| Year |
Citation |
Score |
| 2010 |
Schröder-Tittmann K, Bosse-Doenecke E, Reedtz-Runge S, Ihling C, Sinz A, Tittmann K, Rudolph R. Recombinant expression, in vitro refolding, and biophysical characterization of the human glucagon-like peptide-1 receptor Biochemistry. 49: 7956-7965. PMID 20690636 DOI: 10.1021/Bi101159S |
0.324 |
|
| 2006 |
Kliemannel M, Weininger U, Balbach J, Schwarz E, Rudolph R. Examination of the slow unfolding of pro-nerve growth factor argues against a loop threading mechanism for nerve growth factor Biochemistry. 45: 3517-3524. PMID 16533032 DOI: 10.1021/Bi051896T |
0.37 |
|
| 2004 |
Huemmerich D, Helsen CW, Quedzuweit S, Oschmann J, Rudolph R, Scheibel T. Primary structure elements of spider dragline silks and their contribution to protein solubility. Biochemistry. 43: 13604-12. PMID 15491167 DOI: 10.1021/Bi048983Q |
0.36 |
|
| 2002 |
Buchner J, Rudolph R, Lilie H. Intradomain disulfide bonds impede formation of the alternatively folded state of antibody chains. Journal of Molecular Biology. 318: 829-36. PMID 12054826 DOI: 10.1016/S0022-2836(02)00171-7 |
0.52 |
|
| 2002 |
Winter J, Klappa P, Freedman RB, Lilie H, Rudolph R. Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin. The Journal of Biological Chemistry. 277: 310-7. PMID 11694508 DOI: 10.1074/jbc.M107832200 |
0.307 |
|
| 2001 |
Richter SA, Stubenrauch K, Lilie H, Rudolph R. Polyionic fusion peptides function as specific dimerization motifs Protein Engineering. 14: 775-783. PMID 11739896 DOI: 10.1093/Protein/14.10.775 |
0.321 |
|
| 1999 |
Esser D, Rudolph R, Jaenicke R, Böhm G. The HU protein from Thermotoga maritima: Recombinant expression, purification and physicochemical characterization of an extremely hyperthermophilic DNA-binding protein Journal of Molecular Biology. 291: 1135-1146. PMID 10518949 DOI: 10.1006/Jmbi.1999.3022 |
0.469 |
|
| 1998 |
Nichtl A, Buchner J, Jaenicke R, Rudolph R, Scheibel T. Folding and association of beta-Galactosidase. Journal of Molecular Biology. 282: 1083-91. PMID 9753555 DOI: 10.1006/Jmbi.1998.2075 |
0.644 |
|
| 1998 |
Tittmann K, Proske D, Spinka M, Ghisla S, Rudolph R, Hübner G, Kern G. Activation of thiamin diphosphate and FAD in the phosphate-dependent pyruvate oxidase from Lactobacillus plantarum Journal of Biological Chemistry. 273: 12929-12934. PMID 9582325 DOI: 10.1074/jbc.273.21.12929 |
0.337 |
|
| 1997 |
Rudolph R, Lilie H. In vitro‐Faltung von Inclusion Body‐Proteinen Nachrichten Aus Chemie Technik Und Laboratorium. 45: 753-758. DOI: 10.1002/Nadc.19970450709 |
0.303 |
|
| 1996 |
Stempfer G, Höll-Neugebauer B, Kopetzki E, Rudolph R. A fusion protein designed for noncovalent immobilization: Stability, enzymatic activity, and use in an enzyme reactor Nature Biotechnology. 14: 481-484. PMID 9630924 |
0.323 |
|
| 1996 |
Lamba D, Bauer M, Huber R, Fischer S, Rudolph R, Kohnert U, Bode W. The 2.3 Å Crystal Structure of the Catalytic Domain of Recombinant Two-chain Human Tissue-type Plasminogen Activator Journal of Molecular Biology. 258: 117-135. PMID 8613982 DOI: 10.1006/Jmbi.1996.0238 |
0.357 |
|
| 1996 |
Berchtold H, Rudolph R, Kiefhaber T, Darlison MG, Breitenbach U, Lübbert H, Boddeke HGWM, Blohm D. Biochemie und Molekulargenetik 1995 Nachrichten Aus Chemie Technik Und Laboratorium. 44: 168-182. DOI: 10.1002/Nadc.19960440209 |
