
Shearwin KE, Timasheff SN. Linkage between ligand binding and control of tubulin conformation. Biochemistry. 31: 8080-9. PMID 1510990 DOI: 10.1021/Bi00149A044 |
0.642 |
|
| 1992 |
Timasheff SN. Water as ligand: preferential binding and exclusion of denaturants in protein unfolding. Biochemistry. 31: 9857-64. PMID 1390769 DOI: 10.1021/Bi00156A001 |
0.343 |
|
| 1992 |
Bhat R, Timasheff SN. Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols. Protein Science : a Publication of the Protein Society. 1: 1133-43. PMID 1304392 DOI: 10.1002/Pro.5560010907 |
0.602 |
|
| 1992 |
Timasheff SN. Solvent effects on protein stability. Current Opinion in Structural Biology 1992, 2:35...-39 Current Opinion in Structural Biology. 2: 35-39. DOI: 10.1016/0959-440X(92)90173-5 |
0.378 |
|
| 1991 |
Andreu JM, Gorbunoff MJ, Medrano FJ, Rossi M, Timasheff SN. Mechanism of colchicine binding to tubulin. Tolerance of substituents in ring C' of biphenyl analogues. Biochemistry. 30: 3777-86. PMID 2015233 DOI: 10.1021/Bi00229A027 |
0.317 |
|
| 1991 |
Medrano FJ, Andreu JM, Gorbunoff MJ, Timasheff SN. Roles of ring C oxygens in the binding of colchicine to tubulin. Biochemistry. 30: 3770-7. PMID 2015232 DOI: 10.1021/Bi00229A026 |
0.356 |
|
| 1991 |
Prakash V, Timasheff SN. Mechanism of interaction of vinca alkaloids with tubulin: catharanthine and vindoline. Biochemistry. 30: 873-80. PMID 1988072 DOI: 10.1021/Bi00217A042 |
0.397 |
|
| 1991 |
Timasheff SN, Andreu JM, Na GC. Physical and spectroscopic methods for the evaluation of the interactions of antimitotic agents with tubulin. Pharmacology & Therapeutics. 52: 191-210. PMID 1818336 DOI: 10.1016/0163-7258(91)90008-A |
0.367 |
|
| 1990 |
Arakawa T, Bhat R, Timasheff SN. Why preferential hydration does not always stabilize the native structure of globular proteins. Biochemistry. 29: 1924-31. PMID 2331472 DOI: 10.1021/Bi00459A037 |
0.595 |
|
| 1990 |
Arakawa T, Bhat R, Timasheff SN. Preferential interactions determine protein solubility in three-component solutions: the MgCl2 system. Biochemistry. 29: 1914-23. PMID 2331471 DOI: 10.1021/Bi00459A036 |
0.626 |
|
| 1988 |
Ward LD, Timasheff SN. Energy-transfer studies of the distance between the high-affinity metal binding site and the colchicine and 8-anilino-1-naphthalenesulfonic acid binding sites on calf brain tubulin. Biochemistry. 27: 1508-14. PMID 3365404 DOI: 10.1021/Bi00405A017 |
0.33 |
|
| 1988 |
Timasheff SN, Arakawa T. Mechanism of protein precipitation and stabilization by co-solvents Journal of Crystal Growth. 90: 39-46. DOI: 10.1016/0022-0248(88)90296-5 |
0.426 |
|
| 1987 |
Arakawa T, Timasheff SN. Abnormal solubility behavior of beta-lactoglobulin: salting-in by glycine and NaCl. Biochemistry. 26: 5147-53. PMID 3663650 DOI: 10.1021/Bi00390A038 |
0.368 |
|
| 1987 |
Howard W, Timasheff SN. Quasielastic light scattering studies of tubulin aggregation. Archives of Biochemistry and Biophysics. 255: 446-52. PMID 3592684 DOI: 10.1016/0003-9861(87)90413-9 |
