| Year |
Citation |
Score |
| 2016 |
Buchner J, Eisenberg D, Schmid F. In memoriam - Rainer Jaenicke. Protein Science : a Publication of the Protein Society. PMID 27977893 DOI: 10.1002/Pro.3098 |
0.49 |
|
| 2016 |
Ries LK, Schmid FX, Schmidpeter PA. Incorporation of an Unnatural Amino Acid as a Domain-Specific Fluorescence Probe in a Two-Domain Protein. Biochemistry. 55: 6739-6742. PMID 27951650 DOI: 10.1021/Acs.Biochem.6B00898 |
0.402 |
|
| 2016 |
Jakob RP, Schmidpeter PA, Koch JR, Schmid FX, Maier T. Structural and Functional Characterization of a Novel Family of Cyclophilins, the AquaCyps. Plos One. 11: e0157070. PMID 27276069 DOI: 10.1371/Journal.Pone.0157070 |
0.425 |
|
| 2015 |
Schmidpeter PA, Ries LK, Theer T, Schmid FX. Long-Range Energetic Changes Triggered by a Proline Switch in the Signal Adapter Protein c-CrkII. Journal of Molecular Biology. PMID 26456136 DOI: 10.1016/J.Jmb.2015.09.028 |
0.385 |
|
| 2015 |
Schmidpeter PA, Schmid FX. Prolyl isomerization and its catalysis in protein folding and protein function. Journal of Molecular Biology. 427: 1609-31. PMID 25676311 DOI: 10.1016/J.Jmb.2015.01.023 |
0.503 |
|
| 2015 |
Schmidpeter PA, Koch JR, Schmid FX. Control of protein function by prolyl isomerization. Biochimica Et Biophysica Acta. 1850: 1973-82. PMID 25542300 DOI: 10.1016/J.Bbagen.2014.12.019 |
0.45 |
|
| 2015 |
Jakob RP, Koch JR, Burmann BM, Schmidpeter PA, Hunkeler M, Hiller S, Schmid FX, Maier T. Dimeric Structure of the Bacterial Extracellular Foldase PrsA. The Journal of Biological Chemistry. 290: 3278-92. PMID 25525259 DOI: 10.1074/Jbc.M114.622910 |
0.427 |
|
| 2015 |
Schmidpeter PA, Schmid FX. Prolyl isomerization as a molecular memory in the allosteric regulation of the signal adapter protein c-CrkII. The Journal of Biological Chemistry. 290: 3021-32. PMID 25488658 DOI: 10.1074/Jbc.M114.617308 |
0.38 |
|
| 2015 |
Schmid FX. How proteins knot their ties Journal of Molecular Biology. 427: 225-227. PMID 25451603 DOI: 10.1016/J.Jmb.2014.10.018 |
0.386 |
|
| 2015 |
Godin-Roulling A, Schmidpeter PA, Schmid FX, Feller G. Functional adaptations of the bacterial chaperone trigger factor to extreme environmental temperatures. Environmental Microbiology. 17: 2407-20. PMID 25389111 DOI: 10.1111/1462-2920.12707 |
0.426 |
|
| 2015 |
Schmidpeter PAM, Schmid FX. Prolyl Isomerization and Its Catalysis in Protein Folding and Protein Function Journal of Molecular Biology. DOI: 10.1016/j.jmb.2015.01.023 |
0.351 |
|
| 2014 |
Koch JR, Schmid FX. Mia40 combines thiol oxidase and disulfide isomerase activity to efficiently catalyze oxidative folding in mitochondria Journal of Molecular Biology. 426: 4087-4098. PMID 25451030 DOI: 10.1016/J.Jmb.2014.10.022 |
0.467 |
|
| 2014 |
Koch JR, Schmid FX. Mia40 is optimized for function in mitochondrial oxidative protein folding and import. Acs Chemical Biology. 9: 2049-57. PMID 24983157 DOI: 10.1021/Cb500408N |
0.458 |
|
| 2014 |
Schmidpeter PAM, Schmid FX. Molecular determinants of a regulatory prolyl isomerization in the signal adapter protein c-CrkII Acs Chemical Biology. 9: 1145-1152. PMID 24571054 DOI: 10.1021/Cb500001N |
0.389 |
|
| 2014 |
Hoffmann-Thoms S, Jakob RP, Schmid FX. Energetic communication between functional sites of the gene-3-protein during infection by phage fd Journal of Molecular Biology. 426: 1711-1722. PMID 24440124 DOI: 10.1016/J.Jmb.2014.01.002 |
0.405 |
|
| 2014 |
Koch JR, Schmid FX. Mia40 targets cysteines in a hydrophobic environment to direct oxidative protein folding in the mitochondria. Nature Communications. 5: 3041. PMID 24407114 DOI: 10.1038/Ncomms4041 |
0.452 |
|
| 2013 |
Geitner AJ, Varga E, Wehmer M, Schmid FX. Generation of a highly active folding enzyme by combining a parvulin-type prolyl isomerase from sura with an unrelated chaperone domain Journal of Molecular Biology. 425: 4089-4098. PMID 23871892 DOI: 10.1016/J.Jmb.2013.06.038 |
0.444 |
|
| 2013 |
Kovermann M, Schmid FX, Balbach J. Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD Biological Chemistry. 394: 965-975. PMID 23585180 DOI: 10.1515/Hsz-2013-0137 |
0.647 |
|
| 2013 |
Hoffmann-Thoms S, Weininger U, Eckert B, Jakob RP, Koch JR, Balbach J, Schmid FX. Initiation of phage infection by partial unfolding and prolyl isomerization Journal of Biological Chemistry. 288: 12979-12991. PMID 23486474 DOI: 10.1074/Jbc.M112.442525 |
0.663 |
|
| 2013 |
Zoldák G, Geitner AJ, Schmid FX. The prolyl isomerase SlyD is a highly efficient enzyme but decelerates the conformational folding of a client protein Journal of the American Chemical Society. 135: 4372-4379. PMID 23445547 DOI: 10.1021/Ja311775A |
0.509 |
|
| 2013 |
Li J, Zoldak G, Kriehuber T, Soroka J, Schmid FX, Richter K, Buchner J. Unique proline-rich domain regulates the chaperone function of AIPL1. Biochemistry. 52: 2089-96. PMID 23418749 DOI: 10.1021/Bi301648Q |
0.58 |
|
| 2012 |
Carstensen L, Sperl JM, Bocola M, List F, Schmid FX, Sterner R. Conservation of the folding mechanism between designed primordial (βα)8-barrel proteins and their modern descendant Journal of the American Chemical Society. 134: 12786-12791. PMID 22758610 DOI: 10.1021/Ja304951V |
0.51 |
|
| 2012 |
