| Year |
Citation |
Score |
| 2002 |
Kalnine NN, Schachman HK. Quantitative urea gradient gel electrophoresis for studies of dissociation and unfolding of oligomeric proteins Biophysical Chemistry. 101: 133-144. PMID 12487995 DOI: 10.1016/S0301-4622(02)00154-0 |
0.318 |
|
| 2001 |
Ni X, Schachman HK. In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains Protein Science. 10: 519-527. PMID 11344320 DOI: 10.1110/Ps.38901 |
0.311 |
|
| 2000 |
Schachman HK. Still looking for the ivory tower Annual Review of Biochemistry. 69: 1-29. PMID 10966451 DOI: 10.1146/Annurev.Biochem.69.1.1 |
0.33 |
|
| 1996 |
Murata LB, Schachman HK. Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: Characterization of the active site and evidence for an interdomain carboxy-terminal helix in ornithine transcarbamoylase Protein Science. 5: 709-718. PMID 8845761 DOI: 10.1002/Pro.5560050416 |
0.302 |
|
| 1996 |
Yang YR, Schachman HK. A bifunctional fusion protein containing the maltose-binding polypeptide and the catalytic chain of aspartate transcarbamoylase: Assembly, oligomers, and domains Biophysical Chemistry. 59: 289-297. PMID 8672717 DOI: 10.1016/0301-4622(96)00018-X |
0.306 |
|
| 1993 |
Zhou BB, Schachman HK. Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase Protein Science. 2: 103-112. PMID 8443583 DOI: 10.1002/Pro.5560020111 |
0.303 |
|
| 1993 |
Yang YR, Schachman HK. In vivo formation of active aspartate transcarbamoylase from complementing fragments of the catalytic polypeptide chains Protein Science. 2: 1013-1023. PMID 8318886 DOI: 10.1002/Pro.5560020614 |
0.308 |
|
| 1993 |
Powers VM, Yang YR, Fogli MJ, Schachman HK. Reconstitution of active catalytic trimer of aspartate transcarbamoylase from proteolytically cleaved polypeptide chains Protein Science. 2: 1001-1012. PMID 8318885 DOI: 10.1002/Pro.5560020613 |
0.325 |
|
| 1993 |
Yang YR, Schachman HK. Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains Proceedings of the National Academy of Sciences of the United States of America. 90: 11980-11984. PMID 8265657 DOI: 10.1073/Pnas.90.24.11980 |
0.303 |
|
| 1993 |
Anfinsen CB, Bessman MJ, Schachman HK, Schellman JA, Von Hippel PH, Young M. Remembering Bill Harrington Trends in Biochemical Sciences. 18: 364-365. DOI: 10.1016/0968-0004(93)90089-6 |
0.53 |
|
| 1993 |
Schachman HK. Asparate transcarbamoylase. Current opinion in structural biology 1993, 3:960-967 Current Opinion in Structural Biology. 3: 960-967. DOI: 10.1016/0959-440X(93)90162-E |
0.311 |
|
| 1992 |
Waldrop GL, Turnbull JL, Parmentier LE, Lee S, O'Leary MH, Cleland WW, Schachman HK. The contribution of threonine 55 to catalysis in aspartate transcarbamoylase. Biochemistry. 31: 6592-7. PMID 1633171 DOI: 10.1021/Bi00143A032 |
0.327 |
|
| 1992 |
Waldrop GL, Turnbull JL, Parmentier LE, O'Leary MH, Cleland WW, Schachman HK. Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine. Biochemistry. 31: 6585-91. PMID 1633170 DOI: 10.1021/Bi00143A031 |
0.319 |
|
| 1992 |
Parmentier LE, O'Leary MH, Schachman HK, Cleland WW. 13C isotope effects as a probe of the kinetic mechanism and allosteric properties of Escherichia coli aspartate transcarbamylase. Biochemistry. 31: 6570-6. PMID 1633168 DOI: 10.1021/Bi00143A029 |
