| Year |
Citation |
Score |
| 2003 |
Tolan DR, Schuler B, Beernink PT, Jaenicke R. Thermodynamic analysis of the dissociation of the aldolase tetramer substituted at one or both of the subunit interfaces Biological Chemistry. 384: 1463-1471. PMID 14669989 DOI: 10.1515/Bc.2003.162 |
0.649 |
|
| 2003 |
Tiefenbach HJ, Durchschlag H, Schneider G, Jaenicke R. Thermodynamic analysis of serum albumin denaturation by sodium dodecyl sulfate Progress in Colloid and Polymer Science. 122: 130-140. DOI: 10.1007/3-540-36114-6_16 |
0.43 |
|
| 2002 |
Schuler B, Kremer W, Kalbitzer HR, Jaenicke R. Role of entropy in protein thermostability: Folding kinetics of a hyperthermophilic cold shock protein at high temperatures using 19F NMR Biochemistry. 41: 11670-11680. PMID 12269809 DOI: 10.1021/Bi026293L |
0.634 |
|
| 2001 |
Jaenicke R, Slingsby C. Lens crystallins and their microbial homologs: Structure, stability, and function Critical Reviews in Biochemistry and Molecular Biology. 36: 435-499. PMID 11724156 DOI: 10.1080/20014091074237 |
0.432 |
|
| 2001 |
Jaenicke R, Böhm G. Thermostability of proteins from Thermotoga maritima Methods in Enzymology. 334: 438-469. PMID 11398482 DOI: 10.1016/S0076-6879(01)34485-3 |
0.361 |
|
| 2001 |
Kremer W, Schuler B, Harrieder S, Geyer M, Gronwald W, Welker C, Jaenicke R, Kalbitzer HR. Solution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritima European Journal of Biochemistry. 268: 2527-2539. PMID 11322871 DOI: 10.1046/J.1432-1327.2001.02127.X |
0.608 |
|
| 2001 |
Dams T, Jaenicke R. Dihydrofolate reductase from Thermotoga maritima Methods in Enzymology. 331: 305-317. PMID 11265474 DOI: 10.1016/S0076-6879(01)31068-6 |
0.438 |
|
| 2001 |
Clout NJ, Kretschmar M, Jaenicke R, Slingsby C. Crystal structure of the calcium-loaded spherulin 3a dimer sheds light on the evolution of the eye lens βγ-crystallin domain fold Structure. 9: 115-124. PMID 11250196 DOI: 10.1016/S0969-2126(01)00573-1 |
0.309 |
|
| 2001 |
Durchschlag H, Tiefenbach KJ, Gebauer S, Jaenicke R. Spectroscopic investigations of detergents and protein-detergent complexes Journal of Molecular Structure. 563: 449-455. DOI: 10.1016/S0022-2860(00)00890-5 |
0.374 |
|
| 2000 |
Clout NJ, Basak A, Wieligmann K, Bateman OA, Jaenicke R, Slingsby C. The N-terminal domain of βB2-crystallin resembles the putative ancestral homodimer Journal of Molecular Biology. 304: 253-257. PMID 11090271 DOI: 10.1006/Jmbi.2000.4197 |
0.33 |
|
| 2000 |
Wenk M, Herbst R, Hoeger D, Kretschmar M, Lubsen NH, Jaenicke R. Gamma S-crystallin of bovine and human eye lens: Solution structure, stability and folding of the intact two-domain protein and its separate domains Biophysical Chemistry. 86: 95-108. PMID 11026675 DOI: 10.1016/S0301-4622(00)00161-7 |
0.384 |
|
| 2000 |
Berr K, Wassenberg D, Lilie H, Behlke J, Jaenicke R. ε-Crystallin from duck eye lens. Comparison of its quaternary structure and stability with other lactate dehydrogenases and complex formation with α-crystallin European Journal of Biochemistry. 267: 5413-5420. PMID 10951199 DOI: 10.1046/J.1432-1327.2000.01598.X |
0.42 |
|
| 2000 |
Jaenicke R. Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity? Proceedings of the National Academy of Sciences of the United States of America. 97: 2962-2964. PMID 10737776 DOI: 10.1073/Pnas.97.7.2962 |
0.426 |
|
| 2000 |
Dams T, Auerbach G, Bader G, Jacob U, Ploom T, Huber R, Jaenicke R. The crystal structure of dihydrofolate reductase from Thermotoga maritima: Molecular features of thermostability Journal of Molecular Biology. 297: 659-672. PMID 10731419 DOI: 10.1006/Jmbi.2000.3570 |
0.459 |
|
| 2000 |
Wassenberg D, Liebl W, Jaenicke R. Maltose-binding protein from the hyperthermophilic bacterium Thermotoga maritima: Stability and binding properties Journal of Molecular Biology. 295: 279-288. PMID 10623526 DOI: 10.1006/Jmbi.1999.3367 |
0.395 |
|
| 2000 |
Durchschlag H, Tiefenbach KJ, Weber R, Kuchenmüller B, Jaenicke R. Comparative investigations of the molecular properties of detergents and protein-detergent complexes Colloid and Polymer Science. 278: 312-320. DOI: 10.1007/S003960050519 |
0.383 |
|
| 1999 |
Maes D, Zeelen JP, Thanki N, Beaucamp N, Alvarez M, Thi MH, Backmann J, Martial JA, Wyns L, Jaenicke R, Wierenga RK. The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures. Proteins. 37: 441-53. PMID 10591103 DOI: 10.1002/(Sici)1097-0134(19991115)37:3<441::Aid-Prot11>3.0.Co;2-7 |
0.385 |
|
| 1999 |
Kretschmar M, Jaenicke R. Stability of a homo-dimeric Ca2+-binding member of the βγ-crystallin superfamily: DSC measurements on spherulin 3a from Physarum polycephalum Journal of Molecular Biology. 291: 1147-1153. PMID 10518950 DOI: 10.1006/Jmbi.1999.3037 |
0.366 |
|
| 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 |
0.559 |
|
| 1999 |
Wenk M, Jaenicke R. Calorimetric analysis of the Ca2+-binding βγ-crystallin homolog protein S from Myxococcus xanthus: Intrinsic stability and mutual stabilization of domains Journal of Molecular Biology. 293: 117-124. PMID 10512720 DOI: 10.1006/Jmbi.1999.3146 |
0.388 |
|
| 1999 |
Frankenberg N, Welker C, Jaenicke R. Does the elimination of ion pairs affect the thermal stability of cold shock protein from the hyperthermophilic bacterium Thermotoga maritima? Febs Letters. 454: 299-302. PMID 10431826 DOI: 10.1016/S0014-5793(99)00829-7 |
0.341 |
|
| 1999 |
Dams T, Jaenicke R. Stability and folding of dihydrofolate reductase from the hyperthermophilic bacterium Thermotoga maritima Biochemistry. 38: 9169-9178. PMID 10413491 DOI: 10.1021/Bi990635E |
0.44 |
|
| 1999 |
Kretschmar M, Mayr EM, Jaenicke R. Kinetic and thermodynamic stabilization of the betagamma-crystallin homolog spherulin 3a from Physarum polycephalum by calcium binding. Journal of Molecular Biology. 289: 701-5. PMID 10369756 DOI: 10.1006/Jmbi.1999.2833 |
0.331 |
|
| 1999 |