Jakob RP, Geitner AJ, Weininger U, Balbach J, Dobbek H, Schmid FX. Structural and energetic basis of infection by the filamentous bacteriophage IKe Molecular Microbiology. 84: 1124-1138. PMID 22591114 DOI: 10.1111/J.1365-2958.2012.08079.X |
0.604 |
|
| 2012 |
Geitner AJ, Schmid FX. Combination of the human prolyl isomerase FKBP12 with unrelated chaperone domains leads to chimeric folding enzymes with high activity Journal of Molecular Biology. 420: 335-349. PMID 22542528 DOI: 10.1016/J.Jmb.2012.04.018 |
0.457 |
|
| 2012 |
Hoffmann-Thoms S, Schmid FX. A kinetic approach to determining the conformational stability of a protein that dimerizes after folding Biochemistry. 51: 3948-3956. PMID 22509974 DOI: 10.1021/bi300154z |
0.337 |
|
| 2012 |
Carstensen L, Zoldák G, Schmid FX, Sterner R. Folding mechanism of an extremely thermostable (βα) 8-barrel enzyme: A high kinetic barrier protects the protein from denaturation Biochemistry. 51: 3420-3432. PMID 22455619 DOI: 10.1021/bi300189f |
0.405 |
|
| 2011 |
Schmidpeter PAM, Jahreis G, Geitner AJ, Schmid FX. Prolyl isomerases show low sequence specificity toward the residue following the proline Biochemistry. 50: 4796-4803. PMID 21510665 DOI: 10.1021/Bi200442Q |
0.463 |
|
| 2011 |
Lorenz SH, Schmid FX. Reprogramming the infection mechanism of a filamentous phage Molecular Microbiology. 80: 827-834. PMID 21392130 DOI: 10.1111/J.1365-2958.2011.07617.X |
0.337 |
|
| 2011 |
Zoldák G, Schmid FX. Cooperation of the prolyl isomerase and chaperone activities of the protein folding catalyst SlyD Journal of Molecular Biology. 406: 176-194. PMID 21147124 DOI: 10.1016/J.Jmb.2010.12.010 |
0.486 |
|
| 2011 |
Lorenz SH, Jakob RP, Weininger U, Balbach J, Dobbek H, Schmid FX. The filamentous phages fd and IF1 use different mechanisms to infect escherichia coli Journal of Molecular Biology. 405: 989-1003. PMID 21110981 DOI: 10.1016/J.Jmb.2010.11.030 |
0.586 |
|
| 2010 |
Buttstedt A, Winter R, Sackewitz M, Hause G, Schmid FX, Schwarz E. Influence of the stability of a fused protein and its distance to the amyloidogenic segment on fibril formation. Plos One. 5: e15436. PMID 21124848 DOI: 10.1371/journal.pone.0015436 |
0.365 |
|
| 2010 |
Jakob RP, Zierer BK, Weininger U, Hofmann SD, Lorenz SH, Balbach J, Dobbek H, Schmid FX. Elimination of a Cis-proline-containing loop and turn optimization stabilizes a protein and accelerates its folding Journal of Molecular Biology. 399: 331-346. PMID 20394751 DOI: 10.1016/J.Jmb.2010.04.007 |
0.679 |
|
| 2010 |
Vandenameele J, Lejeune A, Di Paolo A, Brans A, Frère JM, Schmid FX, Matagne A. Folding of class a β-lactamases is rate-limited by peptide bond isomerization and occurs via parallel pathways Biochemistry. 49: 4264-4275. PMID 20384356 DOI: 10.1021/Bi100369D |
0.454 |
|
| 2010 |
Weininger U, Jakob RP, Kovermann M, Balbach J, Schmid FX. The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity Protein Science. 19: 6-18. PMID 19866485 DOI: 10.1002/Pro.277 |
0.665 |
|
| 2009 |
Jakob RP, Zoldák G, Aumüller T, Schmid FX. Chaperone domains convert prolyl isomerases into generic catalysts of protein folding Proceedings of the National Academy of Sciences of the United States of America. 106: 20282-20287. PMID 19920179 DOI: 10.1073/Pnas.0909544106 |
0.538 |
|
| 2009 |
Zoldák G, Aumüller T, Lücke C, Hritz J, Oostenbrink C, Fischer G, Schmid FX. A library of fluorescent peptides for exploring the substrate specificities of prolyl isomerases Biochemistry. 48: 10423-10436. PMID 19785464 DOI: 10.1021/Bi9014242 |
0.536 |
|
| 2009 |
Weininger U, Jakob RP, Eckert B, Schweimer K, Schmid FX, Balbach J. A remote prolyl isomerization controls domain assembly via a hydrogen bonding network Proceedings of the National Academy of Sciences of the United States of America. 106: 12335-12340. PMID 19617535 DOI: 10.1073/Pnas.0902102106 |
0.65 |
|
| 2009 |
Thoms S, Max KE, Wunderlich M, Jacso T, Lilie H, Reif B, Heinemann U, Schmid FX. Dimer formation of a stabilized Gbeta1 variant: a structural and energetic analysis. Journal of Molecular Biology. 391: 918-32. PMID 19527728 DOI: 10.1016/J.Jmb.2009.06.031 |
0.415 |
|
| 2009 |
Weininger U, Haupt C, Schweimer K, Graubner W, Kovermann M, Brüser T, Scholz C, Schaarschmidt P, Zoldak G, Schmid FX, Balbach J. NMR Solution Structure of SlyD from Escherichia coli: Spatial Separation of Prolyl Isomerase and Chaperone Function Journal of Molecular Biology. 387: 295-305. PMID 19356587 DOI: 10.1016/J.Jmb.2009.01.034 |
0.645 |
|
| 2009 |
Jakob RP, Schmid FX. Molecular Determinants of a Native-State Prolyl Isomerization Journal of Molecular Biology. 387: 1017-1031. PMID 19232524 DOI: 10.1016/J.Jmb.2009.02.021 |
0.483 |
|
| 2009 |
Piontek C, Varón Silva D, Heinlein C, Pöhner C, Mezzato S, Ring P, Martin A, Schmid FX, Unverzagt C. Semisynthesis of a homogeneous glycoprotein enzyme: Ribonuclease C: Part 2 Angewandte Chemie - International Edition. 48: 1941-1945. PMID 19180621 DOI: 10.1002/Anie.200804735 |
0.326 |
|
| 2009 |
Piontek C, Ring P, Harjes O, Heinlein C, Mezzato S, Lombana N, Pöhner C, Püttner M, Varón Silva D, Martin A, Schmid FX, Unverzagt C. Semisynthesis of a homogeneous glycoprotein enzyme: Ribonuclease C: Part 1 Angewandte Chemie - International Edition. 48: 1936-1940. PMID 19173366 DOI: 10.1002/Anie.200804734 |
0.37 |
|
| 2009 |