0.346 |
|
| 1987 |
Monasterio O, Timasheff SN. Inhibition of tubulin self-assembly and tubulin-colchicine GTPase activity by guanosine 5'-(gamma-fluorotriphosphate). Biochemistry. 26: 6091-9. PMID 2825770 DOI: 10.1021/Bi00393A022 |
0.642 |
|
| 1986 |
Howard WD, Timasheff SN. GDP state of tubulin: stabilization of double rings. Biochemistry. 25: 8292-300. PMID 3814585 DOI: 10.1021/Bi00373A025 |
0.348 |
|
| 1986 |
Hinz HJ, Timasheff SN. Enthalpy changes in microtubule assembly from pure tubulin. Biochemistry. 25: 8285-91. PMID 3814584 DOI: 10.1021/Bi00373A024 |
0.306 |
|
| 1986 |
Na GC, Timasheff SN. Interaction of vinblastine with calf brain tubulin: effects of magnesium ions. Biochemistry. 25: 6222-8. PMID 3790519 DOI: 10.1021/Bi00368A058 |
0.369 |
|
| 1986 |
Na GC, Timasheff SN. Interaction of vinblastine with calf brain tubulin: multiple equilibria. Biochemistry. 25: 6214-22. PMID 3790518 DOI: 10.1021/Bi00368A057 |
0.389 |
|
| 1986 |
Andreu JM, Timasheff SN. The measurement of cooperative protein self-assembly by turbidity and other techniques. Methods in Enzymology. 130: 47-59. PMID 3773745 DOI: 10.1016/0076-6879(86)30007-7 |
0.356 |
|
| 1986 |
Prakash V, Timasheff SN. Criteria for distinguishing self-associations in velocity sedimentation. Methods in Enzymology. 130: 3-6. PMID 3773737 DOI: 10.1016/0076-6879(86)30003-X |
0.32 |
|
| 1986 |
Andreu JM, Timasheff SN. Tubulin-colchicine interactions and polymerization of the complex. Annals of the New York Academy of Sciences. 466: 676-89. PMID 3460443 DOI: 10.1111/J.1749-6632.1986.Tb38451.X |
0.301 |
|
| 1985 |
Prakash V, Timasheff SN. Calculation of partial specific volumes of proteins in 8 M urea solution. Methods in Enzymology. 117: 53-60. PMID 4079814 DOI: 10.1016/S0076-6879(85)17006-0 |
0.33 |
|
| 1985 |
Na GC, Timasheff SN. Measurement and analysis of ligand-binding isotherms linked to protein self-associations. Methods in Enzymology. 117: 496-519. PMID 4079813 DOI: 10.1016/S0076-6879(85)17027-8 |
0.311 |
|
| 1985 |
Na GC, Timasheff SN. Velocity sedimentation study of ligand-induced protein self-association. Methods in Enzymology. 117: 459-95. PMID 4079812 DOI: 10.1016/S0076-6879(85)17026-6 |
0.304 |
|
| 1985 |
Arakawa T, Timasheff SN. Mechanism of poly(ethylene glycol) interaction with proteins. Biochemistry. 24: 6756-62. PMID 4074726 DOI: 10.1021/Bi00345A005 |
0.386 |
|
| 1985 |
Prakash V, Timasheff SN. Vincristine-induced self-association of calf brain tubulin. Biochemistry. 24: 5004-10. PMID 4074673 DOI: 10.1021/Bi00340A007 |
0.339 |
|
| 1985 |
Arakawa T, Timasheff SN. The stabilization of proteins by osmolytes. Biophysical Journal. 47: 411-4. PMID 3978211 DOI: 10.1016/S0006-3495(85)83932-1 |
0.376 |
|
| 1984 |
Andreu JM, Gorbunoff MJ, Lee JC, Timasheff SN. Interaction of tubulin with bifunctional colchicine analogues: an equilibrium study. Biochemistry. 23: 1742-52. PMID 6722122 DOI: 10.1021/Bi00303A025 |
0.397 |
|