Wassenberg D, Welker C, Jaenicke R. Thermodynamics of the unfolding of the cold-shock protein from Thermotoga maritima Journal of Molecular Biology. 289: 187-193. PMID 10339416 DOI: 10.1006/Jmbi.1999.2772 |
0.398 |
|
| 1999 |
Zaiss K, Jaenicke R. Thermodynamic study of phosphoglycerate kinase from Thermotoga maritima and its isolated domains: Reversible thermal unfolding monitored by differential scanning calorimetry and circular dichroism spectroscopy Biochemistry. 38: 4633-4639. PMID 10194385 DOI: 10.1021/Bi982447E |
0.354 |
|
| 1999 |
Wenk M, Baumgartner R, Holak TA, Huber R, Jaenicke R, Mayr EM. The domains of protein S from Myxococcus xanthus: structure, stability and interactions. Journal of Molecular Biology. 286: 1533-45. PMID 10064714 DOI: 10.1006/Jmbi.1999.2582 |
0.385 |
|
| 1999 |
Kretschmar M, Mayr EM, Jaenicke R. Homo-dimeric spherulin 3a: a single-domain member of the beta gamma-crystallin superfamily. Biological Chemistry. 380: 89-94. PMID 10064142 DOI: 10.1515/Bc.1999.012 |
0.438 |
|
| 1999 |
Minuth T, Henn M, Rutkat K, Andrä S, Frey G, Rachel R, Stetter KO, Jaenicke R. The recombinant thermosome from the hyperthermophilic archaeon Methanopyrus kandleri: In vitro analysis of its chaperone activity Biological Chemistry. 380: 55-62. PMID 10064137 DOI: 10.1515/Bc.1999.007 |
0.431 |
|
| 1999 |
Welker C, Böhm G, Schurig H, Jaenicke R. Cloning, overexpression, purification, and physicochemical characterization of a cold shock protein homolog from the hyperthermophilic bacterium Thermotoga maritima Protein Science. 8: 394-403. PMID 10048332 DOI: 10.1110/Ps.8.2.394 |
0.347 |
|
| 1999 |
Wieligmann K, Mayr EM, Jaenicke R. Folding and self-assembly of the domains of betaB2-crystallin from rat eye lens. Journal of Molecular Biology. 286: 989-94. PMID 10047476 DOI: 10.1006/Jmbi.1999.2554 |
0.354 |
|
| 1999 |
Scheibel T, Siegmund HI, Jaenicke R, Ganz P, Lilie H, Buchner J. The charged region of Hsp90 modulates the function of the N-terminal domain. Proceedings of the National Academy of Sciences of the United States of America. 96: 1297-302. PMID 9990018 DOI: 10.1073/Pnas.96.4.1297 |
0.708 |
|
| 1998 |
Van De Klundert FAJM, Smulders RHPH, Gijsen MLJ, Lindner RA, Jaenicke R, Carver JA, De Jong WW. The mammalian small heat-shock protein Hsp20 forms dimers and is a poor chaperone European Journal of Biochemistry. 258: 1014-1021. PMID 9990320 DOI: 10.1046/J.1432-1327.1998.2581014.X |
0.351 |
|
| 1998 |
Jaenicke R, Böhm G. The stability of proteins in extreme environments Current Opinion in Structural Biology. 8: 738-748. PMID 9914256 DOI: 10.1016/S0959-440X(98)80094-8 |
0.356 |
|
| 1998 |
Minuth T, Frey G, Lindner P, Rachel R, Stetter KO, Jaenicke R. Recombinant homo- and hetero-oligomers of an ultrastable chaperonin from the archaeon Pyrodictium occultum show chaperone activity in vitro European Journal of Biochemistry. 258: 837-845. PMID 9874254 DOI: 10.1046/J.1432-1327.1998.2580837.X |
0.396 |
|
| 1998 |
Wenk M, Jaenicke R, Mayr EM. Kinetic stabilisation of a modular protein by domain interactions. Febs Letters. 438: 127-30. PMID 9821973 DOI: 10.1016/S0014-5793(98)01287-3 |
0.341 |
|
| 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 |
0.782 |
|
| 1998 |
Minuth T, Krämer B, Lehle K, Jaenicke R, Kohnert U. The spectroscopic analysis, inhibition and binding studies demonstrate the equivalence of Erythrina caffra trypsin inhibitor and the recombinant substitution variant recSerETI. Journal of Biotechnology. 62: 231-9. PMID 9729806 DOI: 10.1016/S0168-1656(98)00066-2 |
0.34 |
|
| 1998 |
Andrä S, Frey G, Jaenicke R, Stetter KO. The thermosome from Methanopyrus kandleri possesses an NH4+-dependent ATPase activity. European Journal of Biochemistry / Febs. 255: 93-9. PMID 9692906 DOI: 10.1046/J.1432-1327.1998.2550093.X |
0.399 |
|
| 1998 |
Wieligmann K, Norledge B, Jaenicke R, Mayr EM. Eye lens betaB2-crystallin: circular permutation does not influence the oligomerization state but enhances the conformational stability. Journal of Molecular Biology. 280: 721-9. PMID 9677299 DOI: 10.1006/Jmbi.1998.1887 |
0.419 |
|
| 1998 |
Grättinger M, Dankesreiter A, Schurig H, Jaenicke R. Recombinant phosphoglycerate kinase from the hyperthermophilic bacterium Thermotoga maritima: catalytic, spectral and thermodynamic properties. Journal of Molecular Biology. 280: 525-33. PMID 9665854 DOI: 10.1006/Jmbi.1998.1861 |
0.419 |
|
| 1998 |
Auerbach G, Ostendorp R, Prade L, Korndörfer I, Dams T, Huber R, Jaenicke R. Lactate dehydrogenase from the hyperthermophilic bacterium thermotoga maritima: the crystal structure at 2.1 A resolution reveals strategies for intrinsic protein stabilization. Structure (London, England : 1993). 6: 769-81. PMID 9655830 DOI: 10.1016/S0969-2126(98)00078-1 |
0.4 |
|
| 1998 |
Bayer P, Arndt A, Metzger S, Mahajan R, Melchior F, Jaenicke R, Becker J. Structure determination of the small ubiquitin-related modifier SUMO-1. Journal of Molecular Biology. 280: 275-86. PMID 9654451 DOI: 10.1006/Jmbi.1998.1839 |
0.406 |
|
| 1998 |
Palme S, Jaenicke R, Slingsby C. Unusual domain pairing in a mutant of bovine lens gammaB-crystallin. Journal of Molecular Biology. 279: 1053-9. PMID 9642083 DOI: 10.1006/Jmbi.1998.1850 |
0.327 |
|
| 1998 |
Jaenicke R. Protein self-organization in vitro and in vivo: partitioning between physical biochemistry and cell biology. Biological Chemistry. 379: 237-43. PMID 9563818 |
0.377 |
|
| 1998 |
Jaenicke R. What ultrastable globular proteins teach us about protein stabilization Biochemistry (Moscow). 63: 312-321. PMID 9526128 |
0.311 |
|
| 1998 |
Perl D, Welker C, Schindler T, Schröder K, Marahiel MA, Jaenicke R, Schmid FX. Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nature Structural Biology. 5: 229-35. PMID 9501917 DOI: 10.1038/Nsb0398-229 |
0.752 |
|
| 1997 |