Zoldák G, Carstensen L, Scholz C, Schmid FX. Consequences of Domain Insertion on the Stability and Folding Mechanism of a Protein Journal of Molecular Biology. 386: 1138-1152. PMID 19136015 DOI: 10.1016/J.Jmb.2008.12.052 |
0.414 |
|
| 2008 |
Merkens H, Kappl R, Jakob RP, Schmid FX, Fetzner S. Quercetinase QueD of Streptomyces sp. FLA, a monocupin dioxygenase with a preference for nickel and cobalt Biochemistry. 47: 12185-12196. PMID 18950192 DOI: 10.1021/Bi801398X |
0.307 |
|
| 2008 |
Kather I, Jakob RP, Dobbek H, Schmid FX. Increased Folding Stability of TEM-1 β-Lactamase by In Vitro Selection Journal of Molecular Biology. 383: 238-251. PMID 18706424 DOI: 10.1016/J.Jmb.2008.07.082 |
0.45 |
|
| 2008 |
Kather I, Jakob R, Dobbek H, Schmid FX. Changing the Determinants of Protein Stability from Covalent to Non-Covalent Interactions by In Vitro Evolution: A Structural and Energetic Analysis Journal of Molecular Biology. 381: 1040-1054. PMID 18621056 DOI: 10.1016/J.Jmb.2008.06.073 |
0.474 |
|
| 2008 |
Sackewitz M, Von Einem S, Hause G, Wunderlich M, Schmid FX, Schwarz E. A folded and functional protein domain in an amyloid-like fibril Protein Science. 17: 1044-1054. PMID 18424511 DOI: 10.1110/ps.073276308 |
0.352 |
|
| 2008 |
Scholz C, Thirault L, Schaarschmidt P, Zarnt T, Faatz E, Engel AM, Upmeier B, Bollhagen R, Eckert B, Schmid FX. Chaperone-aided in vitro renaturation of an engineered E1 envelope protein for detection of anti-rubella virus IgG antibodies Biochemistry. 47: 4276-4287. PMID 18330994 DOI: 10.1021/Bi702435V |
0.303 |
|
| 2008 |
Jakob RP, Schmid FX. Energetic Coupling Between Native-State Prolyl Isomerization and Conformational Protein Folding Journal of Molecular Biology. 377: 1560-1575. PMID 18325533 DOI: 10.1016/J.Jmb.2008.02.010 |
0.525 |
|
| 2008 |
Schmid F. Prolyl Isomerization in Protein Folding Protein Folding Handbook. 2: 916-945. DOI: 10.1002/9783527619498.ch25 |
0.396 |
|
| 2008 |
Schmid F. Spectroscopic Techniques to Study Protein Folding and Stability Protein Folding Handbook. 1: 22-44. DOI: 10.1002/9783527619498.ch2 |
0.312 |
|
| 2007 |
Wunderlich M, Max KE, Roske Y, Mueller U, Heinemann U, Schmid FX. Optimization of the gbeta1 domain by computational design and by in vitro evolution: structural and energetic basis of stabilization. Journal of Molecular Biology. 373: 775-84. PMID 17868696 DOI: 10.1016/J.Jmb.2007.08.004 |
0.401 |
|
| 2007 |
Eckert B, Schmid FX. A Conformational Unfolding Reaction Activates Phage fd for the Infection of Escherichia coli Journal of Molecular Biology. 373: 452-461. PMID 17822712 DOI: 10.1016/J.Jmb.2007.07.060 |
0.484 |
|
| 2007 |
Löw C, Weininger U, Zeeb M, Zhang W, Laue ED, Schmid FX, Balbach J. Folding Mechanism of an Ankyrin Repeat Protein: Scaffold and Active Site Formation of Human CDK Inhibitor p19INK4d Journal of Molecular Biology. 373: 219-231. PMID 17804013 DOI: 10.1016/J.Jmb.2007.07.063 |
0.685 |
|
| 2007 |
Max KE, Wunderlich M, Roske Y, Schmid FX, Heinemann U. Optimized variants of the cold shock protein from in vitro selection: structural basis of their high thermostability. Journal of Molecular Biology. 369: 1087-97. PMID 17481655 DOI: 10.1016/J.Jmb.2007.04.016 |
0.394 |
|
| 2007 |
Knappe TA, Eckert B, Schaarschmidt P, Scholz C, Schmid FX. Insertion of a Chaperone Domain Converts FKBP12 into a Powerful Catalyst of Protein Folding Journal of Molecular Biology. 368: 1458-1468. PMID 17397867 DOI: 10.1016/J.Jmb.2007.02.097 |
0.501 |
|
| 2006 |
Garcia-Mira MM, Schmid FX. Key Role of Coulombic Interactions for the Folding Transition State of the Cold Shock Protein Journal of Molecular Biology. 364: 458-468. PMID 17020767 DOI: 10.1016/J.Jmb.2006.08.071 |
0.462 |
|
| 2006 |
Wunderlich M, Schmid FX. In Vitro Evolution of a Hyperstable Gβ1 Variant Journal of Molecular Biology. 363: 545-557. PMID 16978647 DOI: 10.1016/J.Jmb.2006.08.034 |
0.376 |
|
| 2006 |
Magg C, Kubelka J, Holtermann G, Haas E, Schmid FX. Specificity of the Initial Collapse in the Folding of the Cold Shock Protein Journal of Molecular Biology. 360: 1067-1080. PMID 16815441 DOI: 10.1016/J.Jmb.2006.05.073 |
0.472 |
|
| 2006 |
Wunderlich M, Schmid FX. The correlation between protein stability and dipole moment: A critical test Protein Engineering, Design and Selection. 19: 355-358. PMID 16720692 DOI: 10.1093/Protein/Gzl019 |
0.365 |
|
| 2006 |
Scholz C, Eckert B, Hagn F, Schaarschmidt P, Balbach J, Schmid FX. SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities Biochemistry. 45: 20-33. PMID 16388577 DOI: 10.1021/Bi051922N |
0.699 |
|
| 2005 |
Kather I, Bippes CA, Schmid FX. A stable disulfide-free gene-3-protein of phage fd generated by in vitro evolution Journal of Molecular Biology. 354: 666-678. PMID 16259997 DOI: 10.1016/J.Jmb.2005.09.086 |
0.473 |
|
| 2005 |
Wunderlich M, Martin A, Staab CA, Schmid FX. Evolutionary protein stabilization in comparison with computational design Journal of Molecular Biology. 351: 1160-1168. PMID 16051264 DOI: 10.1016/J.Jmb.2005.06.059 |
0.36 |
|
| 2005 |
Eckert B, Martin A, Balbach J, Schmid FX. Prolyl isomerization as a molecular timer in phage infection Nature Structural and Molecular Biology. 12: 619-623. PMID 15937494 DOI: 10.1038/Nsmb946 |
0.623 |
|
| 2005 |