0.548 |
|
| 1995 |
Lilie H, Rudolph R, Buchner J. Association of antibody chains at different stages of folding: Prolyl isomerization occurs after formation of quaternary structure Journal of Molecular Biology. 248: 190-201. PMID 7731044 DOI: 10.1006/Jmbi.1995.0211 |
0.601 |
|
| 1994 |
Muller YA, Schumacher G, Rudolph R, Schulz GE. The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum Journal of Molecular Biology. 237: 315-335. PMID 8145244 DOI: 10.1006/Jmbi.1994.1233 |
0.41 |
|
| 1994 |
Zink T, Ross A, Lüers K, Cieslar C, Rudolph R, Holak TA. Structure and dynamics of the human granulocyte colony-stimulating factor determined by NMR spectroscopy. Loop mobility in a four-helix-bundle protein Biochemistry. 33: 8453-8463. PMID 7518249 DOI: 10.1021/Bi00194A009 |
0.337 |
|
| 1993 |
Schumann J, Böhm G, Schumacher G, Rudolph R, Jaenicke R. Stabilization of creatinase from Pseudomonas putida by random mutagenesis. Protein Science : a Publication of the Protein Society. 2: 1612-20. PMID 8251936 DOI: 10.1002/Pro.5560021007 |
0.542 |
|
| 1993 |
Lilie H, Lang K, Rudolph R, Buchner J. Prolyl isomerases catalyze antibody folding in vitro Protein Science. 2: 1490-1496. PMID 8104614 DOI: 10.1002/Pro.5560020913 |
0.609 |
|
| 1992 |
Kohnert U, Rudolph R, Verheijen JH, Jacoline E, Weening-Verhoeff D, Stern A, Opitz U, Martin U, Lill H, Prinz H, Lechner M, Kresse G, Bucket P, Fischer S. Biochemical properties of the kringle 2 and protease domains are maintained in the refolded t-PA deletion variant BM 06.022. Protein Engineering. 5: 93-100. PMID 1321420 DOI: 10.1093/Protein/5.1.93 |
0.312 |
|
| 1992 |
Risse B, Stempfer G, Rudolph R, Schumacher G, Jaenicke R. Characterization of the stabilizing effect of point mutations of pyruvate oxidase from Lactobacillus plantarum: protection of the native state by modulating coenzyme binding and subunit interaction. Protein Science : a Publication of the Protein Society. 1: 1710-8. PMID 1304900 DOI: 10.1002/Pro.5560011219 |
0.566 |
|
| 1992 |
Risse B, Stempfer G, Rudolph R, Möllering H, Jaenicke R. Stability and reconstitution of pyruvate oxidase from Lactobacillus plantarum: dissection of the stabilizing effects of coenzyme binding and subunit interaction. Protein Science : a Publication of the Protein Society. 1: 1699-709. PMID 1304899 DOI: 10.1002/Pro.5560011218 |
0.602 |
|
| 1992 |
Rudolph R, Siebendritt R, Kiefhaber T. Reversible unfolding and refolding behavior of a monomeric aldolase from Staphylococcus aureus Protein Science. 1: 654-666. PMID 1304364 DOI: 10.1002/Pro.5560010511 |
0.681 |
|
| 1991 |
Siebendritt R, Sharma AK, Rudolph R, Jaenicke R. Analysis of protein folding by fast protein liquid chromatography. Modular domain folding of gamma-II-crystallin from calf eye-lens. Biological Chemistry Hoppe-Seyler. 372: 23-6. PMID 2039601 DOI: 10.1515/Bchm3.1991.372.1.23 |
0.56 |
|
| 1991 |
Goldberg ME, Rudolph R, Jaenicke R. A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme. Biochemistry. 30: 2790-7. PMID 2007117 DOI: 10.1021/Bi00225A008 |
0.633 |
|
| 1991 |
Buchner J, Renner M, Lilie H, Hinz HJ, Jaenicke R, Kiefhabel T, Rudolph R. Alternatively folded states of an immunoglobulin. Biochemistry. 30: 6922-9. PMID 1906346 DOI: 10.1021/Bi00242A016 |
0.673 |
|
| 1991 |