0.31 |
|
| 1992 |
Peterson CB, Burman DL, Schachman HK. Effects of replacement of active site residue glutamine 231 on activity and allosteric properties of aspartate transcarbamoylase. Biochemistry. 31: 8508-15. PMID 1390636 DOI: 10.1021/Bi00151A018 |
0.322 |
|
| 1991 |
Markby DW, Zhou BB, Schachman HK. A 70-amino acid zinc-binding polypeptide from the regulatory chain of aspartate transcarbamoylase forms a stable complex with the catalytic subunit leading to markedly altered enzyme activity Proceedings of the National Academy of Sciences of the United States of America. 88: 10568-10572. PMID 1961722 DOI: 10.1073/Pnas.88.23.10568 |
0.337 |
|
| 1991 |
Peterson CB, Schachman HK. Role of a carboxyl-terminal helix in the assembly, interchain interactions, and stability of aspartate transcarbamoylase Proceedings of the National Academy of Sciences of the United States of America. 88: 458-462. PMID 1899140 DOI: 10.1073/Pnas.88.2.458 |
0.316 |
|
| 1990 |
Newell JO, Schachman HK. Amino acid substitutions which stabilize aspartate transcarbamoylase in the R state disrupt both homotropic and heterotropic effects Biophysical Chemistry. 37: 183-196. PMID 2285780 DOI: 10.1016/0301-4622(90)88018-N |
0.328 |
|
| 1990 |
Eisenstein E, Markby DW, Schachman HK. Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase Biochemistry. 29: 3724-3731. PMID 2187530 DOI: 10.1021/Bi00467A019 |
0.337 |
|
| 1989 |
Werner WE, Cann JR, Schachman HK. Boundary spreading in sedimentation velocity experiments on partially liganded aspartate transcarbamoylase. A ligand-mediated isomerization. Journal of Molecular Biology. 206: 231-7. PMID 2649685 DOI: 10.1016/0022-2836(89)90536-6 |
0.329 |
|
| 1989 |
Werner WE, Schachman HK. Analysis of the ligand-promoted global conformational change in aspartate transcarbamoylase. Evidence for a two-state transition from boundary spreading in sedimentation velocity experiments Journal of Molecular Biology. 206: 221-230. PMID 2649684 DOI: 10.1016/0022-2836(89)90535-4 |
0.323 |
|
| 1988 |
Kleanthous C, Wemmer DE, Schachman HK. The role of an active site histidine in the catalytic mechanism of aspartate transcarbamoylase Journal of Biological Chemistry. 263: 13062-13067. PMID 3047117 DOI: 10.13018/Bmr2229 |
0.305 |
|
| 1988 |
Lu T, Young T, Schachman H, Kim S. Preliminary Results on the Crystal and Molecular Structure of Native and Mutant Aspartate Carbamoyltransferase at Neutral pH Journal of the Chinese Chemical Society. 35: 315-319. DOI: 10.1002/Jccs.198800047 |
0.309 |
|
| 1987 |
Yang YR, Schachman HK. Hybridization as a technique for studying interchain interactions in the catalytic trimers of aspartate transcarbamoylase Analytical Biochemistry. 163: 188-195. PMID 3039866 DOI: 10.1016/0003-2697(87)90111-4 |
0.32 |
|
| 1986 |
Robey EA, Wente SR, Markby DW, Flint A, Yang YR, Schachman HK. Effect of amino acid substitutions on the catalytic and regulatory properties of aspartate transcarbamoylase. Proceedings of the National Academy of Sciences of the United States of America. 83: 5934-8. PMID 3526345 DOI: 10.1073/Pnas.83.16.5934 |
0.32 |
|
| 1985 |
