Publikationen

2018

  • Sabbagh J.J., Cordova R.A, Zheng D., Criado-Marrero M., Lemus A., Li P., Baker J.D., Nordhues B.A., Darling A.L., Martinez-Licha C., Rutz D.A., Patel S., Buchner J., Leahy J.W., Koren J., Dickey C.A. & Blair L.J. (2018)
    Targeting the FKBP51/GR/Hsp90 complex to identify functionally relevant treatments for depression and PTSD.
    ACS Chem Biol.
  • Rutz D.A, Luo Q., Freiburger L., Madl T., Kaila V.R.I., Sattler M. & Buchner J. (2018)
    A switch point in the molecular chaperone Hsp90 responding to client interaction.
    Nat Commun 9, 1472.
  • Rosam M, Krader D., Nickels C., Hochmair J., Back K.C., Agam G., Barth A., Zeymer C., Hendrix J., Schneider M., Antes I., Reinstein J., Lamb D.C & Buchner J. (2018)
    Bap (Sil1) regulates the molecular chaperone BiP by coupling release of nucleotide and substrate.
    Nat Struct Mol Biol 25, 90-100.
  • Jahn M., Tych K., Girstmair H., Steinmassl M., Hugel T., Buchner J. & Rief M. (2018)
    Folding and domain interactions of three orthologs of Hsp90 studied by single-molecule force spectroscopy.
    Structure 26, 96-105 e4.

2017

  • Stiegler S.C., Rübbelke M, Korotkov V.S, Weiwad M., John C, Fischer G., Sieber S.A., Sattler M. & Buchner J. (2017)
    A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.
    J Biol Chem 292, 17073 - 17083.
  • Schuster M., Schnell L., Feigl P., Birkhofer C., Mohr K., Roeder M., Carle S., Langer S., Tippel F., Buchner J., Fischer G., Hausch F., Frick M., Schwan C., Aktories K., Schiene-Fischer C. & Barth H. (2017)
    The Hsp90 machinery facilitates the transport of diphtheria toxin into human cells.
    Sci Rep 7, 613.
  • Schopf F.H., Biebl M.M. & Buchner J. (2017)
    The HSP90 chaperone machinery.
    Nat Rev Mol Cell Biol 18, 345 - 360.
  • Preis W., Bestehorn A., Buchner J. & Haslbeck M. (2017)
    An alternative splice variant of human alphaA-crystallin modulates the oligomer ensemble and the chaperone activity of alpha-crystallins.
    Cell Stress Chaperones 22, 541 - 552.
  • Mymrikov E.V., Daake M.A., Richter B., Haslbeck M. & Buchner J. (2017)
    The chaperone activity and substrate spectrum of human small heat shock proteins.
    J Biol Chem 292, 672 - 684.
  • Luo Q., Boczek E.E., Wang Q., Buchner J. & Kaila V.R.I. (2017)
    Hsp90 dependence of a kinase is determined by its conformational landscape.
    Sci Rep 7, 43996.
  • Hora M., Carballo-Pacheco M., Weber B., Morris V.K., Wittkopf A., Buchner J., Strodel B. & Reif B. (2017)
    Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains.
    Sci Rep 7, 41515.
  • Hora M., Carballo Pacheco M., Weber B., Buchner J., Strodel B. & Reif B. (2017)
    Solid- and solution-state nuclear magnetic resonance spectroscopic studies on antibody light chain amyloid formation and interactions with epigallocatechin gallate.
    Amyloid 24, 10.
  • Gade Malmos K., Blancas-Mejia L.M., Weber B., Buchner J., Ramirez-Alvarado M., Naiki H. & Otzen D. (2017)
    ThT 101: a primer on the use of thioflavin T to investigate amyloid formation.
    Amyloid 24, 1 - 16.