Buchner J, Schmidt M, Fuchs M, Jaenicke R, Rudolph R, Schmid FX, Kiefhaber T. GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry. 30: 1586-91. PMID 1671555 DOI: 10.1021/Bi00220A020 |
0.774 |
|
| 1991 |
Buchner J, Rudolph R. Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Bio/Technology (Nature Publishing Company). 9: 157-62. PMID 1369317 DOI: 10.1038/Nbt0291-157 |
0.545 |
|
| 1991 |
Buchner J, Rudolph R. Routes to active proteins from transformed microorganisms. Current Opinion in Biotechnology. 2: 532-538. PMID 1367672 DOI: 10.1016/0958-1669(91)90077-I |
0.539 |
|
| 1991 |
Kiefhaber T, Rudolph R, Kohler HH, Buchner J. Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation. Bio/Technology (Nature Publishing Company). 9: 825-9. PMID 1367356 DOI: 10.1038/Nbt0991-825 |
0.714 |
|
| 1990 |
Rudolph R, Siebendritt R, Nesslaŭer G, Sharma AK, Jaenicke R. Folding of an all-beta protein: independent domain folding in gamma II-crystallin from calf eye lens. Proceedings of the National Academy of Sciences of the United States of America. 87: 4625-9. PMID 2352939 DOI: 10.1073/Pnas.87.12.4625 |
0.598 |
|
| 1990 |
Scheibe R, Rudolph R, Reng W, Jaenicke R. Structural and catalytic properties of oxidized and reduced chloroplast NADP-malate dehydrogenase upon denaturation and renaturation. European Journal of Biochemistry / Febs. 189: 581-7. PMID 2351138 DOI: 10.1111/J.1432-1033.1990.Tb15526.X |
0.591 |
|
| 1990 |
Sharma AK, Minke-Gogl V, Gohl P, Siebendritt R, Jaenicke R, Rudolph R. Limited proteolysis of gamma II-crystallin from calf eye lens. Physicochemical studies on the N-terminal domain and the intact two-domain protein. European Journal of Biochemistry / Febs. 194: 603-9. PMID 2269285 DOI: 10.1111/J.1432-1033.1990.Tb15659.X |
0.542 |
|
| 1987 |
Opitz U, Rudolph R, Jaenicke R, Ericsson L, Neurath H. Proteolytic dimers of porcine muscle lactate dehydrogenase: characterization, folding, and reconstitution of the truncated and nicked polypeptide chain. Biochemistry. 26: 1399-406. PMID 3567177 DOI: 10.1021/Bi00379A028 |
0.558 |
|
| 1987 |
Teschner W, Rudolph R, Garel JR. Intermediates on the folding pathway of octopine dehydrogenase from Pecten jacobaeus Biochemistry. 26: 2791-2796. DOI: 10.1021/Bi00384A021 |
0.349 |
|
| 1986 |
Jaenicke R, Rudolph R. Refolding and association of oligomeric proteins. Methods in Enzymology. 131: 218-50. PMID 3773759 DOI: 10.1016/0076-6879(86)31043-7 |
0.513 |
|
| 1986 |
Rudolph R, Fuchs I, Jaenicke R. Reassociation of dimeric cytoplasmic malate dehydrogenase is determined by slow and very slow folding reactions. Biochemistry. 25: 1662-9. PMID 3707900 DOI: 10.1021/Bi00355A033 |
0.643 |
|
| 1986 |
Jaenicke R, Rudolph R, Feingold DS. Dissociation and in vitro reconstitution of bovine liver uridine diphosphoglucose dehydrogenase. The paired subunit nature of the enzyme. Biochemistry. 25: 7283-7. PMID 3099833 |
0.605 |
|
| 1986 |
Söylemez Z, Rudolph R, Jaenicke R. Isoproterenol inhibition of horse serum cholinesterase is connected with subunit dissociation. Biological Chemistry Hoppe-Seyler. 367: 705-13. PMID 3094553 DOI: 10.1515/Bchm3.1986.367.2.705 |
0.577 |
|
| 1985 |
Gerl M, Rudolph R, Jaenicke R. Mechanism and specificity of reconstitution of dimeric lactate dehydrogenase from Limulus polyphemus. Biological Chemistry Hoppe-Seyler. 366: 447-54. PMID 4005047 DOI: 10.1515/Bchm3.1985.366.1.447 |