Foote J, Schachman HK. Homotropic effects in aspartate transcarbamoylase. What happens when the enzyme binds a single molecule of the bisubstrate analog N-phosphonacetyl-l-aspartate? Journal of Molecular Biology. 186: 175-184. PMID 3908690 DOI: 10.1016/0022-2836(85)90267-0 |
0.305 |
|
| 1985 |
Cohen RE, Foote J, Schachman HK. On conformational changes in the regulatory enzyme aspartate transcarbamoylase. Current Topics in Cellular Regulation. 26: 177-190. PMID 3907993 DOI: 10.1016/B978-0-12-152826-3.50021-8 |
0.318 |
|
| 1984 |
Hunt JB, Neece SH, Schachman HK, Ginsburg A. Mercurial-promoted Zn2+ release from Escherichia coli aspartate transcarbamoylase Journal of Biological Chemistry. 259: 14793-14803. PMID 6389552 |
0.448 |
|
| 1984 |
Hunt JB, Neece SH, Schachman HK, Ginsburg A. Mercurial-promoted Zn2+ release from E. coli aspartate transcarbamoylase Federation Proceedings. 43: no. 2345. |
0.419 |
|
| 1981 |
Hensley P, Yang YR, Schachman HK. On the detection of homotropic effects in enzymes of low co-operativity. Application to modified aspartate transcarbamoylase Journal of Molecular Biology. 152: 131-152. PMID 7040676 DOI: 10.1016/0022-2836(81)90098-X |
0.304 |
|
| 1981 |
Shrake A, Ginsburg A, Schachman HK. Calorimetric estimate of the enthalpy change for the substrate-promoted conformational transition of aspartate transcarbamoylase from Escherichia coli Journal of Biological Chemistry. 256: 5005-5015. PMID 7014568 |
0.441 |
|
| 1979 |
Hensley P, Schachman HK. Communication between dissimilar subunits in aspartate transcarbamoylase: effect of inhibitor and activator on the conformation of the catalytic polypeptide chains. Proceedings of the National Academy of Sciences of the United States of America. 76: 3732-3736. PMID 386346 DOI: 10.1073/Pnas.76.8.3732 |
0.333 |
|
| 1978 |
Howlett GJ, Yeh E, Schachman HK. Protein-ligand binding studies with a table-top, air-driven, high-speed centrifuge Archives of Biochemistry and Biophysics. 190: 809-819. PMID 718177 DOI: 10.1016/0003-9861(78)90341-7 |
0.328 |
|
| 1978 |
Yang YR, Kirschner MW, Schachman HK. [5] Aspartate transcarbamoylase (Escherichia coli): Preparation of subunits Methods in Enzymology. 51: 35-41. PMID 357897 DOI: 10.1016/S0076-6879(78)51007-0 |
0.307 |
|
| 1978 |
Syvanen M, Schachman HK. Donnan effect as measured by sedimentation equilibrium for the protein cytochrome c Biopolymers. 17: 943-956. PMID 207369 DOI: 10.1002/Bip.1978.360170412 |
0.317 |
|
| 1977 |
Subramani S, Bothwell MA, Gibbons I, Yang YR, Schachman HK. Ligand-promoted weakening of intersubunit bonding domains in aspartate transcarbamolylase. Proceedings of the National Academy of Sciences of the United States of America. 74: 3777-81. PMID 333446 DOI: 10.1073/Pnas.74.9.3777 |
0.302 |
|
| 1976 |
Gibbons I, Schachman HK. A method for the separation of hybrids of chromatographically identical oligomeric proteins. Use of 3,4,5,6-tetrahydrophthaloyl groups as a reversible "chromatographic handle" Biochemistry. 15: 52-60. PMID 1247510 DOI: 10.1021/Bi00646A009 |
0.32 |
|
| 1976 |
Gibbons I, Ritchey JM, Schachman HK. Concerted allosteric transition in hybrids of aspartate transcarbamoylase containing different arrangements of active and inactive sites. Biochemistry. 15: 1324-30. PMID 766835 DOI: 10.1021/Bi00651A024 |
0.319 |
|
| 1976 |
