| Year |
Citation |
Score |
| 2005 |
Schneider B, Knöchel T, Darimont B, Hennig M, Dietrich S, Babinger K, Kirschner K, Sterner R. Role of the N-terminal extension of the (betaalpha)8-barrel enzyme indole-3-glycerol phosphate synthase for its fold, stability, and catalytic activity. Biochemistry. 44: 16405-12. PMID 16342933 DOI: 10.1021/Bi051640N |
0.51 |
|
| 2002 |
Henn-Sax M, Thoma R, Schmidt S, Hennig M, Kirschner K, Sterner R. Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substrates. Biochemistry. 41: 12032-42. PMID 12356303 DOI: 10.1021/Bi026092H |
0.47 |
|
| 2002 |
Mayans O, Ivens A, Nissen LJ, Kirschner K, Wilmanns M. Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry. The Embo Journal. 21: 3245-54. PMID 12093726 DOI: 10.1093/Emboj/Cdf298 |
0.43 |
|
| 2002 |
Hennig M, Darimont BD, Jansonius JN, Kirschner K. The catalytic mechanism of indole-3-glycerol phosphate synthase: crystal structures of complexes of the enzyme from Sulfolobus solfataricus with substrate analogue, substrate, and product. Journal of Molecular Biology. 319: 757-66. PMID 12054868 DOI: 10.1016/S0022-2836(02)00378-9 |
0.459 |
|
| 2002 |
Ivens A, Mayans O, Szadkowski H, Jürgens C, Wilmanns M, Kirschner K. Stabilization of a (betaalpha)8-barrel protein by an engineered disulfide bridge. European Journal of Biochemistry / Febs. 269: 1145-53. PMID 11856350 DOI: 10.1046/J.1432-1033.2002.02745.X |
0.396 |
|
| 2002 |
Knöchel T, Pappenberger A, Jansonius JN, Kirschner K. The crystal structure of indoleglycerol-phosphate synthase from Thermotoga maritima. Kinetic stabilization by salt bridges. The Journal of Biological Chemistry. 277: 8626-34. PMID 11741953 DOI: 10.1074/Jbc.M109517200 |
0.42 |
|
| 2001 |
Ivens A, Mayans O, Szadkowski H, Wilmanns M, Kirschner K. Purification, characterization and crystallization of thermostable anthranilate phosphoribosyltransferase from Sulfolobus solfataricus. European Journal of Biochemistry. 268: 2246-52. PMID 11298741 DOI: 10.1046/J.1432-1327.2001.02102.X |
0.358 |
|
| 2001 |
Sterner R, Merz A, Thoma R, Kirschner K. Phosphoribosylanthranilate isomerase and indoleglycerol-phosphate synthase: tryptophan biosynthetic enzymes from Thermotoga maritima. Methods in Enzymology. 331: 270-80. PMID 11265469 DOI: 10.1016/S0076-6879(01)31064-9 |
0.496 |
|
| 2000 |
Thoma R, Hennig M, Sterner R, Kirschner K. Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermotoga maritima. Structure (London, England : 1993). 8: 265-76. PMID 10745009 DOI: 10.1016/S0969-2126(00)00106-4 |
0.381 |
|
| 2000 |
Merz A, Yee MC, Szadkowski H, Pappenberger G, Crameri A, Stemmer WP, Yanofsky C, Kirschner K. Improving the catalytic activity of a thermophilic enzyme at low temperatures. Biochemistry. 39: 880-9. PMID 10653631 DOI: 10.1021/Bi992333I |
0.469 |
|
| 1999 |
Knöchel T, Ivens A, Hester G, Gonzalez A, Bauerle R, Wilmanns M, Kirschner K, Jansonius JN. The crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications. Proceedings of the National Academy of Sciences of the United States of America. 96: 9479-84. PMID 10449718 DOI: 10.1073/Pnas.96.17.9479 |
0.481 |
|
| 1999 |