Pappenberger G, Schurig H, Jaenicke R. Disruption of an ionic network leads to accelerated thermal denaturation of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima. Journal of Molecular Biology. 274: 676-83. PMID 9417944 DOI: 10.1006/Jmbi.1997.1421 |
0.399 |
|
| 1997 |
Auerbach G, Huber R, Grättinger M, Zaiss K, Schurig H, Jaenicke R, Jacob U. Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability. Structure (London, England : 1993). 5: 1475-83. PMID 9384563 DOI: 10.1016/S0969-2126(97)00297-9 |
0.381 |
|
| 1997 |
Jaenicke R, Seckler R. Protein misassembly in vitro. Advances in Protein Chemistry. 50: 1-59. PMID 9338078 DOI: 10.1016/S0065-3233(08)60318-6 |
0.673 |
|
| 1997 |
Beaucamp N, Hofmann A, Kellerer B, Jaenicke R. Dissection of the gene of the bifunctional PGK-TIM fusion protein from the hyperthermophilic bacterium Thermotoga maritima: design and characterization of the separate triosephosphate isomerase. Protein Science : a Publication of the Protein Society. 6: 2159-65. PMID 9336838 DOI: 10.1002/Pro.5560061010 |
0.474 |
|
| 1997 |
Rosinke B, Renner C, Mayr EM, Jaenicke R, Holak TA. Ca2+-loaded spherulin 3a from Physarum polycephalum adopts the prototype gamma-crystallin fold in aqueous solution. Journal of Molecular Biology. 271: 645-55. PMID 9281431 DOI: 10.1006/Jmbi.1997.1184 |
0.313 |
|
| 1997 |
Beaucamp N, Schurig H, Jaenicke R. The PGK-TIM fusion protein from Thermotoga maritima and its constituent parts are intrinsically stable and fold independently. Biological Chemistry. 378: 679-85. PMID 9278147 DOI: 10.1515/Bchm.1997.378.7.679 |
0.436 |
|
| 1997 |
Wassenberg D, Schurig H, Liebl W, Jaenicke R. Xylanase XynA from the hyperthermophilic bacterium Thermotoga maritima: structure and stability of the recombinant enzyme and its isolated cellulose-binding domain. Protein Science : a Publication of the Protein Society. 6: 1718-26. PMID 9260284 DOI: 10.1002/Pro.5560060812 |
0.443 |
|
| 1997 |
Norledge BV, Trinkl S, Jaenicke R, Slingsby C. The X-ray structure of a mutant eye lens beta B2-crystallin with truncated sequence extensions. Protein Science : a Publication of the Protein Society. 6: 1612-20. PMID 9260274 DOI: 10.1002/Pro.5560060802 |
0.341 |
|
| 1997 |
Schliebs W, Thanki N, Jaenicke R, Wierenga RK. A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability. Biochemistry. 36: 9655-62. PMID 9245397 DOI: 10.1021/Bi963086A |
0.391 |
|
| 1997 |
Palme S, Slingsby C, Jaenicke R. Mutational analysis of hydrophobic domain interactions in gamma B-crystallin from bovine eye lens. Protein Science : a Publication of the Protein Society. 6: 1529-36. PMID 9232654 DOI: 10.1002/Pro.5560060717 |
0.362 |
|
| 1997 |
Mayr EM, Jaenicke R, Glockshuber R. The domains in gammaB-crystallin: identical fold-different stabilities. Journal of Molecular Biology. 269: 260-9. PMID 9191069 DOI: 10.1006/Jmbi.1997.1033 |
0.356 |
|
| 1997 |
Thanki N, Zeelen JP, Mathieu M, Jaenicke R, Abagyan RA, Wierenga RK, Schliebs W. Protein engineering with monomeric triosephosphate isomerase (monoTIM): the modelling and structure verification of a seven-residue loop. Protein Engineering. 10: 159-67. PMID 9089815 DOI: 10.1093/Protein/10.2.159 |
0.371 |
|
| 1996 |
Lehle K, Kohnert U, Stern A, Popp F, Jaenicke R. Effect of disulfide bonds on the structure, function, and stability of the trypsin/tPA inhibitor from Erythrina caffra: site-directed mutagenesis, expression, and physiochemical characterization. Nature Biotechnology. 14: 476-80. PMID 9630923 DOI: 10.1038/Nbt0496-476 |
0.391 |
|
| 1996 |
Lisse T, Bartels D, Kalbitzer HR, Jaenicke R. The recombinant dehydrin-like desiccation stress protein from the resurrection plant Craterostigma plantagineum displays no defined three-dimensional structure in its native state. Biological Chemistry. 377: 555-61. PMID 9067253 DOI: 10.1515/Bchm3.1996.377.9.555 |
0.414 |
|
| 1996 |
Jaenicke R. How do proteins acquire their three-dimensional structure and stability? Die Naturwissenschaften. 83: 544-54. PMID 9008837 DOI: 10.1007/s001140050330 |
0.359 |
|
| 1996 |
Dams T, Ostendorp R, Ott M, Rutkat K, Jaenicke R. Tetrameric and octameric lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima. Structure and stability of the two active forms. European Journal of Biochemistry / Febs. 240: 274-9. PMID 8925837 DOI: 10.1111/J.1432-1033.1996.0274H.X |
0.455 |
|
| 1996 |
Jaenicke R, Schurig H, Beaucamp N, Ostendorp R. Structure and stability of hyperstable proteins: glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima. Advances in Protein Chemistry. 48: 181-269. PMID 8791626 DOI: 10.1016/S0065-3233(08)60363-0 |
0.421 |
|
| 1996 |
Ostendorp R, Auerbach G, Jaenicke R. Extremely thermostable L(+)-lactate dehydrogenase from Thermotoga maritima: cloning, characterization, and crystallization of the recombinant enzyme in its tetrameric and octameric state. Protein Science : a Publication of the Protein Society. 5: 862-73. PMID 8732758 DOI: 10.1002/Pro.5560050508 |
0.412 |
|
| 1996 |
Jaenicke R. Glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima: strategies of protein stabilization. Fems Microbiology Reviews. 18: 215-24. PMID 8639329 DOI: 10.1016/0168-6445(96)00013-7 |
0.309 |
|
| 1996 |
Norledge BV, Mayr EM, Glockshuber R, Bateman OA, Slingsby C, Jaenicke R, Driessen HP. The X-ray structures of two mutant crystallin domains shed light on the evolution of multi-domain proteins. Nature Structural Biology. 3: 267-74. PMID 8605629 DOI: 10.1038/Nsb0396-267 |
0.333 |
|
| 1996 |
Jaenicke R. Stability and folding of ultrastable proteins: eye lens crystallins and enzymes from thermophiles. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 10: 84-92. PMID 8566552 DOI: 10.1096/Fasebj.10.1.8566552 |
0.445 |
|
| 1995 |
Borchert TV, Kishan KV, Zeelen JP, Schliebs W, Thanki N, Abagyan R, Jaenicke R, Wierenga RK. Three new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, loop-4 and loop-8. Structure (London, England : 1993). 3: 669-79. PMID 8591044 DOI: 10.1016/S0969-2126(01)00202-7 |