Blackburn MN, Schachman HK. Alteration of the allosteric properties of aspartate transcarbamoylase by pyridoxylation of the catalytic and regulatory subunits Biochemistry. 15: 1316-1323. PMID 766834 DOI: 10.1021/Bi00651A023 |
0.313 |
|
| 1975 |
Nagel GM, Schachman HK. Cooperative interactions in hybrids of aspartate transcarbamylase containing succinylated regulatory polypeptide chains. Biochemistry. 14: 3195-203. PMID 1096938 DOI: 10.1021/Bi00685A025 |
0.318 |
|
| 1974 |
Gibbons I, Yang YR, Schachman HK. Cooperative interactions in aspartate transcarbamoylase. 1. Hybrids composed of native and chemically inactivated catalytic polypeptide chains Proceedings of the National Academy of Sciences of the United States of America. 71: 4452-4456. PMID 4612521 DOI: 10.1073/Pnas.71.11.4452 |
0.325 |
|
| 1974 |
Bothwell M, Schachman HK. Pathways of assembly of aspartate transcarbamoylase from catalytic and regulatory subunits Proceedings of the National Academy of Sciences of the United States of America. 71: 3221-3225. PMID 4606892 DOI: 10.1073/Pnas.71.8.3221 |
0.306 |
|
| 1974 |
Yang YR, Syvanen JM, Nagel GM, Schachman HK. Aspartate transcarbamoylase molecules lacking one regulatory subunit Proceedings of the National Academy of Sciences of the United States of America. 71: 918-922. PMID 4595576 DOI: 10.1073/Pnas.71.3.918 |
0.317 |
|
| 1973 |
Edelstein SJ, Schachman HK. Measurement of partial specific volume by sedimentation equilibrium in H2O-D2O solutions. Methods in Enzymology. 27: 82-98. PMID 4797942 DOI: 10.1016/S0076-6879(73)27006-4 |
0.606 |
|
| 1973 |
Schachman HK, Edelstein SJ. Ultracentrifugal studies with absorption optics and a split-beam photoelectric scanner. Methods in Enzymology. 27: 3-59. PMID 4359237 DOI: 10.1016/S0076-6879(73)27003-9 |
0.605 |
|
| 1973 |
Smith GD, Schachman HK. Effect of D2O and nicotinamide adenine dinucleotide on the sedimentation properties and structure of glyceraldehyde phosphate dehydrogenase Biochemistry. 12: 3789-3801. PMID 4355539 DOI: 10.1021/Bi00744A001 |
0.308 |
|
| 1973 |
Schachman HK, Edelstein SJ. [1] Ultracentrifugal studies with absorption optics and a split-beam photoelectric scanner Methods in Enzymology. 27: 3-59. DOI: 10.1016/S0076-6879(73)27003-9 |
0.503 |
|
| 1972 |
Richards EG, Bell-Clark J, Kirschner M, Rosenthal A, Schachman HK. Alignment of schlieren and Rayleigh optical systems in the ultracentrifuge. 3. Design, construction, and placement of Rayleigh mask Analytical Biochemistry. 46: 295-331. PMID 5017662 DOI: 10.1016/0003-2697(72)90423-X |
0.627 |
|
| 1971 |
Richards EG, Teller DC, Hoagland VD, Haschemeyer RH, Schachman HK. Alignment of schlieren and Rayleigh optical systems in the ultracentrifuge. II. A general procedure. Analytical Biochemistry. 41: 215-47. PMID 5578542 DOI: 10.1016/0003-2697(71)90206-5 |
0.711 |
|
| 1971 |
Richards EG, Teller D, Schachman HK. Alignment of schlieren and Rayleigh optical systems in the ultracentrifuge. I. Focusing of the camera and cylindrical lenses. Analytical Biochemistry. 41: 189-214. PMID 5578541 DOI: 10.1016/0003-2697(71)90205-3 |
0.723 |
|
| 1971 |