Merz A, Knöchel T, Jansonius JN, Kirschner K. The hyperthermostable indoleglycerol phosphate synthase from Thermotoga maritima is destabilized by mutational disruption of two solvent-exposed salt bridges. Journal of Molecular Biology. 288: 753-63. PMID 10329177 DOI: 10.1006/Jmbi.1999.2709 |
0.448 |
|
| 1999 |
Thoma R, Schwander M, Liebl W, Kirschner K, Sterner R. A histidine gene cluster of the hyperthermophile Thermotoga maritima: sequence analysis and evolutionary significance. Extremophiles : Life Under Extreme Conditions. 2: 379-89. PMID 9827326 DOI: 10.1007/S007920050082 |
0.384 |
|
| 1998 |
Darimont B, Stehlin C, Szadkowski H, Kirschner K. Mutational analysis of the active site of indoleglycerol phosphate synthase from Escherichia coli. Protein Science : a Publication of the Protein Society. 7: 1221-32. PMID 9605328 DOI: 10.1002/Pro.5560070518 |
0.454 |
|
| 1997 |
Hennig M, Sterner R, Kirschner K, Jansonius JN. Crystal structure at 2.0 A resolution of phosphoribosyl anthranilate isomerase from the hyperthermophile Thermotoga maritima: possible determinants of protein stability. Biochemistry. 36: 6009-16. PMID 9166771 DOI: 10.1021/Bi962718Q |
0.462 |
|
| 1997 |
Stehlin C, Dahm A, Kirschner K. Deletion mutagenesis as a test of evolutionary relatedness of indoleglycerol phosphate synthase with other TIM barrel enzymes. Febs Letters. 403: 268-72. PMID 9091315 DOI: 10.1016/S0014-5793(97)00066-5 |
0.502 |
|
| 1997 |
Sterner R, Kleemann GR, Szadkowski H, Lustig A, Hennig M, Kirschner K. Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer. Protein Science : a Publication of the Protein Society. 5: 2000-8. PMID 8897600 DOI: 10.1002/Pro.5560051006 |
0.408 |
|
| 1996 |
Knöchel TR, Hennig M, Merz A, Darimont B, Kirschner K, Jansonius JN. The crystal structure of indole-3-glycerol phosphate synthase from the hyperthermophilic archaeon Sulfolobus solfataricus in three different crystal forms: effects of ionic strength. Journal of Molecular Biology. 262: 502-15. PMID 8893859 DOI: 10.1006/Jmbi.1996.0531 |
0.348 |
|
| 1996 |
Niermann T, Kirschner K. The predicted secondary structure of the G-type glutamine amidotransferase is compatible with TIM-barrel topology. Protein Engineering. 8: 535-42. PMID 8532677 DOI: 10.1093/Protein/8.6.535 |
0.421 |
|
| 1995 |
Hennig M, Darimont B, Sterner R, Kirschner K, Jansonius JN. 2.0 A structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability. Structure (London, England : 1993). 3: 1295-306. PMID 8747456 DOI: 10.1016/S0969-2126(01)00267-2 |
0.486 |
|
| 1995 |
Hommel U, Eberhard M, Kirschner K. Phosphoribosyl anthranilate isomerase catalyzes a reversible amadori reaction. Biochemistry. 34: 5429-39. PMID 7727401 DOI: 10.1021/Bi00016A014 |
0.441 |
|
| 1995 |
Eberhard M, Tsai-Pflugfelder M, Bolewska K, Hommel U, Kirschner K. Indoleglycerol phosphate synthase-phosphoribosyl anthranilate isomerase: comparison of the bifunctional enzyme from Escherichia coli with engineered monofunctional domains. Biochemistry. 34: 5419-28. PMID 7727400 DOI: 10.1021/Bi00016A013 |
0.496 |
|
| 1995 |
Sterner R, Dahm A, Darimont B, Ivens A, Liebl W, Kirschner K. (Beta alpha)8-barrel proteins of tryptophan biosynthesis in the hyperthermophile Thermotoga maritima. The Embo Journal. 14: 4395-4402. DOI: 10.1002/J.1460-2075.1995.Tb00118.X |