Wunderlich M, Martin A, Schmid FX. Stabilization of the cold shock protein CspB from Bacillus subtilis by evolutionary optimization of coulombic interactions Journal of Molecular Biology. 347: 1063-1076. PMID 15784264 DOI: 10.1016/J.Jmb.2005.02.014 |
0.387 |
|
| 2005 |
Scholz C, Schaarschmidt P, Engel AM, Andres H, Schmitt U, Faatz E, Balbach J, Schmid FX. Functional solubilization of aggregation-prone HIV envelope proteins by covalent fusion with chaperone modules Journal of Molecular Biology. 345: 1229-1241. PMID 15644217 DOI: 10.1016/J.Jmb.2004.10.091 |
0.569 |
|
| 2005 |
SCHMID FX. Proline Isomerization in Unfolded Ribonuclease A European Journal of Biochemistry. 128: 77-80. DOI: 10.1111/J.1432-1033.1982.Tb06935.X |
0.382 |
|
| 2004 |
Klouche M, Peri G, Knabbe C, Eckstein HH, Schmid FX, Schmitz G, Mantovani A. Modified atherogenic lipoproteins induce expression of pentraxin-3 by human vascular smooth muscle cells Atherosclerosis. 175: 221-228. PMID 15262177 DOI: 10.1016/J.Atherosclerosis.2004.03.020 |
0.304 |
|
| 2004 |
Sterner R, Schmid FX. De novo design of an enzyme Science. 304: 1916-1917. PMID 15218133 DOI: 10.1126/Science.1100482 |
0.326 |
|
| 2004 |
Garcia-Mira MM, Boehringer D, Schmid FX. The folding transition state of the cold shock protein is strongly polarized Journal of Molecular Biology. 339: 555-569. PMID 15147842 DOI: 10.1016/J.Jmb.2004.04.011 |
0.334 |
|
| 2004 |
Magg C, Schmid FX. Rapid Collapse Precedes the Fast Two-state Folding of the Cold Shock Protein Journal of Molecular Biology. 335: 1309-1323. PMID 14729346 DOI: 10.1016/J.Jmb.2003.11.050 |
0.494 |
|
| 2003 |
Martin A, Schmid FX. A proline switch controls folding and domain interactions in the gene-3-protein of the filamentous phage fd. Journal of Molecular Biology. 331: 1131-40. PMID 12927547 DOI: 10.1016/S0022-2836(03)00864-7 |
0.4 |
|
| 2003 |
Martin A, Schmid FX, Sieber V. Proside: a phage-based method for selecting thermostable proteins. Methods in Molecular Biology (Clifton, N.J.). 230: 57-70. PMID 12824569 DOI: 10.1385/1-59259-396-8:57 |
0.328 |
|
| 2003 |
Martin A, Schmid FX. The folding mechanism of a two-domain protein: folding kinetics and domain docking of the gene-3 protein of phage fd. Journal of Molecular Biology. 329: 599-610. PMID 12767837 DOI: 10.1016/S0022-2836(03)00433-9 |
0.404 |
|
| 2003 |
Martin A, Schmid FX. Evolutionary stabilization of the gene-3-protein of phage fd reveals the principles that govern the thermodynamic stability of two-domain proteins. Journal of Molecular Biology. 328: 863-75. PMID 12729760 DOI: 10.1016/S0022-2836(03)00359-0 |
0.412 |
|
| 2003 |
Maier R, Eckert B, Scholz C, Lilie H, Schmid FX. Interaction of trigger factor with the ribosome. Journal of Molecular Biology. 326: 585-92. PMID 12559924 DOI: 10.1016/S0022-2836(02)01427-4 |
0.316 |
|
| 2002 |
Perl D, Schmid FX. Some like it hot: the molecular determinants of protein thermostability. Chembiochem : a European Journal of Chemical Biology. 3: 39-44. PMID 17590951 DOI: 10.1002/1439-7633(20020104)3:1<39::Aid-Cbic39>3.0.Co;2-D |
0.391 |
|
| 2002 |
Martin A, Kather I, Schmid FX. Origins of the high stability of an in vitro-selected cold-shock protein. Journal of Molecular Biology. 318: 1341-9. PMID 12083522 DOI: 10.1016/S0022-2836(02)00243-7 |
0.396 |
|
| 2002 |
Jacob MH, Saudan C, Holtermann G, Martin A, Perl D, Merbach AE, Schmid FX. Water contributes actively to the rapid crossing of a protein unfolding barrier. Journal of Molecular Biology. 318: 837-45. PMID 12054827 DOI: 10.1016/S0022-2836(02)00165-1 |
0.446 |
|
| 2002 |
Dominy BN, Perl D, Schmid FX, Brooks CL. The effects of ionic strength on protein stability: the cold shock protein family. Journal of Molecular Biology. 319: 541-54. PMID 12051927 DOI: 10.1016/S0022-2836(02)00259-0 |
0.451 |
|
| 2002 |
Perl D, Jacob M, Bánó M, Stupák M, Antalík M, Schmid FX. Thermodynamics of a diffusional protein folding reaction. Biophysical Chemistry. 96: 173-90. PMID 12034439 DOI: 10.1016/S0301-4622(02)00024-8 |
0.465 |
|
| 2002 |
Schiene-Fischer C, Habazettl J, Schmid FX, Fischer G. The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase. Nature Structural Biology. 9: 419-24. PMID 12021775 DOI: 10.1038/Nsb804 |
0.592 |
|
| 2001 |
Delbrück H, Mueller U, Perl D, Schmid FX, Heinemann U. Crystal structures of mutant forms of the Bacillus caldolyticus cold shock protein differing in thermal stability. Journal of Molecular Biology. 313: 359-69. PMID 11800562 DOI: 10.1006/Jmbi.2001.5051 |
0.462 |
|
| 2001 |
Perl D, Schmid FX. Electrostatic Stabilization of a Thermophilic Cold Shock Protein Journal of Molecular Biology. 313: 343-357. PMID 11800561 DOI: 10.1006/Jmbi.2001.5050 |
0.447 |
|
| 2001 |
Perl D, Holtermann G, Schmid FX. Role of the chain termini for the folding transition state of the cold shock protein Biochemistry. 40: 15501-15511. PMID 11747425 DOI: 10.1021/Bi011378S |
0.503 |
|
| 2001 |
Maier R, Scholz C, Schmid FX. Dynamic association of trigger factor with protein substrates Journal of Molecular Biology. 314: 1181-1190. PMID 11743733 DOI: 10.1006/Jmbi.2000.5192 |
0.486 |
|
| 2001 |
Schindler I, Renz A, Schmid FX, Beck E. Activation of spinach pullulanase by reduction results in a decrease in the number of isomeric forms Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1548: 175-186. PMID 11513962 DOI: 10.1016/S0167-4838(01)00228-X |
0.396 |
|
| 2001 |