0.383 |
|
| 1995 |
Korndörfer I, Steipe B, Huber R, Tomschy A, Jaenicke R. The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 A resolution. Journal of Molecular Biology. 246: 511-21. PMID 7877172 DOI: 10.1006/Jmbi.1994.0103 |
0.378 |
|
| 1995 |
Marx UC, Austermann S, Bayer P, Adermann K, Ejchart A, Sticht H, Walter S, Schmid FX, Jaenicke R, Forssmann WG. Structure of human parathyroid hormone 1-37 in solution. The Journal of Biological Chemistry. 270: 15194-202. PMID 7797503 DOI: 10.1074/jbc.270.25.15194 |
0.704 |
|
| 1995 |
Jaenicke R. Folding and association versus misfolding and aggregation of proteins. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 348: 97-105. PMID 7770492 DOI: 10.1098/rstb.1995.0050 |
0.373 |
|
| 1995 |
Schurig H, Rutkat K, Rachel R, Jaenicke R. Octameric enolase from the hyperthermophilic bacterium Thermotoga maritima: purification, characterization, and image processing. Protein Science : a Publication of the Protein Society. 4: 228-36. PMID 7757011 DOI: 10.1002/Pro.5560040209 |
0.399 |
|
| 1995 |
Lilie H, Jaenicke R, Buchner J. Characterization of a quaternary-structured folding intermediate of an antibody Fab-fragment. Protein Science : a Publication of the Protein Society. 4: 917-24. PMID 7663347 DOI: 10.1002/Pro.5560040511 |
0.59 |
|
| 1995 |
Borchert TV, Zeelen JP, Schliebs W, Callens M, Minke W, Jaenicke R, Wierenga RK. An interface point-mutation variant of triosephosphate isomerase is compactly folded and monomeric at low protein concentrations. Febs Letters. 367: 315-8. PMID 7607330 DOI: 10.1016/0014-5793(95)00586-X |
0.416 |
|
| 1995 |
Komar AA, Jaenicke R. Kinetics of translation of gamma B crystallin and its circularly permutated variant in an in vitro cell-free system: possible relations to codon distribution and protein folding. Febs Letters. 376: 195-8. PMID 7498540 DOI: 10.1016/0014-5793(95)01275-0 |
0.356 |
|
| 1995 |
Jaenicke R. The protein folding problem and tertiary structure prediction Febs Letters. 361: 129-130. DOI: 10.1016/0014-5793(99)90003-0 |
0.329 |
|
| 1994 |
Gross M, Jaenicke R. Proteins under pressure. The influence of high hydrostatic pressure on structure, function and assembly of proteins and protein complexes. European Journal of Biochemistry / Febs. 221: 617-30. PMID 8174542 DOI: 10.1111/J.1432-1033.1994.Tb18774.X |
0.346 |
|
| 1994 |
Bohm G, Jaenicke R. A structure-based model for the halophilic adaptation of dihydrofolate reductase from Halobacterium volcanii Protein Engineering. 7: 213-220. PMID 8170925 DOI: 10.1093/Protein/7.2.213 |
0.359 |
|
| 1994 |
Borchert TV, Abagyan R, Jaenicke R, Wierenga RK. Design, creation, and characterization of a stable, monomeric triosephosphate isomerase. Proceedings of the National Academy of Sciences of the United States of America. 91: 1515-8. PMID 8108439 DOI: 10.1073/Pnas.91.4.1515 |
0.441 |
|
| 1994 |
Grziwa A, Maack S, Pühler G, Wiegand G, Baumeister W, Jaenicke R. Dissociation and reconstitution of the Thermoplasma proteasome. European Journal of Biochemistry / Febs. 223: 1061-7. PMID 8055945 DOI: 10.1111/J.1432-1033.1994.Tb19084.X |
0.39 |
|
| 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 |
0.424 |
|
| 1994 |
Schmidt M, Rutkat K, Rachel R, Pfeifer G, Jaenicke R, Viitanen P, Lorimer G, Buchner J. Symmetric complexes of GroE chaperonins as part of the functional cycle. Science (New York, N.Y.). 265: 656-9. PMID 7913554 DOI: 10.1126/Science.7913554 |
0.57 |
|
| 1994 |
Bohm G, Jaenicke R. Relevance of sequence statistics for the properties of extremophilic proteins International Journal of Peptide and Protein Research. 43: 97-106. PMID 7908011 DOI: 10.1111/J.1399-3011.1994.Tb00380.X |
0.381 |
|
| 1994 |
Zarina S, Slingsby C, Jaenicke R, Zaidi ZH, Driessen H, Srinivasan N. Three-dimensional model and quaternary structure of the human eye lens protein gamma S-crystallin based on beta- and gamma-crystallin X-ray coordinates and ultracentrifugation. Protein Science : a Publication of the Protein Society. 3: 1840-6. PMID 7849599 DOI: 10.1002/Pro.5560031023 |
0.324 |
|
| 1994 |
Tomschy A, Böhm G, Jaenicke R. The effect of ion pairs on the thermal stability of D-glyceraldehyde 3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima. Protein Engineering. 7: 1471-8. PMID 7716158 DOI: 10.1093/Protein/7.12.1471 |
0.365 |
|
| 1993 |
Tomschy A, Glockshuber R, Jaenicke R. Functional expression of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima in Escherichia coli. Authenticity and kinetic properties of the recombinant enzyme. European Journal of Biochemistry. 214: 43-50. PMID 8508805 DOI: 10.1111/J.1432-1033.1993.Tb17894.X |
0.389 |
|
| 1993 |
Schumann J, Jaenicke R. Creatinase in its collapsed A state shows properties of a molten globule with dimeric quaternary structure European Journal of Biochemistry. 213: 1225-1233. PMID 8504814 DOI: 10.1111/J.1432-1033.1993.Tb17873.X |
0.485 |
|
| 1993 |
Gross M, Auerbach G, Jaenicke R. The catalytic activities of monomeric enzymes show complex pressure dependence. Febs Letters. 321: 256-60. PMID 8477859 DOI: 10.1016/0014-5793(93)80120-J |
0.348 |
|
| 1993 |
Rehaber V, Jaenicke R. The low-temperature folding intermediate of hyperthermophilic D-glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima shows a native-like cooperative unfolding transition. Febs Letters. 317: 163-6. PMID 8428625 DOI: 10.1016/0014-5793(93)81514-Z |
0.442 |
|
| 1993 |
Gross M, Lehle K, Jaenicke R, Nierhaus KH. Pressure-induced dissociation of ribosomes and elongation cycle intermediates. Stabilizing conditions and identification of the most sensitive functional state European Journal of Biochemistry. 218: 463-468. PMID 8269935 DOI: 10.1111/J.1432-1033.1993.Tb18397.X |