0.421 |
|
| 1994 |
Jecht M, Tomschy A, Kirschner K, Jaenicke R. Autonomous folding of the excised coenzyme-binding domain of D-glyceraldehyde 3-phosphate dehydrogenase from Thermotoga maritima. Protein Science : a Publication of the Protein Society. 3: 411-8. PMID 8019412 DOI: 10.1002/Pro.5560030305 |
0.459 |
|
| 1993 |
Urfer R, Kirschner K. The importance of surface loops for stabilizing an eightfold beta alpha barrel protein. Protein Science : a Publication of the Protein Society. 1: 31-45. PMID 1304881 DOI: 10.1002/Pro.5560010105 |
0.428 |
|
| 1992 |
Niermann T, Kirschner K. Use of homologous sequences to improve protein secondary structure prediction. Methods in Enzymology. 202: 45-59. PMID 1784184 DOI: 10.1016/0076-6879(91)02006-U |
0.338 |
|
| 1992 |
Buchwalder A, Szadkowski H, Kirschner K. A fully active variant of dihydrofolate reductase with a circularly permuted sequence. Biochemistry. 31: 1621-30. PMID 1737018 DOI: 10.1021/Bi00121A006 |
0.437 |
|
| 1992 |
Leistler B, Herold M, Kirschner K. Collapsed intermediates in the reconstitution of dimeric aspartate aminotransferase from Escherichia coli European Journal of Biochemistry. 205: 603-611. PMID 1572361 DOI: 10.1111/J.1432-1033.1992.Tb16818.X |
0.383 |
|
| 1992 |
Eder J, Kirschner K. Stable substructures of eightfold βα-barrel proteins: Fragment complementation of phosphoribosylanthranilate isomerase Biochemistry. 31: 3617-3625. PMID 1567820 DOI: 10.1021/Bi00129A010 |
0.381 |
|
| 1991 |
Herold M, Leistler B, Hage A, Luger K, Kirschner K. Autonomous folding and coenzyme binding of the excised pyridoxal 5′-phosphate binding domain of aspartate aminotransferase from Escherichia coli Biochemistry. 30: 3612-3620. PMID 2015218 DOI: 10.1021/Bi00229A004 |
0.61 |
|
| 1991 |
Lane AN, Kirschner K. Mechanism of the physiological reaction catalyzed by tryptophan synthase from Escherichia coli. Biochemistry. 30: 479-84. PMID 1899028 DOI: 10.1021/Bi00216A025 |
0.43 |
|
| 1991 |
Kirschner K, Lane AN, Strasser AW. Reciprocal communication between the lyase and synthase active sites of the tryptophan synthase bienzyme complex. Biochemistry. 30: 472-8. PMID 1899027 DOI: 10.1021/Bi00216A024 |
0.423 |
|
| 1991 |
Wilmanns M, Hyde CC, Davies DR, Kirschner K, Jansonius JN. Structural conservation in parallel beta/alpha-barrel enzymes that catalyze three sequential reactions in the pathway of tryptophan biosynthesis. Biochemistry. 30: 9161-9. PMID 1892826 DOI: 10.1021/Bi00102A006 |
0.502 |
|
| 1991 |
Niermann T, Kirschner K. Improving the prediction of secondary structure of 'TIM-barrel' enzymes. Protein Engineering. 4: 359-70. PMID 1857718 DOI: 10.1093/Protein/4.3.359 |
0.422 |
|
| 1990 |
Ibel K, May RP, Kirschner K, Szadkowski H, Mascher E, Lundahl P. Protein-decorated micelle structure of sodium-dodecyl-sulfate--protein complexes as determined by neutron scattering. European Journal of Biochemistry. 190: 311-8. PMID 2194800 DOI: 10.1111/J.1432-1033.1990.Tb15578.X |
0.372 |
|
| 1990 |