Martin A, Sieber V, Schmid FX. In-vitro selection of highly stabilized protein variants with optimized surface Journal of Molecular Biology. 309: 717-726. PMID 11397091 DOI: 10.1006/Jmbi.2001.4698 |
0.426 |
|
| 2001 |
Behrens S, Maier R, de Cock H, Schmid FX, Gross CA. The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. The Embo Journal. 20: 285-94. PMID 11226178 DOI: 10.1093/Emboj/20.1.285 |
0.399 |
|
| 2000 |
Perl D, Mueller U, Heinemann U, Schmid FX. Two exposed amino acid residues confer thermostability on a cold shock protein Nature Structural Biology. 7: 380-383. PMID 10802734 DOI: 10.1038/75151 |
0.477 |
|
| 2000 |
Mueller U, Perl D, Schmid FX, Heinemann U. Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock protein Journal of Molecular Biology. 297: 975-988. PMID 10736231 DOI: 10.1006/Jmbi.2000.3602 |
0.446 |
|
| 1999 |
Jacob M, Schmid FX. Protein folding as a diffusional process Biochemistry. 38: 13773-13779. PMID 10529221 DOI: 10.1021/Bi991503O |
0.494 |
|
| 1999 |
Jacob M, Geeves M, Holtermann G, Schmid FX. Diffusional barrier crossing in a two-state protein folding reaction Nature Structural Biology. 6: 923-926. PMID 10504725 DOI: 10.1038/13289 |
0.487 |
|
| 1999 |
Jacob M, Holtermann G, Perl D, Reinstein J, Schindler T, Geeves MA, Schmid FX. Microsecond folding of the cold shock protein measured by a pressure- jump technique Biochemistry. 38: 2882-2891. PMID 10074340 DOI: 10.1021/Bi982487I |
0.467 |
|
| 1999 |
Scholz C, Maier P, Dolinski K, Heitman J, Schmid FX. R73A and H144Q mutants of the yeast mitochondrial cyclophilin Cpr3 exhibit a low prolyl isomerase activity in both peptide and protein-folding assays Febs Letters. 443: 367-369. PMID 10025965 DOI: 10.1016/S0014-5793(98)01735-9 |
0.452 |
|
| 1999 |
Schindler T, Graumann PL, Perl D, Ma S, Schmid FX, Marahiel MA. The family of cold shock proteins of Bacillus subtilis: Stability and dynamics in vitro and in vivo Journal of Biological Chemistry. 274: 3407-3413. PMID 9920884 DOI: 10.1074/Jbc.274.6.3407 |
0.44 |
|
| 1999 |
Balbach J, Steegborn C, Schindler T, Schmid FX. A protein folding intermediate of ribonuclease T1 characterized at high resolution by 1D and 2D real-time NMR spectroscopy. Journal of Molecular Biology. 285: 829-42. PMID 9878447 DOI: 10.1006/Jmbi.1998.2364 |
0.648 |
|
| 1998 |
Sieber V, Plückthun A, Schmid FX. Selecting proteins with improved stability by a phage-based method Nature Biotechnology. 16: 955-960. PMID 9788353 DOI: 10.1038/Nbt1098-955 |
0.459 |
|
| 1998 |
Göthel SF, Scholz C, Schmid FX, Marahiel MA. Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions Biochemistry. 37: 13392-13399. PMID 9748346 DOI: 10.1021/Bi981253W |
0.454 |
|
| 1998 |
Scholz C, Scherer G, Mayr LM, Schindler T, Fischer G, Schmid FX. Prolyl isomerases do not catalyze isomerization of non-prolyl peptide bonds Biological Chemistry. 379: 361-365. PMID 9563833 |
0.538 |
|
| 1998 |
Scholz C, Mücke M, Rape M, Pecht A, Pahl A, Bang H, Schmid FX. Recognition of protein substrates by the prolyl isomerase trigger factor is independent of proline residues. Journal of Molecular Biology. 277: 723-32. PMID 9533890 DOI: 10.1006/Jmbi.1997.1604 |
0.477 |
|
| 1998 |
Schindler T, Perl D, Graumann P, Sieber V, Marahiel MA, Schmid FX. Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis Proteins: Structure, Function and Genetics. 30: 401-406. PMID 9533624 DOI: 10.1002/(Sici)1097-0134(19980301)30:4<401::Aid-Prot7>3.0.Co;2-L |
0.46 |
|
| 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 |
0.767 |
|
| 1998 |
Vanhove M, Lejeune A, Guillaume G, Virden R, Pain RH, Schmid FX, Frère JM. A collapsed intermediate with nonnative packing of hydrophobic residues in the folding of TEM-1 beta-lactamase. Biochemistry. 37: 1941-50. PMID 9485321 DOI: 10.1021/bi972143c |
0.351 |
|
| 1997 |
Dolinski K, Scholz C, Muir RS, Rospert S, Schmid FX, Cardenas ME, Heitman J. Functions of FKBP12 and mitochondrial cyclophilin active site residues in vitro and in vivo in Saccharomyces cerevisiae. Molecular Biology of the Cell. 8: 2267-80. PMID 9362068 DOI: 10.1091/Mbc.8.11.2267 |
0.398 |
|
| 1997 |
Scholz C, Rahfeld J, Fischer G, Schmid FX. Catalysis of protein folding by Parvulin Journal of Molecular Biology. 273: 752-762. PMID 9356262 DOI: 10.1006/Jmbi.1997.1301 |
0.682 |
|
| 1997 |
Agashe VR, Schmid FX, Udgaonkar JB. Thermodynamics of the complex protein unfolding reaction of barstar. Biochemistry. 36: 12288-95. PMID 9315868 DOI: 10.1021/Bi971062D |
0.619 |
|
| 1997 |
Scholz C, Schindler T, Dolinski K, Heitman J, Schmid FX. Cyclophilin active site mutants have native prolyl isomerase activity with a protein substrate Febs Letters. 414: 69-73. PMID 9305734 DOI: 10.1016/S0014-5793(97)00979-4 |
0.423 |
|
| 1997 |
Zarnt T, Tradler T, Stoller G, Scholz C, Schmid FX, Fischer G. Modular structure of the trigger factor required for high activity in protein folding Journal of Molecular Biology. 271: 827-837. PMID 9299330 DOI: 10.1006/Jmbi.1997.1206 |
0.64 |
|
| 1997 |
Jacob M, Schindler T, Balbach J, Schmid FX. Diffusion control in an elementary protein folding reaction. Proceedings of the National Academy of Sciences of the United States of America. 94: 5622-7. PMID 9159122 DOI: 10.1073/Pnas.94.11.5622 |
0.683 |
|
| 1997 |