| 1984 |
Gorbunoff MJ, Timasheff SN. The interaction of proteins with hydroxyapatite. III. Mechanism. Analytical Biochemistry. 136: 440-5. PMID 6721144 DOI: 10.1016/0003-2697(84)90241-0 |
0.386 |
|
| 1984 |
Arakawa T, Timasheff SN. Protein stabilization and destabilization by guanidinium salts. Biochemistry. 23: 5924-9. PMID 6525341 DOI: 10.1021/Bi00320A005 |
0.388 |
|
| 1984 |
Arakawa T, Timasheff SN. Mechanism of protein salting in and salting out by divalent cation salts: balance between hydration and salt binding. Biochemistry. 23: 5912-23. PMID 6525340 DOI: 10.1021/Bi00320A004 |
0.377 |
|
| 1984 |
Arakawa T, Timasheff SN. The mechanism of action of Na glutamate, lysine HCl, and piperazine-N,N'-bis(2-ethanesulfonic acid) in the stabilization of tubulin and microtubule formation. The Journal of Biological Chemistry. 259: 4979-86. PMID 6325414 |
0.3 |
|
| 1983 |
Arakawa T, Timasheff SN. Preferential interactions of proteins with solvent components in aqueous amino acid solutions. Archives of Biochemistry and Biophysics. 224: 169-77. PMID 6870251 DOI: 10.1016/0003-9861(83)90201-1 |
0.324 |
|
| 1983 |
Andreu JM, Wagenknecht T, Timasheff SN. Polymerization of the tubulin-colchicine complex: relation to microtubule assembly. Biochemistry. 22: 1556-66. PMID 6849866 DOI: 10.1021/Bi00276A006 |
0.334 |
|
| 1982 |
Prakash V, Timasheff SN. Aging of tubulin at neutral pH. Journal of Molecular Biology. 160: 499-515. PMID 7154071 DOI: 10.1016/0022-2836(82)90310-2 |
0.397 |
|
| 1982 |
Arakawa T, Timasheff SN. Preferential interactions of proteins with salts in concentrated solutions. Biochemistry. 21: 6545-52. PMID 7150575 DOI: 10.1021/Bi00268A034 |
0.397 |
|
| 1982 |
Arakawa T, Timasheff SN. Stabilization of protein structure by sugars. Biochemistry. 21: 6536-44. PMID 7150574 DOI: 10.1021/Bi00268A033 |
0.391 |
|
| 1982 |
Andreu JM, Timasheff SN. Conformational states of tubulin liganded to colchicine, tropolone methyl ether, and podophyllotoxin. Biochemistry. 21: 6465-76. PMID 7150568 DOI: 10.1021/Bi00268A023 |
0.381 |
|
| 1982 |
Na GC, Timasheff SN. Physical properties of purified calf brain tubulin. Methods in Enzymology. 85: 393-408. PMID 7121278 DOI: 10.1016/0076-6879(82)85040-4 |
0.307 |
|
| 1982 |
Andreu JM, Timasheff SN. Interaction of tubulin with single ring analogues of colchicine. Biochemistry. 21: 534-43. PMID 7066305 DOI: 10.1021/Bi00532A019 |
0.363 |
|
| 1982 |
Andreu JM, Timasheff SN. The interactions of tropolone with magnesium ions and tubulin. Biochimica Et Biophysica Acta. 714: 373-7. PMID 7055621 DOI: 10.1016/0304-4165(82)90348-8 |
0.341 |
|
| 1981 |
Na GC, Timasheff SN. Interaction of calf brain tubulin with glycerol. Journal of Molecular Biology. 151: 165-78. PMID 7328652 DOI: 10.1016/0022-2836(81)90226-6 |
0.39 |
|
| 1981 |
Prakash V, Timasheff SN. The calculation of partial specific volumes of proteins in 8 M urea solution. Analytical Biochemistry. 117: 330-5. PMID 7325369 DOI: 10.1016/0003-2697(81)90788-0 |