Kirschner MW, Schachman HK. Conformational changes in proteins as measured by difference sedimentation studies. II. Effect of stereospecific ligands on the catalytic subunit of aspartate transcarbamylase. Biochemistry. 10: 1919-26. PMID 5563768 DOI: 10.1021/Bi00786A028 |
0.322 |
|
| 1971 |
Kirschner MW, Schachman HK. Conformational changes in proteins as measured by difference sedimentation studies. I. A technique for measuring small changes in sedimentation coefficient. Biochemistry. 10: 1900-19. PMID 5563767 DOI: 10.1021/Bi00786A027 |
0.313 |
|
| 1971 |
Kellett GL, Schachman HK. Dissociation of hemoglobin into subunits. Monomer formation and the influence of ligands Journal of Molecular Biology. 59: 387-399. PMID 4999040 DOI: 10.1016/0022-2836(71)90306-8 |
0.301 |
|
| 1970 |
Meighen EA, Pigiet V, Schachman HK. Hybridization of native and chemically modified enzymes. 3. The catalytic subunits of aspartate transcarbamylase Proceedings of the National Academy of Sciences of the United States of America. 65: 234-241. PMID 5263753 DOI: 10.1073/Pnas.65.1.234 |
0.314 |
|
| 1969 |
Teller DC, Horbett TA, Richards EG, Schachman HK. ULTRACENTRIFUGE STUDIES WITH RAYLEIGH INTERFERENCE OPTICS. III. COMPUTATIONAL METHODS APPLIED TO HIGH-SPEED SEDIMENTATION EQUILIBRIUM EXPERIMENTS Annals of the New York Academy of Sciences. 164: 66-100. DOI: 10.1111/J.1749-6632.1969.Tb14033.X |
0.715 |
|
| 1968 |
Richards EG, Teller DC, Schachman HK. Ultracentrifuge studies with Rayleigh interference optics. II. Low-speed sedimentation equilibrium of homogeneous systems. Biochemistry. 7: 1054-76. PMID 5657846 DOI: 10.1021/bi00843a026 |
0.708 |
|
| 1967 |
Edelstein SJ, Schachman HK. The simultaneous determination of partial specific volumes and molecular weights with microgram quantities. The Journal of Biological Chemistry. 242: 306-11. PMID 6016615 |
0.5 |
|
| 1966 |
Schachman HK, Edelstein SJ. Ultracentrifuge studies with absorption optics. IV. Molecular weight determinations at the microgram level. Biochemistry. 5: 2681-705. PMID 5968578 |
0.531 |
|
| 1965 |
Gerhart JC, Schachman HK. Distinct subunits for the regulation and catalytic activity of aspartate transcarbamylase. Biochemistry. 4: 1054-62. PMID 5320387 DOI: 10.1021/Bi00882A012 |
0.341 |
|
| 1963 |
LAMERS K, PUTNEY F, STEINBERG IZ, SCHACHMAN HK. ULTRACENTRIFUGE STUDIES WITH ABSORPTION OPTICS. 3. A SPLIT-BEAM PHOTOELECTRIC, SCANNING ABSORPTION SYSTEM. Archives of Biochemistry and Biophysics. 103: 379-400. PMID 14099549 DOI: 10.1016/0003-9861(63)90428-4 |
0.32 |
|
| 1962 |
Schachman HK, Gropper L, Hanlon S, Putney F. Ultracentrifuge studies with absorption optics. II. Incorporation of a monochromator and its application to the study of proteins and interacting systems Archives of Biochemistry and Biophysics. 99: 175-190. PMID 13976566 DOI: 10.1016/0003-9861(62)90259-X |
0.357 |
|
| 1962 |
Hanlon S, Lamers K, Lauterbach G, Johnson R, Schachman HK. Ultracentrifuge studies with absorption optics. I. An automatic photoelectric scanning absorption system Archives of Biochemistry and Biophysics. 99: 157-174. PMID 13952541 DOI: 10.1016/0003-9861(62)90258-8 |
0.371 |
|
| 1960 |
GINSBURG A, SCHACHMAN HK. Studies on the enzymatic breakdown of proteins. II. The action of pepsin on ribonuclease and considerations of the structure of ribonuclease. The Journal of Biological Chemistry. 235: 115-23. PMID 13850236 |