0.325 |
|
| 1993 |
Kern G, Kern D, Jaenicke R, Seckler R. Kinetics of folding and association of differently glycosylated variants of invertase from Saccharomyces cerevisiae Protein Science. 2: 1862-1868. PMID 8268797 DOI: 10.1002/Pro.5560021108 |
0.727 |
|
| 1993 |
Hilbert M, Bohm G, Jaenicke R. Structural relationships of homologous proteins as a fundamental principle in homology modeling Proteins: Structure, Function and Genetics. 17: 138-151. PMID 8265562 DOI: 10.1002/Prot.340170204 |
0.343 |
|
| 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 |
0.57 |
|
| 1993 |
Reng W, Riessland R, Scheibe R, Jaenicke R. Cloning, site-specific mutagenesis, expression and characterization of full-length chloroplast NADP-malate dehydrogenase from Pisum sativum European Journal of Biochemistry. 217: 189-197. PMID 8223554 DOI: 10.1111/J.1432-1033.1993.Tb18233.X |
0.427 |
|
| 1993 |
Schumann J, Möllering H, Jaenicke R. Intrinsic stability and extrinsic stabilization of creatinase from Pseudomonas putida. Biological Chemistry Hoppe-Seyler. 374: 427-34. PMID 8216893 DOI: 10.1515/Bchm3.1993.374.7-12.427 |
0.391 |
|
| 1993 |
Eppendorfer S, Konig S, Golbik R, Neef H, Lehle K, Jaenicke R, Schellenberger A, Hubner G. Effects of metal ions, thiamine diphosphate analogues and subunit interactions on the reconstitution behaviour of pyruvate decarboxylase from brewer's yeast Biological Chemistry Hoppe-Seyler. 374: 1129-1134. PMID 8129859 DOI: 10.1515/Bchm3.1993.374.7-12.1129 |
0.349 |
|
| 1993 |
Jaenicke R. What does protein refolding in vitro tell us about protein folding in the cell? Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 339: 287-94; discussion 2. PMID 8098533 DOI: 10.1098/RSTB.1993.0027 |
0.359 |
|
| 1993 |
Böhm G, Jaenicke R. Correlation functions as a tool for protein modeling and structure analysis. Protein Science : a Publication of the Protein Society. 1: 1269-78. PMID 1303745 DOI: 10.1002/Pro.5560011005 |
0.372 |
|
| 1993 |
OSTENDORP R, LIEBL W, SCHURIG H, JAENICKE R. The l-lactate dehydrogenase gene of the hyperthermophilic bacterium Thermotoga maritima cloned by complementation in Escherichia coli European Journal of Biochemistry. 216: 709-715. DOI: 10.1111/J.1432-1033.1993.Tb18190.X |
0.324 |
|
| 1993 |
Jaenicke R. Role of accessory proteins in protein folding Current Opinion in Structural Biology. 3: 104-112. DOI: 10.1016/0959-440X(93)90209-4 |
0.472 |
|
| 1992 |
Rehaber P, Seckler R, Jaenicke R. Intermolecular interactions involved in the association of the variant surface glycoprotein of Trypanosoma brucei. Biological Chemistry Hoppe-Seyler. 372: 593-8. PMID 1958317 DOI: 10.1515/Bchm3.1991.372.2.593 |
0.655 |
|
| 1992 |
Jaenicke R. Protein stability and molecular adaptation to extreme conditions. European Journal of Biochemistry. 202: 715-28. PMID 1765088 DOI: 10.1111/J.1432-1033.1991.Tb16426.X |
0.432 |
|
| 1992 |
Seckler R, Jaenicke R. Protein folding and protein refolding. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 6: 2545-52. PMID 1592207 DOI: 10.1096/Fasebj.6.8.1592207 |
0.717 |
|
| 1992 |
Kern G, Schmidt M, Buchner J, Jaenicke R. Glycosylation inhibits the interaction of invertase with the chaperone GroEL. Febs Letters. 305: 203-5. PMID 1363729 DOI: 10.1016/0014-5793(92)80667-6 |
0.583 |
|
| 1992 |
Van Der Vies SM, Viitanen PV, Gatenby AA, Lorimer GH, Jaenicke R. Conformational states of ribulosebisphosphate carboxylase and their interaction with chaperonin 60 Biochemistry®. 31: 3635-3644. PMID 1348956 DOI: 10.1021/Bi00129A012 |
0.377 |
|
| 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 |
0.599 |
|
| 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 |
0.618 |
|
| 1992 |
Kern G, Schülke N, Schmid FX, Jaenicke R. Stability, quaternary structure, and folding of internal, external, and core-glycosylated invertase from yeast. Protein Science : a Publication of the Protein Society. 1: 120-31. PMID 1304875 DOI: 10.1002/Pro.5560010112 |
0.785 |
|
| 1992 |
Glockshuber R, Mayr E, Berr K, Trinkl S, Jaenicke R. Folding and stability of recombinant crystallins expressed in Escherichia coli Experimental Eye Research. 55: 165. DOI: 10.1016/0014-4835(92)90773-L |
0.32 |
|
| 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 |
0.58 |
|
| 1991 |
Kaufmann M, Schwarz T, Jaenicke R, Schnackerz KD, Meyer HE, Bartholmes P. Limited proteolysis of the beta 2-dimer of tryptophan synthase yields an enzymatically active derivative that binds alpha-subunits. Biochemistry. 30: 4173-9. PMID 2021608 DOI: 10.1021/Bi00231A010 |
0.335 |
|
| 1991 |
Jaenicke R. Protein folding: local structures, domains, subunits, and assemblies. Biochemistry. 30: 3147-61. PMID 2009257 DOI: 10.1021/Bi00227A001 |
0.372 |
|
| 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 |
0.634 |
|
| 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 |
0.696 |
|
| 1991 |
Schumann J, Wrba A, Jaenicke R, Stetter KO. Topographical and enzymatic characterization of amylases from the extremely thermophilic eubacterium Thermotoga maritima. Febs Letters. 282: 122-6. PMID 1709115 DOI: 10.1016/0014-5793(91)80459-G |
0.381 |
|
| 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 |
0.79 |
|
| 1991 |
Schultes V, Jaenicke R. Folding intermediates of hyperthermophilic D-glyceraldehyde-3-phosphate dehydrogenase from Thermotoga maritima
are trapped at low temperature Febs Letters. 290: 235-238. DOI: 10.1016/0014-5793(91)81268-D |
0.387 |
|
| 1990 |
Jaenicke R, Muiznieks I, Aslanidis C, Schmitt R. Ultracentrifugal analysis of the quaternary structure of the raf repressor from Escherichia coli. Febs Letters. 260: 233-5. PMID 2404799 DOI: 10.1016/0014-5793(90)80111-U |
0.39 |
|
| 1990 |
Schultes V, Deutzmann R, Jaenicke R. Complete amino-acid sequence of glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima. European Journal of Biochemistry. 192: 25-31. PMID 2401296 DOI: 10.1111/J.1432-1033.1990.Tb19190.X |