0.385 |
|
| 1981 |
Prakash V, Loucheux C, Scheufele S, Gorbunoff MJ, Timasheff SN. Interactions of proteins with solvent components in 8 M urea. Archives of Biochemistry and Biophysics. 210: 455-64. PMID 7305338 DOI: 10.1016/0003-9861(81)90209-5 |
0.422 |
|
| 1981 |
Gekko K, Timasheff SN. Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. Biochemistry. 20: 4667-76. PMID 7295639 DOI: 10.1021/Bi00519A023 |
0.401 |
|
| 1981 |
Gekko K, Timasheff SN. Thermodynamic and kinetic examination of protein stabilization by glycerol. Biochemistry. 20: 4677-86. PMID 6271170 DOI: 10.1021/Bi00519A024 |
0.365 |
|
| 1981 |
Andreu JM, Timasheff SN. The ligand- and microtubule assembly-induced GTPase activity of purified calf brain tubulin. Archives of Biochemistry and Biophysics. 211: 151-7. PMID 6118090 DOI: 10.1016/0003-9861(81)90440-9 |
0.349 |
|
| 1980 |
Prakash V, Timasheff SN. Interaction of vincristine with calf brain tubulin. Biochemical Society Transactions. 8: 725. PMID 7461264 DOI: 10.1042/Bst0080725 |
0.387 |
|
| 1980 |
Na GC, Timasheff SN. Thermodynamic linkage between tubulin self-association and the binding of vinblastine. Biochemistry. 19: 1355-65. PMID 7387994 DOI: 10.1021/Bi00548A014 |
0.354 |
|
| 1980 |
Na GC, Timasheff SN. Stoichiometry of the vinblastine-induced self-association of calf brain tubulin. Biochemistry. 19: 1347-54. PMID 7387993 DOI: 10.1021/Bi00548A013 |
0.304 |
|
| 1979 |
Lee JC, Timasheff SN. The calculation of partial specific volumes of proteins in 6 M guanidine hydrochloride. Methods in Enzymology. 61: 49-57. PMID 481235 DOI: 10.1016/0076-6879(79)61006-6 |
0.399 |
|
| 1979 |
Lee JC, Gekko K, Timasheff SN. Measurements of preferential solvent interactions by densimetric techniques. Methods in Enzymology. 61: 26-49. PMID 481227 DOI: 10.1016/0076-6879(79)61005-4 |
0.329 |
|
| 1979 |
Timasheff SN. The in vitro assembly of microtubules from purified brain tubulin Trends in Biochemical Sciences. 4: 61-65. DOI: 10.1016/0968-0004(79)90264-0 |
0.324 |
|
| 1978 |
Lee JC, Tweedy N, Timasheff SN. In vitro reconstitution of calf brain microtubules: effects of macromolecules. Biochemistry. 17: 2783-90. PMID 758003 DOI: 10.1021/Bi00607A013 |
0.368 |
|
| 1978 |
Gorbunoff MJ, Fosmire G, Timasheff SN. Low pH dimerization of chymotrypsin in solution. Biochemistry. 17: 4055-65. PMID 30471 DOI: 10.1021/Bi00612A029 |
0.32 |
|
| 1978 |
Pittz EP, Timasheff SN. Interaction of ribonuclease A with aqueous 2-methyl-2,4-pentanediol at pH 5.8. Biochemistry. 17: 615-23. PMID 23825 DOI: 10.1021/Bi00597A009 |
0.375 |
|
| 1978 |
Lee JC, Corfman D, Frigon RP, Timasheff SN. Conformational study of calf brain tubulin. Archives of Biochemistry and Biophysics. 185: 4-14. PMID 23729 DOI: 10.1016/0003-9861(78)90137-6 |
0.304 |
|
| 1977 |
Na C, Timasheff SN. Physical-chemical study of daunomycin-tubulin interactions. Archives of Biochemistry and Biophysics. 182: 147-54. PMID 883828 DOI: 10.1016/0003-9861(77)90293-4 |