0.601 |
|
| 1985 |
Rudolph R. The use of limited proteolysis in studies on protein folding and association. Biochemical Society Transactions. 13: 308-312. PMID 3926553 DOI: 10.1042/Bst0130308 |
0.35 |
|
| 1984 |
Zettlmeissl G, Teschner W, Rudolph R, Jaenicke R, Gäde G. Isolation, physicochemical properties, and folding of octopine dehydrogenase from Pecten jacobaeus. European Journal of Biochemistry / Febs. 143: 401-7. PMID 6468402 DOI: 10.1111/J.1432-1033.1984.Tb08387.X |
0.597 |
|
| 1983 |
Rudolph R, Bohrer M, Fischer S. Physicochemical characterization of a fast refolding monomeric class I fructose-1,6-bisphosphate aldolase from Staphylococcus aureus. European Journal of Biochemistry. 131: 383-6. PMID 6832156 DOI: 10.1111/J.1432-1033.1983.Tb07274.X |
0.439 |
|
| 1983 |
Girg R, Jaenicke R, Rudolph R. Dimers of porcine skeletal muscle lactate dehydrogenase produced by limited proteolysis during reassociation are enzymatically active in the presence of stabilizing salt. Biochemistry International. 7: 433-41. PMID 6679740 |
0.583 |
|
| 1983 |
Girg R, Rudolph R, Jaenicke R. The dimeric intermediate on the pathway of reconstitution of lactate dehydrogenase is enzymatically active. Febs Letters. 163: 132-5. PMID 6628683 DOI: 10.1016/0014-5793(83)81179-X |
0.532 |
|
| 1983 |
Rudolph R, Fuchs I. Influence of glutathione on the reactivation of enzymes containing cysteine or cystine. Biological Chemistry. 364: 813-820. PMID 6618443 DOI: 10.1515/Bchm2.1983.364.2.813 |
0.43 |
|
| 1983 |
Zettlmeissl G, Rudolph R, Jaenicke R. Limited proteolysis as a tool to study the kinetics of protein folding: conformational rearrangements in acid-dissociated lactic dehydrogenase as determined by pepsin digestion. Archives of Biochemistry and Biophysics. 224: 161-8. PMID 6408987 DOI: 10.1016/0003-9861(83)90200-X |
0.609 |
|
| 1983 |
Hermann R, Rudolph R, Jaenicke R, Price NC, Scobbie A. The reconstitution of denatured phosphoglycerate mutase. The Journal of Biological Chemistry. 258: 11014-9. PMID 6309828 |
0.577 |
|
| 1982 |
Hermann R, Rudolph R, Jaenicke R. The use of subunit hybridization to monitor the reassociation of porcine lactate dehydrogenase after acid dissociation. Hoppe-Seyler's Zeitschrift FüR Physiologische Chemie. 363: 1259-65. PMID 7141407 DOI: 10.1515/Bchm2.1982.363.2.1259 |
0.559 |
|
| 1982 |
Zettlmeissl G, Rudolph R, Jaenicke R. The yield of reactivation of lactic dehydrogenase after guanidine HCl denaturation is not determined by proline cis in equilibrium trans isomerization. European Journal of Biochemistry / Febs. 125: 605-8. PMID 7117258 DOI: 10.1111/J.1432-1033.1982.Tb06725.X |
0.616 |
|
| 1982 |
Zettlmeissl G, Rudolph R, Jaenicke R. Rate-determining folding and association reactions on the reconstitution pathway of porcine skeletal muscle lactic dehydrogenase after denaturation by guanidine hydrochloride. Biochemistry. 21: 3946-50. PMID 6812620 |
0.548 |
|
| 1981 |
Zettlmeissl G, Rudolph R, Jaenicke R. Reconstitution of lactic dehydrogenase after acid dissociation. The yield of reactivation is determined by conformational rearrangements of the dissociated monomers. European Journal of Biochemistry / Febs. 121: 169-75. PMID 7327168 DOI: 10.1111/J.1432-1033.1981.Tb06446.X |