Luger K, Szadkowski H, Kirschner K. An 8-fold βα barrel protein with redundant folding possibilities Protein Engineering, Design and Selection. 3: 249-258. PMID 2188262 DOI: 10.1093/Protein/3.4.249 |
0.593 |
|
| 1989 |
Jäger J, Köhler E, Tucker P, Sauder U, Housley-Markovic Z, Fotheringham I, Edwards M, Hunter M, Kirschner K, Jansonius JN. Crystallization and preliminary X-ray studies of an aspartate aminotransferase mutant from Escherichia coli. Journal of Molecular Biology. 209: 499-501. PMID 2685322 DOI: 10.1016/0022-2836(89)90014-4 |
0.304 |
|
| 1989 |
Hommel U, Lustig A, Kirschner K. Purification and characterization of yeast anthranilate phosphoribosyltransferase. European Journal of Biochemistry. 180: 33-40. PMID 2651124 DOI: 10.1111/J.1432-1033.1989.Tb14611.X |
0.444 |
|
| 1989 |
Luger K, Hommel U, Herold M, Hofsteenge J, Kirschner K. Correct folding of circularly permuted variants of a βα barrel enzyme in vivo Science. 243: 206-210. PMID 2643160 DOI: 10.1126/Science.2643160 |
0.631 |
|
| 1989 |
Eberhard M, Kirschner K. Modification of a catalytically important residue of indoleglycerol-phosphate synthase from Escherichia coli. Febs Letters. 245: 219-22. PMID 2494074 DOI: 10.1016/0014-5793(89)80225-X |
0.382 |
|
| 1988 |
Crawford IP, Niermann T, Kirschner K. Prediction of secondary structure by evolutionary comparison: application to the alpha subunit of tryptophan synthase. Proteins. 2: 118-29. PMID 3328860 DOI: 10.1002/Prot.340020206 |
0.414 |
|
| 1987 |
Priestle JP, Grütter MG, White JL, Vincent MG, Kania M, Wilson E, Jardetzky TS, Kirschner K, Jansonius JN. Three-dimensional structure of the bifunctional enzyme N-(5'-phosphoribosyl)anthranilate isomerase-indole-3-glycerol-phosphate synthase from Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 84: 5690-4. PMID 3303031 DOI: 10.1073/Pnas.84.16.5690 |
0.669 |
|
| 1987 |
Kirschner K, Szadkowski H, Jardetzky TS, Hager V. Phosphoribosylanthranilate isomerase-indoleglycerol-phosphate synthase from Escherichia coli. Methods in Enzymology. 142: 386-97. PMID 3298981 DOI: 10.1016/S0076-6879(87)42050-8 |
0.59 |
|
| 1986 |
Ahmed SA, Fairwell T, Dunn S, Kirschner K, Miles EW. Identification of three sites of proteolytic cleavage in the hinge region between the two domains of the beta 2 subunit of tryptophan synthase of Escherichia coli or Salmonella typhimurium. Biochemistry. 25: 3118-24. PMID 3524672 DOI: 10.1021/Bi00359A008 |
0.445 |
|
| 1985 |
Prantl F, Strasser A, Aebi M, Furter R, Niederberger P, Kirschner K, Huetter R. Purification and characterization of the indole-3-glycerolphosphate synthase/anthranilate synthase complex of Saccharomyces cerevisiae European Journal of Biochemistry. 146: 95-100. PMID 3881257 DOI: 10.1111/J.1432-1033.1985.Tb08624.X |
0.351 |
|
| 1985 |
Ibel K, May RP, Kirschner K, Lane AN, Szadkowski H, Dauvergne MT, Zulauf M. The domain structure of tryptophan synthase. A neutron scattering study. European Journal of Biochemistry. 151: 505-14. PMID 2992969 DOI: 10.1111/J.1432-1033.1985.Tb09131.X |
0.417 |
|
| 1984 |
Lane A, Paul C, Kirschner K. The mechanism of self-assembly of the multi-enzyme complex tryptophan synthase from Escherichia coli. The Embo Journal. 3: 279-287. DOI: 10.1002/J.1460-2075.1984.Tb01797.X |