0.37 |
|
| 1977 |
Lee JC, Timasheff SN. In vitro reconstitution of calf brain microtubules: effects of solution variables. Biochemistry. 16: 1754-64. PMID 856260 DOI: 10.1021/Bi00627A037 |
0.361 |
|
| 1975 |
Frigon RP, Timasheff SN. Magnesium-induced self-association of calf brain tubulin. II. Thermodynamics Biochemistry. 14: 4567-4573. PMID 1182104 DOI: 10.1021/Bi00692A002 |
0.355 |
|
| 1975 |
Lee JC, Frigon RP, Timasheff SN. Structural stability of calf brain microtubule protein Annals of the New York Academy of Sciences. 284-291. PMID 1056747 DOI: 10.1111/J.1749-6632.1975.Tb19207.X |
0.315 |
|
| 1975 |
Lee JC, Timasheff SN. The reconstitution of microtubules from purified calf brain tubulin Biochemistry. 14: 5183-5187. PMID 811253 DOI: 10.1021/Bi00694A025 |
0.308 |
|
| 1974 |
Lee JC, Timasheff SN. Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride Biochemistry. 13: 257-265. PMID 4855654 DOI: 10.1021/Bi00699A005 |
0.394 |
|
| 1974 |
Lee JC, Timasheff SN. The calculation of partial specific volumes of proteins in guanidine hydrochloride Archives of Biochemistry and Biophysics. 165: 268-273. PMID 4613272 DOI: 10.1016/0003-9861(74)90164-7 |
0.374 |
|
| 1974 |
Frigon RP, Valenzuela MS, Timasheff SN. Structure of a magnesium-induced polymer of calf brain microtubule protein Archives of Biochemistry and Biophysics. 165: 442-443. PMID 4441083 DOI: 10.1016/0003-9861(74)90183-0 |
0.302 |
|
| 1973 |
Pessen H, Kumosinski TF, Timasheff SN. [9] Small-angle X-ray scattering Methods in Enzymology. 27: 151-209. DOI: 10.1016/S0076-6879(73)27011-8 |
0.363 |
|
| 1971 |
Pessen H, Kumosinski TF, Timasheff SN. The use of small-angle X-ray scattering to determine protein conformation Journal of Agriculatural and Food Chemistry. 19: 698-702. PMID 5163851 DOI: 10.1021/Jf60176A014 |
0.313 |
|
| 1970 |
Weisenberg RC, Timasheff SN. Aggregation of microtubule subunit protein. Effects of divalent cations, colchicine and vinblastine. Biochemistry. 9: 4110-6. PMID 5458644 DOI: 10.1021/Bi00823A012 |
0.364 |
|
| 1968 |
Timasheff SN, Inoue H. Preferential binding of solvent components to proteins in mixed water-organic solvent systems Biochemistry. 7: 2501-2513. DOI: 10.1021/Bi00847A009 |
0.331 |
|
| 1960 |
Timasheff SN, Coleman BD. On light-scattering studies of isoionic proteins Archives of Biochemistry and Biophysics. 87: 63-69. PMID 13838420 |
0.538 |
|
| 1960 |
Townend R, Timasheff SN. Molecular interactions in β-lactoglobulin. III. Light scattering investigation of the stoichiometry of the association between pH 3.7 and 5.2 Journal of the American Chemical Society. 82: 3168-3174. DOI: 10.1021/Ja01497A046 |
0.325 |
|
| 1957 |
Timasheff SN, Dintzis HM, Kirkwood JG, Coleman BD. Light Scattering Investigation of Charge Fluctuations in Isoionic Serum Albumin Solutions1 Journal of the American Chemical Society. 79: 782-791. DOI: 10.1021/Ja01561A003 |
0.642 |
|
| 1956 |