0.596 |
|
| 1981 |
Girg R, Rudolph R, Jaenicke R. Limited proteolysis of porcine-muscle lactic dehydrogenase by thermolysin during reconstitution yields dimers. European Journal of Biochemistry / Febs. 119: 301-5. PMID 7308187 DOI: 10.1111/J.1432-1033.1981.Tb05608.X |
0.612 |
|
| 1981 |
Jaenicke R, Vogel W, Rudolph R. Dimeric intermediates in the dissociation of lactic dehydrogenase. European Journal of Biochemistry / Febs. 114: 525-31. PMID 7238500 DOI: 10.1111/J.1432-1033.1981.Tb05176.X |
0.635 |
|
| 1981 |
Bernhardt G, Rudolph R, Jaenicke R. Reassociation of lactic dehydrogenase from pig heart studied by cross-linking with glutaraldehyde. Zeitschrift FüR Naturforschung. Section C: Biosciences. 36: 772-7. PMID 6795844 DOI: 10.1515/Znc-1981-9-1013 |
0.59 |
|
| 1981 |
Hermann R, Jaenicke R, Rudolph R. Analysis of the reconstitution of oligomeric enzymes by cross-linking with glutaraldehyde: kinetics of reassociation of lactic dehydrogenase. Biochemistry. 20: 5195-201. PMID 6794607 DOI: 10.1021/Bi00521A015 |
0.594 |
|
| 1980 |
Schade BC, Lüdemann HD, Rudolph R, Jaenicke R. Kinetics of reconstitution of porcein muscle lactic dehydrogenase after reversible high pressure dissociation. Biophysical Chemistry. 11: 257-63. PMID 7370389 DOI: 10.1016/0301-4622(80)80028-7 |
0.618 |
|
| 1980 |
Schade BC, Rudolph R, Lüdemann HD, Jaenicke R. Reversible high-pressure dissociation of lactic dehydrogenase from pig muscle. Biochemistry. 19: 1121-6. PMID 7370228 DOI: 10.1021/Bi00547A013 |
0.472 |
|
| 1980 |
Zabori S, Rudolph R, Jaenicke R. Folding and association of triose phosphate isomerase from rabbit muscle. Zeitschrift FüR Naturforschung. Section C: Biosciences. 35: 999-1004. PMID 7210812 DOI: 10.1515/Znc-1980-11-1224 |
0.636 |
|
| 1980 |
Rudolph R, Zettlmeissl G, Jaenicke R. Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 2. Reactivation of irreversibly denatured aggregates. Biochemistry. 18: 5572-5. PMID 518856 DOI: 10.1021/Bi00592A008 |
0.623 |
|
| 1980 |
Zettlmeissl G, Rudolph R, Jaenicke R. Effects of low concentrations of guanidine . HCl on the reconstitution of lactic dehydrogenase from pig muscle in vitro. Evidence for guanidine binding to the native enzyme. European Journal of Biochemistry. 100: 593-8. PMID 510298 DOI: 10.1111/J.1432-1033.1979.Tb04206.X |
0.61 |
|
| 1980 |
Krebs H, Rudolph R, Jaenicke R. Influence of coenzyme on the refolding and reassociation in vitro of glyceraldehyde-3-phosphate dehydrogenase from yeast. European Journal of Biochemistry. 100: 359-64. PMID 228931 DOI: 10.1111/J.1432-1033.1979.Tb04178.X |
0.601 |
|
| 1980 |
Jaenicke R, Krebs H, Rudolph R, Woenckhaus C. Rate enhancement of reconstitution of glyceraldehyde-3-phosphate dehydrogenase by a covalently bound coenzyme analog. Proceedings of the National Academy of Sciences. 77: 1966-1969. DOI: 10.1073/Pnas.77.4.1966 |
0.62 |
|
| 1979 |
Jaenicke R, Rudolph R, Heider I. Quaternary structure, subunit activity, and in vitro association of porcine mitochondrial malic dehydrogenase. Biochemistry. 18: 1217-23. PMID 570852 DOI: 10.1021/Bi00574A016 |
0.493 |
|
| 1979 |
Zettlmeissl G, Rudolph R, Jaenicke R. Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation Biochemistry. 18: 5567-5571. DOI: 10.1021/Bi00592A007 |
0.519 |
|
| 1978 |