0.304 |
|
| 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 |
0.615 |
|
| 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 |
0.599 |
|
| 1990 |
Wrba A, Jaenicke R, Huber R, Stetter KO. Lactate dehydrogenase from the extreme thermophile Thermotoga maritima. European Journal of Biochemistry. 188: 195-201. PMID 2318202 DOI: 10.1111/J.1432-1033.1990.Tb15388.X |
0.415 |
|
| 1990 |
Wrba A, Schweiger A, Schultes V, Jaenicke R, Závodszky P. Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima. Biochemistry. 29: 7584-92. PMID 2271518 DOI: 10.1021/BI00485A007 |
0.323 |
|
| 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 |
0.571 |
|
| 1990 |
Rehaber P, Staudacher N, Seckler R, Bülow R, Overath P, Jaenicke R. Stability and reconstitution of the soluble variant surface glycoprotein (sVSG) from Trypanosoma brucei. Biochemistry. 29: 8217-23. PMID 2252884 DOI: 10.1021/Bi00488A004 |
0.708 |
|
| 1990 |
Hecht K, Langer T, Wrba A, Jaenicke R. Lactate dehydrogenase from the extreme halophilic archaebacterium Halobacterium marismortui. Biological Chemistry Hoppe-Seyler. 371: 515-9. PMID 2117936 DOI: 10.1515/BCHM3.1990.371.1.515 |
0.319 |
|
| 1990 |
Rinas U, Risse B, Jaenicke R, Abel KJ, Zettlmeissl G. Denaturation-renaturation of the fibrin-stabilizing factor XIII a-chain isolated from human placenta. Properties of the native and reconstituted protein. Biological Chemistry Hoppe-Seyler. 371: 49-56. PMID 1969740 DOI: 10.1515/Bchm3.1990.371.1.49 |
0.475 |
|
| 1990 |
Rinas U, Risse B, Jaenicke R, Bröker M, Karges HE, Küpper HA, Zettlmeissl G. Characterization of recombinant factor XIIIa produced in Saccharomyces cerevisiae. Nature Biotechnology. 8: 543-546. PMID 1369439 DOI: 10.1038/Nbt0690-543 |
0.376 |
|
| 1989 |
Vita C, Fontana A, Jaenicke R. Folding of thermolysin fragments. Hydrodynamic properties of isolated domains and subdomains. Febs Journal. 183: 513-518. PMID 2776748 DOI: 10.1111/J.1432-1033.1989.Tb21079.X |
0.379 |
|
| 1989 |
Hecht K, Wrba A, Jaenicke R. Catalytic properties of thermophilic lactate dehydrogenase and halophilic malate dehydrogenase at high temperature and low water activity. European Journal of Biochemistry. 183: 69-74. PMID 2753046 DOI: 10.1111/J.1432-1033.1989.Tb14897.X |
0.393 |
|
| 1989 |
Hecht K, Jaenicke R. Malate dehydrogenase from the extreme halophilic archaebacterium Halobacterium marismortui. Reconstitution of the enzyme after denaturation and dissociation in various denaturants Biochemistry. 28: 4979-4985. DOI: 10.1021/Bi00438A012 |
0.388 |
|
| 1988 |
Gerl M, Jaenicke R, Smith JM, Harrison PM. Self-assembly of apoferritin from horse spleen after reversible chemical modification with 2,3-dimethylmaleic anhydride. Biochemistry. 27: 4089-96. PMID 3415975 DOI: 10.1021/Bi00411A027 |
0.411 |
|
| 1987 |
Jaenicke R, Nöth C. Structure-function relationship of mitochondrial malate dehydrogenase at high dilution and in multicomponent systems. Biological Chemistry Hoppe-Seyler. 368: 871-8. PMID 3620115 DOI: 10.1515/Bchm3.1987.368.2.871 |
0.466 |
|
| 1987 |
Gerl M, Jaenicke R. Assembly of apoferritin from horse spleen: comparison of the protein in its native and reassembled state. Biological Chemistry Hoppe-Seyler. 368: 387-96. PMID 3606823 DOI: 10.1515/Bchm3.1987.368.1.387 |
0.442 |
|
| 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 |
0.569 |
|
| 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 |
0.545 |
|
| 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 |
0.637 |
|
| 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 |
0.609 |
|
| 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 |
0.586 |
|
| 1986 |
HECHT K, WIELAND F, JAENICKE R. The Cell Surface Glycoprotein ofHalobacterium halobium.Physico-chemical Characterization in the Absence and Presence of Salt Biological Chemistry Hoppe-Seyler. 367: 33-38. DOI: 10.1515/Bchm3.1986.367.1.33 |
0.391 |
|
| 1985 |
Seifert T, Bartholmes P, Jaenicke R. Binding of the fluorescent dye 8-anilinonaphthalene 1-sulfonic acid to the native and pressure dissociated beta 2-dimer of tryptophan synthase from Escherichia coli. Zeitschrift Fur Naturforschung. Section C, Biosciences. 39: 1008-11. PMID 6393624 DOI: 10.1515/Znc-1984-9-1023 |
0.321 |
|
| 1985 |
Krebs H, Schmid FX, Jaenicke R. Native-like folding intermediates of homologous ribonucleases. Biochemistry. 24: 3846-52. PMID 4052370 DOI: 10.1021/Bi00336A005 |
0.757 |
|
| 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 |
Seifert T, Bartholmes P, Jaenicke R. Influence of cofactor pyridoxal 5'-phosphate on reversible high-pressure denaturation of isolated beta 2 dimer of tryptophan synthase bienzyme complex from Escherichia coli. Biochemistry. 24: 339-45. PMID 3884040 DOI: 10.1021/Bi00323A016 |
0.415 |
|
| 1985 |
Hermann R, Jaenicke R, Price NC. Evidence for active intermediates during the reconstitution of yeast phosphoglycerate mutase. Biochemistry. 24: 1817-1821. PMID 2990542 DOI: 10.1021/Bi00329A002 |
0.403 |
|
| 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 |
0.64 |
|
| 1984 |
Seifert T, Bartholmes P, Jaenicke R. High-pressure dissociation of the beta 2-dimer of tryptophan synthase from Escherichia coli monitored by sucrose gradient centrifugation. Febs Letters. 173: 381-4. PMID 6378669 DOI: 10.1016/0014-5793(84)80809-1 |
0.309 |
|
| 1983 |
Durchschlag H, Jaenicke R. Partial specific volume changes of proteins densimetric studies. Biochemical and Biophysical Research Communications. 108: 1074-9. PMID 7181881 DOI: 10.1016/0006-291X(82)92109-X |
0.395 |
|
| 1983 |
Müller K, Lüdemann HD, Jaenicke R. Thermodynamics and mechanism of high-pressure deactivation and dissociation of porcine lactic dehydrogenase. Biophysical Chemistry. 16: 1-7. PMID 7139038 DOI: 10.1016/0301-4622(82)85001-1 |
0.38 |
|
| 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 |