Timasheff SN, Moyer AW, Brown RA, Kirkwood JG. THE DISTRIBUTION OF POLIO ANTIBODIES IN SERUM PROTEINS. Proceedings of the National Academy of Sciences of the United States of America. 42: 228-34. PMID 16589854 DOI: 10.1073/Pnas.42.5.228 |
0.47 |
|
| 1956 |
KIRKWOOD JG, TIMASHEFF SN. The effect of ionization on the light scattering of isoionic proteins. Archives of Biochemistry and Biophysics. 65: 50-7. PMID 13373406 DOI: 10.1016/0003-9861(56)90175-8 |
0.537 |
|
| 1955 |
Timasheff SN, Dintzis HM, Kirkwood JG, Coleman BD. STUDIES OF MOLECULAR INTERACTION IN ISOIONIC PROTEIN SOLUTIONS BY LIGHT-SCATTERING. Proceedings of the National Academy of Sciences of the United States of America. 41: 710-4. PMID 16589733 DOI: 10.1073/Pnas.41.10.710 |
0.754 |
|
| 1953 |
TIMASHEFF SN, SHUMAKER JB, KIRKWOOD JG. Semicontinuous electrophoresis-convection. Archives of Biochemistry and Biophysics. 47: 455-64. PMID 13114915 DOI: 10.1016/0003-9861(53)90482-2 |
0.467 |
|
| 1953 |
Timasheff SN, Kirkwood JG. Electrophoresis—Convection Applied to the Complexed Insulin—Protamine System1 Journal of the American Chemical Society. 75: 3124-3126. DOI: 10.1021/Ja01109A024 |
0.429 |
|
| 1953 |
Timasheff SN, Brown RA, Kirkwood JG. The Fractionation of Insulin by Electrophoresis—Convection1 Journal of the American Chemical Society. 75: 3121-3124. DOI: 10.1021/Ja01109A023 |
0.416 |
|
| 1952 |
GIBBS RJ, TIMASHEFF SN, NORD FF. Investigations on proteins and polymers. IX. Denaturation studies of egg albumin with aliphatic amines. Archives of Biochemistry and Biophysics. 40: 85-101. PMID 12997192 DOI: 10.1016/0003-9861(52)90076-3 |
0.609 |
|
| 1952 |
Singer SJ, Timasheff SN, Kirkwood JG. Electrophoresis-convection Applied to Substances Forming Soluble Complexes1 Journal of the American Chemical Society. 74: 5985-5988. DOI: 10.1021/ja01143a049 |
0.453 |
|
| 1952 |
Brown RA, Shumaker JB, Timasheff SN, Kirkwood JG. Experimental Investigation of Fractionation in the Electrophoresis—Convection Apparatus Journal of the American Chemical Society. 74: 460-462. DOI: 10.1021/ja01122a054 |
0.434 |
|
| 1951 |
TIMASHEFF SN, NORD FF. Investigations on proteins and polymers. VI. Interaction of egg albumin with a thiophene-2-azlactone. Archives of Biochemistry and Biophysics. 31: 320-5. PMID 14830241 |
0.509 |
|
| 1951 |
TIMASHEFF SN, NORD FF. Investigations on proteins and polymers. V. Interaction of egg albumin with dodecylamine hydrochloride. Archives of Biochemistry and Biophysics. 31: 309-19. PMID 14830240 DOI: 10.1016/0003-9861(51)90220-2 |
0.582 |
|
| 1949 |
Timasheff SN, Bier M, Nord FF. Aggregation Phenomena in Polyvinyl Alcohol-Acetate Solutions. Proceedings of the National Academy of Sciences of the United States of America. 35: 364-8. PMID 16588906 |
0.433 |
|
| 1949 |
Timasheff SN, Bier M, Nord FF. Communication to the Editor: The Quadratic Term in the Light-Scattering Equation. The Journal of Physical and Colloid Chemistry. 53: 1134-1136. DOI: 10.1021/j150472a014 |
0.439 |
|
| Show low-probability matches. |