Rudolph R, Gerschitz J, Jaenicke R. Effect of zinc(II) on the refolding and reactivation of liver alcohol dehydrogenase. European Journal of Biochemistry. 87: 601-6. PMID 679951 DOI: 10.1111/J.1432-1033.1978.Tb12412.X |
0.57 |
|
| 1978 |
Gerschitz J, Rudolph R, Jaenicke R. Refolding and reactivation of liver alcohol dehydrogenase after dissociation and denaturation in 6M guanidine hydrochloride. European Journal of Biochemistry. 87: 591-9. PMID 210018 DOI: 10.1111/J.1432-1033.1978.Tb12411.X |
0.592 |
|
| 1978 |
Rudolph R, Heider I, Jaenicke R. Mechanism of reactivation and refolding of glyceraldehyde-3-phosphate dehydrogenase from yeast after denaturation and dissociation. European Journal of Biochemistry. 81: 563-70. PMID 202463 DOI: 10.1111/J.1432-1033.1977.Tb11983.X |
0.614 |
|
| 1978 |
Rudolph R, Heider I, Jaenicke R. Effect of coenzymes and temperature on the process of in vitro refolding and reassociation of lactic dehydrogenase isoenzymes. Biochemistry. 16: 5527-31. PMID 200265 DOI: 10.1021/Bi00644A021 |
0.585 |
|
| 1978 |
Rudolph R, Haselbeck A, Knorr F, Jaenicke R. Reconstitution of rabbit muscle aldolase after dissociation and denaturation at alkaline pH. Hoppe-Seyler's Zeitschrift FüR Physiologische Chemie. 359: 867-71. PMID 30685 DOI: 10.1515/Bchm2.1978.359.2.867 |
0.567 |
|
| 1977 |
Gerschitz J, Rudolph R, Jaenicke R. Kinetics of reactivation of rabbit muscle aldolase after denaturation and dissociation in various solvent media. Biophysics of Structure and Mechanism. 3: 291-302. PMID 901915 DOI: 10.1007/BF00535702 |
0.385 |
|
| 1977 |
Rudolph R, Westhof E, Jaenicke R. Kinetic analysis of the reactivation of rabbit muscle aldolase after denaturation with guanidine-HCL. Febs Letters. 73: 204-6. PMID 402289 DOI: 10.1016/0014-5793(77)80981-2 |
0.518 |
|
| 1977 |
Rudolph R, Heider I, Westhof E, Jaenicke R. Mechanism of refolding and reactivation of lactic dehydrogenase from pig heart after dissociation in various solvent media. Biochemistry. 16: 3384-90. PMID 19049 DOI: 10.1021/Bi00634A015 |
0.49 |
|
| 1976 |
Rudolph R, Engelhard M, Jaenicke R. Kinetics of refolding and reactivation of rabbit-muscle aldolase after acid dissociation. European Journal of Biochemistry. 67: 455-62. PMID 986942 DOI: 10.1111/J.1432-1033.1976.Tb10710.X |
0.62 |
|
| 1976 |
Engelhard M, Rudolph R, Jaenicke R. Equilibrium studies on the refolding and reactivation of rabbit-muscle aldolase after acid dissociation. European Journal of Biochemistry. 67: 447-53. PMID 9280 DOI: 10.1111/J.1432-1033.1976.Tb10709.X |
0.6 |
|
| 1976 |
Rudolph R, Jaenicke R. Kinetics of reassociation and reactivation of pig-muscle lactic dehydrogenase after acid dissociation. European Journal of Biochemistry. 63: 409-17. PMID 4322 DOI: 10.1111/J.1432-1033.1976.Tb10242.X |
0.627 |
|
| 1975 |
Rudolph R, Holler E, Jaenicke R. Fluorescence and stopped-flow studies on the N ∡ F transition of serumalbumin Biophysical Chemistry. 3: 226-233. PMID 240454 DOI: 10.1016/0301-4622(75)80014-7 |
0.503 |
|
| 1975 |
Jaenicke R, Engelhard M, Kraus E, Rudolph R. Reversible Dissociation of Glycolytic Enzymes: Kinetic Studies on Lactate Dehydrogenase, Glyceraldehyde 3-Phosphate Dehydrogenase and Aldolase Biochemical Society Transactions. 3: 1051-1054. DOI: 10.1042/Bst0031051 |
0.573 |
|
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