0.6 |
|
| 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 |
0.542 |
|
| 1983 |
Krebs H, Schmid FX, Jaenicke R. Folding of homologous proteins. The refolding of different ribonucleases is independent of sequence variations, proline content and glycosylation. Journal of Molecular Biology. 169: 619-35. PMID 6620387 DOI: 10.1016/S0022-2836(83)80067-9 |
0.763 |
|
| 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 |
0.607 |
|
| 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 |
0.582 |
|
| 1983 |
Durchschlag H, Jaenicke R. Partial specific volume changes of proteins: ultracentrifugal and viscometric studies International Journal of Biological Macromolecules. 5: 143-148. DOI: 10.1016/0141-8130(83)90028-4 |
0.348 |
|
| 1982 |
Müller K, Lüdemann HD, Jaenicke R. Pressure-induced structural changes of pig heart lactic dehydrogenase. Biophysical Chemistry. 14: 101-10. PMID 7326335 DOI: 10.1016/0301-4622(81)85011-9 |
0.368 |
|
| 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 |
0.558 |
|
| 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 |
0.612 |
|
| 1982 |
Seifert T, Bartholmes P, Jaenicke R. Reconstitution of the isolated β2-subunit of tryptophan synthase from Escherichia coli after dissociation induced by high hydrostatic pressure: Equilibrium and kinetic studies Biophysical Chemistry. 15: 1-8. PMID 7041998 DOI: 10.1016/0301-4622(82)87010-5 |
0.335 |
|
| 1982 |
Balk H, Frank A, Bartholmes P, Jaenicke R. Equilibrium and kinetic measurements of the binding of pyridoxal 5'-phosphate to hybrid tryptophan synthase from Escherichia coli. European Journal of Biochemistry. 121: 105-12. PMID 7035165 DOI: 10.1111/J.1432-1033.1981.Tb06437.X |
0.412 |
|
| 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 |
0.531 |
|
| 1982 |
Price NC, Jaenicke R. The quaternary structure of phosphoglycerate mutase from yeast: evidence against dissociation of the tetrameric enzyme at low concentrations. Febs Letters. 143: 283-286. PMID 6288465 DOI: 10.1016/0014-5793(82)80117-8 |
0.4 |
|
| 1982 |
Duckworth HW, Jaenicke R, Perham RN, Wilkie AO, Finch JT, Roberts GC. Limited proteolysis and proton NMR spectroscopy of Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex. European Journal of Biochemistry / Febs. 124: 63-9. PMID 6282590 DOI: 10.1111/J.1432-1033.1982.Tb05906.X |
0.385 |
|
| 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 |
0.599 |
|
| 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 |
0.608 |
|
| 1981 |
Sturtevant JM, Velicelebi G, Jaenicke R, Lauffer MA. Scanning calorimetric investigation of the polymerization of the coat protein of tobacco mosaic virus Biochemistry. 20: 3792-3800. PMID 7272276 DOI: 10.1021/bi00516a019 |
0.565 |
|
| 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 |
0.629 |
|
| 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 |
0.529 |
|
| 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 |
0.587 |
|
| 1981 |
Merkl I, Balk H, Bartholmes P, Jaenicke R. Interactions between Tryptophan Synthase from Escherichia coli and Derivatives of the Coenzyme Pyridoxal 5'-Phosphate Zeitschrift FüR Naturforschung C. 36: 778-783. DOI: 10.1515/Znc-1981-9-1014 |
0.333 |
|
| 1980 |
Niekamp CW, Hinz HJ, Jaenicke R, Woenckhaus C, Jeck R. Correlations between tertiary structure and energetics of coenzyme binding in pig heart muscle lactate dehydrogenase. Biochemistry. 19: 3144-52. PMID 7407036 DOI: 10.1021/Bi00555A005 |
0.35 |
|
| 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 |
0.614 |
|
| 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 |
0.488 |
|
| 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 |
0.628 |
|
| 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 |
0.62 |
|
| 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 |
0.603 |
|
| 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 |
0.617 |
|
| 1979 |
Schmid G, Lüdemann HD, Jaenicke R. Dissociation and aggregation of lactic dehydrogenase by high hydrostatic pressure. European Journal of Biochemistry. 97: 407-13. PMID 572770 DOI: 10.1111/J.1432-1033.1979.Tb13128.X |
0.403 |
|
| 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 |
0.512 |
|
| 1979 |
Bartholmes P, Böker H, Jaenicke R. Purification of tryptophan synthase from Saccharomyces cerevisiae and partial activity of its nicked subunits. Febs Journal. 102: 167-172. PMID 391563 DOI: 10.1111/J.1432-1033.1979.Tb06277.X |
0.402 |
|
| 1979 |
Groha C, Bartholmes P, Jaenicke R. Refolding and reactivation of Escherichia coli tryptophan synthase beta2 subunit after inactivation and dissociation in guanidine hydrochloride at acidic pH. European Journal of Biochemistry. 92: 437-41. PMID 33046 DOI: 10.1111/J.1432-1033.1978.Tb12764.X |
0.43 |
|
| 1979 |
Vogel D, Marcillac GDd, Hirth L, Gregori E, Jaenicke R. Size Distribution in the Higher Stages of Polymerization of the A-Protein of Tobacco Mosaic Virus (vulgare) Zeitschrift FüR Naturforschung C. 34: 782-792. DOI: 10.1515/Znc-1979-9-1021 |
0.383 |
|
| 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 |
0.518 |
|
| 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 |
0.569 |
|
| 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 |
0.584 |
|
| 1978 |
Bartholmes P, Jaenicke R. Reassociation and reactivation of yeast glyceraldehyde-3-phosphate dehydrogenase after dissociation in the presence of ATP. European Journal of Biochemistry. 87: 563-7. PMID 210016 DOI: 10.1111/J.1432-1033.1978.Tb12407.X |
0.42 |
|
| 1978 |
Hinz HJ, Steininger G, Schmid F, Jaenicke R. Studies on an energy structure-function relationship of dehydrogenases II. Calorimetric investigations on the interaction of coenzyme fragments with pig skeletal muscle lactate dehydrogenase Febs Letters. 87: 83-86. PMID 204523 DOI: 10.1016/0014-5793(78)80139-2 |
0.696 |
|
| 1978 |