0.409 |
|
| 1983 |
Wilhelm P, Pilz I, Lane AN, Kirschner K. Small-angle X-ray scattering studies of tryptophan synthase from Escherichia coli and its alpha and beta 2 subunits. European Journal of Biochemistry. 129: 51-6. PMID 6761119 DOI: 10.1111/J.1432-1033.1982.Tb07019.X |
0.363 |
|
| 1983 |
Lane AN, Kirschner K. The catalytic mechanism of tryptophan synthase from Escherichia coli. Kinetics of the reaction of indole with the enzyme--L-serine complexes. European Journal of Biochemistry. 129: 571-82. PMID 6402362 DOI: 10.1111/J.1432-1033.1983.Tb07087.X |
0.412 |
|
| 1983 |
Lane AN, Kirschner K. The mechanism of binding of L-serine to tryptophan synthase from Escherichia coli. European Journal of Biochemistry. 129: 561-70. PMID 6402361 DOI: 10.1111/J.1432-1033.1983.Tb07086.X |
0.403 |
|
| 1982 |
Lane AN, Kirschner K. The mechanism of tryptophan binding to tryptophan synthase from Escherichia coli. European Journal of Biochemistry. 120: 379-87. PMID 7032914 DOI: 10.1111/J.1432-1033.1981.Tb05715.X |
0.43 |
|
| 1981 |
Kirschner K, Szadkowski H, Henschen A, Lottspeich F. Limited proteolysis of N-(5'-phosphoribosyl)anthranilate isomerase: indoleglycerol phosphate synthase from Escherichia coli yields two different enzymically active, functional domains. Journal of Molecular Biology. 143: 395-409. PMID 7014916 DOI: 10.1016/0022-2836(80)90219-3 |
0.461 |
|
| 1980 |
Bartholmes P, Balk H, Kirschner K. Mechanism of reconstitution of the apo beta 2 subunit and the alpha 2 apo beta 2 complex of tryptophan synthase with pyridoxal 5'-Phosphate: kinetic studies. Biochemistry. 19: 4527-33. PMID 6996721 DOI: 10.1021/Bi00560A022 |
0.475 |
|
| 1980 |
Tschopp J, Kirschner K. Subunit interactions of tryptophan synthase from Escherichia coli as revealed by binding studies with pyridoxal phosphate analogues. Biochemistry. 19: 4514-21. PMID 6996720 DOI: 10.1021/Bi00560A020 |
0.467 |
|
| 1980 |
Tschopp J, Kirschner K. Kinetics of cooperative ligand binding to the apo beta 2 subunit of tryptophan synthase and its modulation by the alp ha subunit. Biochemistry. 19: 4521-7. PMID 6773563 DOI: 10.1021/Bi00560A021 |
0.417 |
|
| 1980 |
Dettwiler M, Kirschner K. Tryptophan synthase from Saccharomyces cerevisiae is a dimer of two polypeptide chains of Mr 76000 each. European Journal of Biochemistry. 102: 159-65. PMID 391562 DOI: 10.1111/J.1432-1033.1979.Tb06276.X |
0.351 |
|
| 1980 |
Cohn W, Kirschner K, Paul C. N-(5-Phosphoribosyl)anthranilate isomerase-indoleglycerol-phosphate synthase. 2. Fast-reaction studies show that a fluorescent substrate analogue binds independently to two different sites. Biochemistry. 18: 5953-9. PMID 391280 DOI: 10.1021/Bi00593A030 |
0.41 |
|
| 1980 |
Bisswanger H, Kirschner K, Cohn W, Hager V, Hansson E. N-(5-Phosphoribosyl)anthranilate isomerase-indoleglycerol-phosphate synthase. 1. A substrate analogue binds to two different binding sites on the bifunctional enzyme from Escherichia coli. Biochemistry. 18: 5946-53. PMID 391279 DOI: 10.1021/Bi00593A029 |
0.441 |
|
| 1979 |