Backes H, Berens C, Helbl V, Walter S, Schmid FX, Hillen W. Combinations of the α-helix-turn-α-helix motif of TetR with respective residues from LacI or 434Cro: DNA recognition, inducer binding, and urea- dependent denaturation Biochemistry. 36: 5311-5322. PMID 9154913 DOI: 10.1021/Bi961527K |
0.421 |
|
| 1997 |
Scholz C, Stoller G, Zarnt T, Fischer G, Schmid FX. Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding Embo Journal. 16: 54-58. PMID 9009267 DOI: 10.1093/Emboj/16.1.54 |
0.652 |
|
| 1997 |
Bukau B, Schmid FX, Skerra A, Breitenbach U, Darlison MG, Hammar F. Biochemie und Molekulargenetik 1996 Nachrichten Aus Chemie, Technik Und Laboratorium. 45: 166-178. DOI: 10.1002/Nadc.19970450210 |
0.305 |
|
| 1996 |
Schindler T, Schmid FX. Thermodynamic properties of an extremely rapid protein folding reaction Biochemistry. 35: 16833-16842. PMID 8988022 DOI: 10.1021/Bi962090J |
0.503 |
|
| 1996 |
Schmid FX, Frech C, Scholz C, Walter S. Catalyzed and assisted protein folding of ribonuclease T1. Biological Chemistry. 377: 417-24. PMID 8922275 |
0.414 |
|
| 1996 |
Schindler T, Mayr LM, Landt O, Hahn U, Schmid FX. The role of a trans-proline in the folding mechanism of ribonuclease T1 European Journal of Biochemistry. 241: 516-524. PMID 8917450 DOI: 10.1111/J.1432-1033.1996.00516.X |
0.503 |
|
| 1996 |
Walter S, Lorimer GH, Schmid FX. A thermodynamic coupling mechanism for GroEL-mediated unfolding Proceedings of the National Academy of Sciences of the United States of America. 93: 9425-9430. PMID 8790346 DOI: 10.1073/Pnas.93.18.9425 |
0.513 |
|
| 1996 |
Frech C, Wunderlich M, Glockshuber R, Schmid FX. Competition between DsbA-mediated oxidation and conformational folding of RTEM1 beta-lactamase. Biochemistry. 35: 11386-95. PMID 8784194 DOI: 10.1021/Bi9608525 |
0.446 |
|
| 1996 |
Scholz C, Zarnt T, Kern G, Lang K, Burtscher H, Fischer G, Schmid FX. Autocatalytic folding of the folding catalyst FKBP12 Journal of Biological Chemistry. 271: 12703-12707. PMID 8662669 DOI: 10.1074/Jbc.271.22.12703 |
0.689 |
|
| 1996 |
Frech C, Wunderlich M, Glockshuber R, Schmid FX. Preferential binding of an unfolded protein to DsbA. The Embo Journal. 15: 392-98. PMID 8617214 DOI: 10.1002/J.1460-2075.1996.Tb00369.X |
0.517 |
|
| 1996 |
Mayr LM, Odefey C, Schutkowski M, Schmid FX. Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique Biochemistry. 35: 5550-5561. PMID 8611546 DOI: 10.1021/Bi953035Y |
0.518 |
|
| 1996 |
Schmid FX. Protein folding. Prolyl isomerases join the fold. Current Biology : Cb. 5: 993-4. PMID 8542292 DOI: 10.1016/S0960-9822(95)00197-7 |
0.481 |
|
| 1995 |
Frech C, Schmid FX. DsbA-mediated disulfide bond formation and catalyzed prolyl isomerization in oxidative protein folding. The Journal of Biological Chemistry. 270: 5367-74. PMID 7890650 DOI: 10.1074/Jbc.270.10.5367 |
0.483 |
|
| 1995 |
Odefey C, Mayr LM, Schmid FX. Non-prolyl cis-trans peptide bond isomerization as a rate-determining step in protein unfolding and refolding Journal of Molecular Biology. 245: 69-78. PMID 7823321 DOI: 10.1016/S0022-2836(95)80039-5 |
0.463 |
|
| 1995 |
Kern G, Kern D, Schmid FX, Fischer G. A kinetic analysis of the folding of human carbonic anhydrase II and its catalysis by cyclophilin Journal of Biological Chemistry. 270: 740-745. PMID 7822304 DOI: 10.1074/Jbc.270.2.740 |
0.614 |
|
| 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 |
0.681 |
|
| 1995 |
Frech C, Schmid FX. Influence of protein conformation on disulfide bond formation in the oxidative folding of ribonuclease T1. Journal of Molecular Biology. 251: 135-49. PMID 7643382 DOI: 10.1006/Jmbi.1995.0421 |
0.553 |
|
| 1995 |
Stoller G, Rücknagel KP, Nierhaus KH, Schmid FX, Fischer G, Rahfeld JU. A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor Embo Journal. 14: 4939-4948. PMID 7588623 |
0.507 |
|
| 1995 |
Schindler T, Herrler M, Marahiel MA, Schmid FX. Extremely rapid protein folding in the absence of intermediates. Nature Structural Biology. 2: 663-73. PMID 7552728 DOI: 10.1038/Nsb0895-663 |
0.513 |
|
| 1995 |
Walter S, Hubner B, Hahn U, Schmid FX. Destabilization of a Protein Helix by Electrostatic Interactions Journal of Molecular Biology. 252: 133-143. DOI: 10.1006/Jmbi.1995.0480 |
0.451 |
|
| 1995 |
Stoller G, Rücknagel KP, Nierhaus KH, Schmid FX, Fischer G, Rahfeld JU. A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. The Embo Journal. 14: 4939-4948. DOI: 10.1002/J.1460-2075.1995.Tb00177.X |
0.562 |
|
| 1994 |
Mayr LM, Willbold D, Rösch P, Schmid FX. Generation of a non-prolyl cis peptide bond in ribonuclease T1. Journal of Molecular Biology. 240: 288-93. PMID 8035456 DOI: 10.1006/Jmbi.1994.1446 |
0.407 |
|
| 1994 |
Mücke M, Schmid FX. Intact disulfide bonds decelerate the folding of ribonuclease T1. Journal of Molecular Biology. 239: 713-25. PMID 8014991 DOI: 10.1006/Jmbi.1994.1408 |
0.509 |
|
| 1994 |
Mayr LM, Willbold D, Landt O, Schmid FX. Role of the Cys 2‐Cys 10 disulfide bond for the structure, stability, and folding kinetics of ribonuclease T1 Protein Science. 3: 227-239. PMID 8003959 DOI: 10.1002/Pro.5560030207 |
0.501 |
|
| 1994 |
Mücke M, Schmid FX. A kinetic method to evaluate the two-state character of solvent-induced protein denaturation. Biochemistry. 33: 12930-5. PMID 7947699 DOI: 10.1021/Bi00209A025 |
0.462 |
|
| 1994 |