0.448 |
|
| 1960 |
GINSBURG A, SCHACHMAN HK. Studies on the enzymatic breakdown of proteins. I. Action of chymotrypsin on insulin. The Journal of Biological Chemistry. 235: 108-14. PMID 13850235 |
0.418 |
|
| 1958 |
Hersh RT, Schachman HK. On the size of the protein subunits in bushy stunt virus Virology. 6: 234-243. PMID 13581528 DOI: 10.1016/0042-6822(58)90072-2 |
0.328 |
|
| 1957 |
SCHUMAKER VN, SCHACHMAN HK. Ultracentrifugal analysis of dilute solutions. Biochimica Et Biophysica Acta. 23: 628-39. PMID 13426176 DOI: 10.1016/0006-3002(57)90386-4 |
0.579 |
|
| 1956 |
APPEL P, GINSBURG A, SCHACHMAN HK. Molecular-weight determinations during the approach to sedimentation equilibrium. Archives of Biochemistry and Biophysics. 65: 545-66. PMID 13395509 DOI: 10.1016/0003-9861(56)90213-2 |
0.538 |
|
| 1956 |
HARRINGTON WF, SCHACHMAN HK. Studies on the alkaline degradation of tobacco mosaic virus. I. Ultracentrifugal analysis. Archives of Biochemistry and Biophysics. 65: 278-95. PMID 13373425 DOI: 10.1016/0003-9861(56)90194-1 |
0.562 |
|
| 1956 |
Schumaker VN, Richards EG, Schachman HK. A study of the kinetics of the enzymatic digestion of deoxyribonucleic acid Journal of the American Chemical Society. 78: 4230-4236. DOI: 10.1021/Ja01598A011 |
0.523 |
|
| 1954 |
Trautman R, Schumaker VN, Harrington WF, Schachman HK. The determination of concentrations in the ultracentrifugation of two-component systems The Journal of Chemical Physics. 22: 555-559. DOI: 10.1063/1.1740106 |
0.668 |
|
| 1954 |
Schachman HK, Harrington WF. Ultracentrifuge studies with a synthetic boundary cell. I. General applications Journal of Polymer Science. 12: 379-390. DOI: 10.1002/Pol.1954.120120130 |
0.587 |
|
| 1953 |
Harrington WF, Schachman HK. Analysis of a concentration anomaly in the ultracentrifugation of mixtures Journal of the American Chemical Society. 75: 3533-3539. |
0.491 |
|
| 1952 |
Pickels EG, Harrington WF, Schachman HK. An Ultracentrifuge Cell for Producing Boundaries Synthetically by a Layering Technique. Proceedings of the National Academy of Sciences of the United States of America. 38: 943-8. PMID 16589206 DOI: 10.1073/Pnas.38.11.943 |
0.573 |
|
| 1952 |
Schachman HK, Harrington WF. ON VISCOSITY MEASUREMENT IN THE ULTRACENTRIFUGE1 Journal of the American Chemical Society. 74: 3965-3966. DOI: 10.1021/ja01135a533 |
0.47 |
|
| 1950 |
Schachman HK, Lauffer MA. The density correction of sedimentation constants Journal of the American Chemical Society. 72: 4266-4268. DOI: 10.1021/Ja01165A124 |
0.552 |
|
| 1949 |
Schachman HK, Kauzmann WJ. Viscosity and sedimentation studies on tobacco mosaic virus Journal of Physical and Colloid Chemistry. 53: 150-162. PMID 18112152 |
0.708 |
|
| 1949 |
SCHACHMAN HK, LAUFFER MA. The hydration, size and shape of tobacco mosaic virus. Journal of the American Chemical Society. 71: 536-41. PMID 18112063 DOI: 10.1021/Ja01170A047 |
0.515 |
|
| 1948 |
Schachman HK. Determination of sedimentation constants in the sharples supercentrifuge Journal of Physical and Colloid Chemistry. 52: 1034-1045. PMID 18867473 DOI: 10.1021/J150462A013 |
0.304 |
|
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