Schmid F, Hinz HJ, Jaenicke R. Studies on an energy structure-function relationship of dehydrogenases. I. Calorimetric investigations on the interaction of coenzyme fragments with horse liver alcohol dehydrogenase. Febs Letters. 87: 80-2. PMID 204522 DOI: 10.1016/0014-5793(78)80138-0 |
0.716 |
|
| 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 |
0.609 |
|
| 1978 |
Hinz HJ, Schmidt R, Scheurmann W, Jaenicke R. Thermodynamic studies of binary and ternary complexes of pig-skeletal-muscle lactate dehydrogenase. European Journal of Biochemistry. 80: 543-50. PMID 200427 DOI: 10.1111/J.1432-1033.1977.Tb11910.X |
0.395 |
|
| 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 |
0.583 |
|
| 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 |
0.571 |
|
| 1978 |
SCHMID G, LUDEMANN H, JAENICKE R. Oxidation of Sulfhydryl Groups in Lactate Dehydrogenase under High Hydrostatic Pressure European Journal of Biochemistry. 86: 219-224. DOI: 10.1111/J.1432-1033.1978.Tb12302.X |
0.371 |
|
| 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 |
0.515 |
|
| 1977 |
Durchschlag H, Goldmann K, Wenzl S, Durchschlag G, Jaenicke R. Ultracentrifugal and spectroscopic investigations on malate synthase from baker's yeast. Febs Letters. 73: 247-50. PMID 320043 DOI: 10.1016/0014-5793(77)80991-5 |
0.406 |
|
| 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 |
0.496 |
|
| 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 |
0.616 |
|
| 1976 |
Schmid F, Hinz HJ, Jaenicke R. Thermodynamic studies of binary and ternary complexes of pig heart lactate dehydrogenase. Biochemistry. 15: 3052-9. PMID 182202 DOI: 10.1021/Bi00659A018 |
0.735 |
|
| 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 |
0.605 |
|
| 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 |
|
| 1976 |
Vogel D, Jaenicke R. Circular-dichroism and absorption spectroscopic studies on specific aromatic residues involved in the different modes of aggregation of tobacco-mosaic-virus protein. European Journal of Biochemistry. 61: 423-31. PMID 2466 DOI: 10.1111/J.1432-1033.1976.Tb10036.X |
0.411 |
|
| 1975 |
Schmid G, Lüdemann HD, Jaenicke R. High pressure effects on the activity of glycolytic enzymes. Biophysical Chemistry. 3: 90-8. PMID 1092383 DOI: 10.1016/0301-4622(75)80041-X |
0.346 |
|
| 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 |
0.512 |
|
| 1975 |
Hinz HJ, Jaenicke R. Thermodynamics of complex formation between nicotinamide adenine dinucleotide and pig skeletal muscle lactate dehydrogenase. Biochemistry. 14: 24-7. PMID 162832 DOI: 10.1021/Bi00672A005 |
0.361 |
|
| 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 |
0.578 |
|
| 1975 |
Bartholmes P, Jaenicke R. Molecular properties of yeast glyceraldehyde-3-phosphate dehydrogenase in the presence of ATP and KCl Biochemical and Biophysical Research Communications. 64: 485-492. DOI: 10.1016/0006-291X(75)90347-2 |
0.409 |
|
| 1974 |
Vogel D, Jaenicke R. Conformational changes and proton uptake in the reversible aggregation of tobacco-mosaic-virus protein. European Journal of Biochemistry. 41: 607-15. PMID 4817563 DOI: 10.1111/J.1432-1033.1974.Tb03303.X |
0.393 |
|
| 1974 |
Schmid G, Durchschlag H, Biedermann G, Eggerer H, Jaenicke R. Molecular structure of malate synthase and structural changes upon ligand binding to the enzyme Biochemical and Biophysical Research Communications. 58: 419-426. PMID 4601336 DOI: 10.1016/0006-291X(74)90381-7 |
0.391 |
|
| 1974 |
Hanke T, Bartmann P, Hennecke H, Kosakowski HM, Jaenicke R, Holler E, Böck A. l-Phenylalanyl-tRNA Synthetase of Escherichia coli K-10 Febs Journal. 43: 601-607. PMID 4598754 DOI: 10.1111/J.1432-1033.1974.Tb03447.X |
0.311 |
|
| 1974 |
Jaenicke R. Reassociation and reactivation of lactic dehydrogenase from the unfolded subunits. European Journal of Biochemistry. 46: 149-55. PMID 4369117 DOI: 10.1111/J.1432-1033.1974.Tb03607.X |
0.42 |
|
| 1973 |
Jaenicke R, Bartmann P. Dissociation-association properties of apoferritin in the milligram and microgram range. Biochemical and Biophysical Research Communications. 49: 884-90. PMID 4641711 DOI: 10.1016/0006-291X(72)90295-1 |
0.346 |
|
| 1973 |
Bartholmes P, Durchschlag H, Jaenicke R. Molecular Properties of Lactic Dehydrogenase under the Conditions of the Enzymatic Test Febs Journal. 39: 101-108. PMID 4358821 DOI: 10.1111/J.1432-1033.1973.Tb03108.X |
0.439 |
|
| 1973 |
Hinz H, Jaenicke R. Calorimetric investigation of binding of NADH to pig muscle lactate dehydrogenase Biochemical and Biophysical Research Communications. 54: 1432-1436. DOI: 10.1016/0006-291X(73)91146-7 |
0.333 |
|
| 1972 |
Jaenicke R, Koberstein R, Teuscher B. The enzymically active unit of lactic dehydrogenase. Molecular properties of lactic dehydrogenase at low-protein and high salt concentrations. European Journal of Biochemistry. 23: 150-9. PMID 4331375 DOI: 10.1111/J.1432-1033.1971.Tb01602.X |
0.446 |
|
| 1971 |
Jaenicke R. Volume changes in the isoelectric heat aggregation of serum albumin. European Journal of Biochemistry. 21: 110-5. PMID 5106031 DOI: 10.1111/J.1432-1033.1971.Tb01446.X |
0.346 |
|
| 1971 |
Jaenicke R, Koberstein R. High pressure dissociation of lactic dehydrogenase Febs Letters. 17: 351-354. DOI: 10.1016/0014-5793(71)80185-0 |
0.309 |
|
| 1969 |
Jaenicke R, Lauffer MA. Determination of hydration and partial specific volume of proteins with the spring balance Biochemistry. 8: 3077-3082. PMID 5817623 DOI: 10.1021/Bi00835A058 |
0.584 |
|
| 1969 |
Jaenicke R, Lauffer MA. Polymerization-depolymerization of tobacco mosaic virus protein. XII. Further studies on the role of water Biochemistry. 8: 3083-3092. PMID 5808352 DOI: 10.1021/Bi00835A059 |
0.549 |
|
| 1968 |
Jaenicke R, Schmid D, Knof S. Monodispersity and quaternary structure of glyceraldehyde 3-phosphate dehydrogenase. Biochemistry. 7: 919-26. PMID 5657857 DOI: 10.1021/Bi00843A006 |
0.34 |
|
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