Kern G, Kern D, Schmid FX, Fischer G. Reassessment of the putative chaperone function of prolyl-cis/trans-isomerases Febs Letters. 348: 145-148. PMID 7913447 DOI: 10.1016/0014-5793(94)00591-5 |
0.583 |
|
| 1994 |
Muecke M, Schmid FX. Folding mechanism of ribonuclease T1 in the absence of the disulfide bonds Biochemistry. 33: 14608-14619. DOI: 10.1021/Bi00252A029 |
0.507 |
|
| 1993 |
Mayr LM, Schmid FX. Kinetic models for unfolding and refolding of ribonuclease T1 with substitution of cis-proline 39 by alanine. Journal of Molecular Biology. 231: 913-26. PMID 8515460 DOI: 10.1006/Jmbi.1993.1337 |
0.507 |
|
| 1993 |
Mayr LM, Landt O, Hahn U, Schmid FX. Stability and folding kinetics of ribonuclease T1 are strongly altered by the replacement of cis-proline 39 with alanine. Journal of Molecular Biology. 231: 897-912. PMID 8515459 DOI: 10.1006/Jmbi.1993.1336 |
0.525 |
|
| 1993 |
Mayr LM, Schmid FX. A purification method for labile variants of ribonuclease T1. Protein Expression and Purification. 4: 52-8. PMID 8425108 DOI: 10.1006/Prep.1993.1008 |
0.397 |
|
| 1993 |
Mayr LM, Schmid FX. Stabilization of a protein by guanidinium chloride. Biochemistry. 32: 7994-8. PMID 8347603 DOI: 10.1021/Bi00082A021 |
0.454 |
|
| 1993 |
Schmid FX, Mayr LM, Mücke M, Schönbrunner ER. Prolyl isomerases: role in protein folding. Advances in Protein Chemistry. 44: 25-66. PMID 8317297 DOI: 10.1016/S0065-3233(08)60563-X |
0.551 |
|
| 1993 |
Schmid FX. Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions. Annual Review of Biophysics and Biomolecular Structure. 22: 123-42. PMID 7688608 DOI: 10.1146/Annurev.Bb.22.060193.001011 |
0.506 |
|
| 1992 |
Kiefhaber T, Grunert HP, Hahn U, Schmid FX. Folding of RNase T1 is decelerated by a specific tertiary contact in a folding intermediate Proteins: Structure, Function and Genetics. 12: 171-179. PMID 1603806 DOI: 10.1002/Prot.340120210 |
0.802 |
|
| 1992 |
Schönbrunner ER, Schmid FX. Peptidyl-prolyl cis-trans isomerase improves the efficiency of protein disulfide isomerase as a catalyst of protein folding. Proceedings of the National Academy of Sciences of the United States of America. 89: 4510-3. PMID 1584784 DOI: 10.1073/Pnas.89.10.4510 |
0.508 |
|
| 1992 |
Kiefhaber T, Schmid FX. Kinetic coupling between protein folding and prolyl isomerization. II. Folding of ribonuclease A and ribonuclease T1 Journal of Molecular Biology. 224: 231-240. PMID 1548701 DOI: 10.1016/0022-2836(92)90586-9 |
0.784 |
|
| 1992 |
Kiefhaber T, Kohler HH, Schmid FX. Kinetic coupling between protein folding and prolyl isomerization. I. Theoretical models Journal of Molecular Biology. 224: 217-229. PMID 1548700 DOI: 10.1016/0022-2836(92)90585-8 |
0.784 |
|
| 1992 |
Mücke M, Schmid FX. Enzymatic catalysis of prolyl isomerization in an unfolding protein. Biochemistry. 31: 7848-54. PMID 1510971 DOI: 10.1021/Bi00149A015 |
0.556 |
|
| 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 |
0.766 |
|
| 1992 |
Kiefhaber T, Schmid FX, Willaert K, Engelborghs Y, Chaffotte A. Structure of a rapidly formed intermediate in ribonuclease T1 folding Protein Science. 1: 1162-1172. PMID 1304394 DOI: 10.1002/Pro.5560010910 |
0.801 |
|
| 1992 |
Schultz DA, Schmid FX, Baldwin RL. Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutation. Protein Science : a Publication of the Protein Society. 1: 917-24. PMID 1304376 DOI: 10.1002/Pro.5560010710 |
0.675 |
|
| 1992 |
Schmid FX. The mechanism of protein folding Current Opinion in Structural Biology. 2: 21-25. DOI: 10.1016/0959-440X(92)90171-3 |
0.479 |
|
| 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 |
0.798 |
|
| 1991 |
Schmid FX. Catalysis and assistance of protein folding Current Opinion in Structural Biology. 1: 36-41. DOI: 10.1016/0959-440X(91)90008-H |
0.532 |
|
| 1990 |
Lang K, Schmid FX. Role of two proline-containing turns in the folding of porcine ribonuclease. Journal of Molecular Biology. 212: 185-96. PMID 2319596 DOI: 10.1016/0022-2836(90)90314-C |
0.533 |
|
| 1990 |
Fischer G, Schmid FX. The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell. Biochemistry. 29: 2205-12. PMID 2186809 DOI: 10.1021/Bi00461A001 |
0.621 |
|
| 1990 |
Kiefhaber T, Schmid FX, Renner M, Hinz HJ, Hahn U, Quaas R. Stability of recombinant Lys25-ribonuclease T1. Biochemistry. 29: 8250-7. PMID 2123715 DOI: 10.1021/Bi00488A008 |
0.755 |
|
| 1990 |
Kiefhaber T, Grunert HP, Hahn U, Schmid FX. Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding. Biochemistry. 29: 6475-80. PMID 2119802 DOI: 10.1021/Bi00479A020 |
0.779 |
|
| 1990 |
Kiefhaber T, Quaas R, Hahn U, Schmid FX. Folding of ribonuclease T1. 2. Kinetic models for the folding and unfolding reactions. Biochemistry. 29: 3061-70. PMID 2110824 DOI: 10.1021/Bi00464A024 |
0.794 |
|
| 1990 |
Kiefhaber T, Quaas R, Hahn U, Schmid FX. Folding of ribonuclease T1. 1. Existence of multiple unfolded states created by proline isomerization. Biochemistry. 29: 3053-61. PMID 2110823 DOI: 10.1021/Bi00464A023 |
0.804 |
|
| 1990 |
Tropschug M, Wachter E, Mayer S, Schönbrunner ER, Schmid FX. Isolation and sequence of an FK506-binding protein from N. crassa which catalyses protein folding. Nature. 346: 674-7. PMID 1696687 DOI: 10.1038/346674A0 |
0.509 |
|
| 1989 |