Gschwind HP, Gschwind U, Paul CH, Kirschner K. Affinity chromatography of tryptophan synthase from Escherichia coli. Systematic studies with immobilized tryptophanol phosphate. European Journal of Biochemistry. 96: 403-16. PMID 378665 DOI: 10.1111/J.1432-1033.1979.Tb13052.X |
0.453 |
|
| 1976 |
Kirschner K, Wiskocil RL, Foehn M, Rezeau L. The tryptophan synthase from Escherichia coli. An improved purification procedure for the alpha-subunit and binding studies with substrate analogues. European Journal of Biochemistry. 60: 513-23. PMID 1107044 DOI: 10.1111/J.1432-1033.1975.Tb21030.X |
0.48 |
|
| 1976 |
Weischet WO, Kirschner K. Steady-state kinetic studies of the synthesis of indoleglycerol phosphate catalyzed by the alpha subunit of tryptophan synthase from Escherichia coli. Comparison with the alpha2 beta2-complex. European Journal of Biochemistry. 65: 375-85. PMID 949972 DOI: 10.1111/J.1432-1033.1976.Tb10351.X |
0.474 |
|
| 1976 |
Weischet WO, Kirschner K. The mechanism of the synthesis of indoleglycerol phosphate catalyzed by tryptophan synthase from Escherichia coli. Steady-state kinetic studies. European Journal of Biochemistry. 65: 365-73. PMID 949971 DOI: 10.1111/J.1432-1033.1976.Tb10350.X |
0.399 |
|
| 1976 |
Bartholmes P, Kirschner K, Gschwind HP. Cooperative and noncooperative binding of pyridoxal 5'-phosphate to tryptophan synthase from Escherichia coli. Biochemistry. 15: 4712-7. PMID 788781 DOI: 10.1021/bi00666a027 |
0.315 |
|
| 1976 |
Weischet WO, Kirschner K. The binding of indole to the alpha-subunit and beta2-subunit and to the alpha2beta2-complex of tryptophan synthase from Escherichia coli. Identification of a second indole-binding site on the alpha-subunit. European Journal of Biochemistry. 64: 313-20. PMID 776615 DOI: 10.1111/J.1432-1033.1976.Tb10303.X |
0.445 |
|
| 1972 |
von Ellenrieder G, Kirschner K, Schuster I. The binding of oxidized and reduced nicotinamide adenine-dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase. European Journal of Biochemistry. 26: 220-36. PMID 4339949 DOI: 10.1111/J.1432-1033.1972.Tb01760.X |
0.417 |
|
| 1971 |
Durchschlag H, Puchwein G, Kratky O, Schuster I, Kirschner K. X-ray small-angle scattering of yeast glyceraldehyde-3-phosphate dehydrogenase as a function of saturation with nicotinamide-adenine-dinucleotide. European Journal of Biochemistry / Febs. 19: 9-22. PMID 4323957 DOI: 10.1111/J.1432-1033.1971.Tb01282.X |
0.37 |
|
| 1966 |
Kirschner K, Eigen M, Bittman R, Voigt B. The binding of nicotinamide-adenine dinucleotide to yeast d-glyceraldehyde-3-phosphate dehydrogenase: temperature-jump relaxation studies on the mechanism of an allosteric enzyme. Proceedings of the National Academy of Sciences of the United States of America. 56: 1661-7. PMID 16591399 DOI: 10.1073/Pnas.56.6.1661 |
0.56 |
|
| 1961 |
Kirschner K, Henning U, Lynen F. Zur Biosynthese der Terpene, XIII. Die Hemmung der biologischen Squalensynthese durch 2‐Fluor‐mevalonsäure Justus Liebigs Annalen Der Chemie. 644: 48-64. DOI: 10.1002/jlac.19616440107 |
0.468 |
|
| 1961 |
Kirschner K, Lynen F. Zur Biosynthese der Terpene, XII. Die Synthese der DL‐5‐Phospho‐mevalonsäure Chemische Berichte. 94: 1595-1606. DOI: 10.1002/cber.19610940625 |
0.418 |
|
| Show low-probability matches. |