Fischer G, Wittmann-Liebold B, Lang K, Kiefhaber T, Schmid FX. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature. 337: 476-8. PMID 2492638 DOI: 10.1038/337476A0 |
0.81 |
|
| 1988 |
Lang K, Schmid FX. Protein-disulphide isomerase and prolyl isomerase act differently and independently as catalysts of protein folding. Nature. 331: 453-5. PMID 3277061 DOI: 10.1038/331453A0 |
0.521 |
|
| 1987 |
Grafl R, Lang K, Wrba A, Schmid FX. Folding mechanism of porcine ribonuclease. Journal of Molecular Biology. 191: 281-93. PMID 3806674 DOI: 10.1016/0022-2836(86)90265-2 |
0.503 |
|
| 1987 |
Lang K, Schmid FX, Fischer G. Catalysis of protein folding by prolyl isomerase. Nature. 329: 268-70. PMID 3306408 DOI: 10.1038/329268A0 |
0.676 |
|
| 1986 |
Schmid FX. Proline isomerization during refolding of ribonuclease A is accelerated by the presence of folding intermediates. Febs Letters. 198: 217-20. PMID 3956730 DOI: 10.1016/0014-5793(86)80408-2 |
0.432 |
|
| 1986 |
Schmid FX. Fast-folding and slow-folding forms of unfolded proteins. Methods in Enzymology. 131: 70-82. PMID 3773774 DOI: 10.1016/0076-6879(86)31035-8 |
0.52 |
|
| 1986 |
Lang K, Schmid FX. Use of a trypsin-pulse method to study the refolding pathway of ribonuclease. European Journal of Biochemistry. 159: 275-81. PMID 3758063 DOI: 10.1111/J.1432-1033.1986.Tb09864.X |
0.458 |
|
| 1986 |
Lang K, Wrba A, Krebs H, Schmid FX, Beintema JJ. Folding kinetics of mammalian ribonucleases. Febs Letters. 204: 135-9. PMID 3743758 DOI: 10.1016/0014-5793(86)81401-6 |
0.486 |
|
| 1986 |
Schmid FX, Grafl R, Wrba A, Beintema JJ. Role of proline peptide bond isomerization in unfolding and refolding of ribonuclease. Proceedings of the National Academy of Sciences of the United States of America. 83: 872-6. PMID 3456571 DOI: 10.1073/Pnas.83.4.872 |
0.488 |
|
| 1985 |
Kuwajima K, Schmid FX. Experimental studies of folding kinetics and structural dynamics of small proteins. Advances in Biophysics. 18: 43-74. PMID 6399821 DOI: 10.1016/0065-227X(84)90006-6 |
0.541 |
|
| 1985 |
Krebs H, Schmid FX, Jaenicke R. Native-like folding intermediates of homologous ribonucleases. Biochemistry. 24: 3846-52. PMID 4052370 DOI: 10.1021/Bi00336A005 |
0.771 |
|
| 1984 |
Schmid FX, Buonocore MH, Baldwin RL. Tests of the simple model of Lin and Brandts for the folding kinetics of ribonuclease A. Biochemistry. 23: 3389-94. PMID 6466645 DOI: 10.1021/Bi00310A002 |
0.654 |
|
| 1984 |
Schmid FX, Blaschek H. An early intermediate in the folding of ribonuclease A is protected against cleavage by pepsin. Biochemistry. 23: 2128-2133. PMID 6428447 DOI: 10.1021/Bi00305A004 |
0.507 |
|
| 1983 |
Schmid FX. Mechanism of folding of ribonuclease A. Slow refolding is a sequential reaction via structural intermediates. Biochemistry. 22: 4690-6. PMID 6626523 DOI: 10.1021/Bi00289A013 |
0.513 |
|
| 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 |
0.766 |
|
| 1982 |
Schmid FX. CD properties of the fast- and slow-folding forms of unfolded ribonuclease A. Febs Letters. 139: 190-2. PMID 6281064 DOI: 10.1016/0014-5793(82)80848-X |
0.302 |
|
| 1982 |
Rehage A, Schmid FX. Fast- and slow-refolding forms of unfolded ribonuclease A differ in tyrosine fluorescence Biochemistry. 21: 1499-1505. DOI: 10.1021/Bi00536A006 |
0.301 |
|
| 1981 |
Schmid FX, Blaschek H. A native-like intermediate on the ribonuclease A folding pathway. 2. Comparison of its properties to native ribonuclease A. European Journal of Biochemistry. 114: 111-7. PMID 6260489 DOI: 10.1111/J.1432-1033.1981.Tb06180.X |
0.492 |
|
| 1981 |
Schmid FX. A native-like intermediate on the ribonuclease A folding pathway. 1. Detection by tyrosine fluorescence changes. European Journal of Biochemistry. 114: 105-9. PMID 6260488 DOI: 10.1111/J.1432-1033.1981.Tb06179.X |
0.331 |
|
| 1979 |
Cook KH, Schmid FX, Baldwin RL. Role of proline isomerization in folding of ribonuclease A at low temperatures. Proceedings of the National Academy of Sciences of the United States of America. 76: 6157-61. PMID 293712 DOI: 10.1073/Pnas.76.12.6157 |
0.704 |
|
| 1979 |
Schmid FX, Baldwin RL. The rate of interconversion between the two unfolded forms of ribonuclease A does not depend on guanidinium chloride concentration. Journal of Molecular Biology. 133: 285-7. PMID 231661 DOI: 10.1016/0022-2836(79)90536-9 |
0.681 |
|
| 1979 |
Schmid FX, Baldwin RL. Detection of an early intermediate in the folding of ribonuclease A by protection of amide protons against exchange. Journal of Molecular Biology. 135: 199-215. PMID 43397 DOI: 10.1016/0022-2836(79)90347-4 |
0.696 |
|
| 1979 |
Hagerman PJ, Schmid FX, Baldwin RL. Refolding behavior of a kinetic intermediate observed in the low pH unfolding of ribonuclease A. Biochemistry. 18: 293-7. PMID 33695 DOI: 10.1021/Bi00569A009 |
0.674 |
|
| 1978 |
Schmid FX, Baldwin RL. Acid catalysis of the formation of the slow-folding species of RNase A: evidence that the reaction is proline isomerization. Proceedings of the National Academy of Sciences of the United States of America. 75: 4764-8. PMID 283390 DOI: 10.1073/Pnas.75.10.4764 |
0.684 |
|
| 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 |
0.659 |
|
| 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 |
0.681 |
|
| 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 |
0.703 |
|
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