2016

  • Zierer B.K., Rubbelke M., Tippel F., Madl T., Schopf H.F., Rutz D.A., Richter K., Sattler M. & Buchner J. (2016)
    Importance of cycle timing for the function of the molecular chaperone Hsp90.
    Nat Struct Mol Biol 23, 1020 - 1028.
  • Schneider M., Rosam M., Glaser M., Patronov A., Shah H., Back K.C., Daake M.A., Buchner J. & Antes I. (2016)
    BiPPred: Combined sequence- and structure-based prediction of peptide binding to the Hsp70 chaperone BiP.
    Proteins 84, 1390 - 1407.
  • Rehn A., Moroni E., Zierer B.K., Tippel F., Morra G., John C., Richter K., Colombo G. & Buchner J. (2016)
    Allosteric regulation points control the conformational dynamics of the molecular chaperone Hsp90.
    J Mol Biol 428, 4559 - 4571.
  • Nokwe C.N., Hora M., Zacharias M., Yagi H., Peschek J., Reif B., Goto Y & Buchner J. (2016)
    A stable mutant predisposes antibody domains to amyloid formation through specific non-native interactions.
    J Mol Biol 428, 1315 - 1332.
  • Jamasbi J., Megens R.T.A., Bianchini M., Uhland K., Munch G., Ungerer M., Sherman S., Faussner A., Brandl R., John C., Buchner J., Weber C., Lorenz R., Elia N. & Siess W. (2016)
    Cross-linking GPVI-Fc by anti-Fc antibodies potentiates its inhibition of atherosclerotic plaque- and collagen-induced platelet activation.
    JACC 1, 142-13.
  • Jahn M., Buchner J., Hugel T. & Rief M. (2016)
    Folding and assembly of the large molecular machine Hsp90 studied in single-molecule experiments.
    Proc Natl Acad Sci USA 113, 1232 - 1237.
  • Hoseini H., Pandey S., Jores T., Schmitt A., Franz-Wachtel M., Macek B., Buchner J., Dimmer K.S. & Rapaport D. (2016)
    The cytosolic cochaperone Sti1 is relevant for mitochondrial biogenesis and morphology.
    FEBS J 283, 3338 - 3352.
  • Haslbeck M., Peschek J., Buchner J. & Weinkauf S. (2016)
    Structure and function of alpha-crystallins: Traversing from in vitro to in vivo.
    Biochim Biophys Acta 1860, 149 - 166.
  • Dashivets T., Stracke J., Dengl S., Knaupp A., Pollmann J., Buchner J. & Schlothauer T. (2016)
    Oxidation in the complementarity-determining regions differentially influences the properties of therapeutic antibodies.
    mAbs 8, 1525 - 1535

2015

  • Röhl A., Wengler D., Madl T., Lagleder S., Tippel F., Herrmann M., Hendrix J., Richter K., Hack G., Schmid A.B., Kessler H., Lamb D.C. & Buchner J. (2015)
    Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.
    Nat Commun 6, 6655.
  • Röhl A., Tippel F., Bender E., Schmid A.B., Richter K., Madl T. & Buchner J. (2015)
    Hop/Sti1 phosphorylation inhibits its co-chaperone function.
    EMBO Reports 16, 240 - 9.
  • Rehn A.B. & Buchner J. (2015)
    P23 and Aha1.
    Subcell Biochem 78, 113 - 131.
  • Huang B., Lucas T., Kueppers C., Dong X., Krause M., Bepperling A., Buchner J., Voshol H., Weiss A., Gerrits B. & Kochanek S. (2015)
    Scalable production in human cells and biochemical characterization of full-length normal and mutant huntingtin.
    PloS one 10, e0121055.
  • Haslbeck M., Peschek J., Buchner J. & Weinkauf S. (2015)
    Structure and function of alpha-crystallins: Traversing from in vitro to in vivo.
    Biochimica et Biophysica Acta 25, 00170 - 00171.
  • Haslbeck M. & Buchner J.
    Assays to characterize molecular chaperone function in vitro.
    in Methods Mol Biol. (2015), vol. 1292, pp. 2522 - 3_3.
  • Fleckenstein T., Kastenmüller A., Stein M.L., Peters C., Daake M., Krause M., Weinfurtner D., Haslbeck M., Weinkauf S., Groll M. & Buchner J. (2015)
    The chaperone activity of the developmental small heat shock protein Sip1 is regulated by pH-dependent conformational changes.
    Mol Cell 58, 1067 - 78.
  • Boczek E.E., Reefschläger L.G., Dehling M., Struller T.J., Häusler E., Seidl A., Kaila V.R.I. & Buchner J. (2015)
    Conformational processing of oncogenic v-Src kinase by the molecular chaperone Hsp90.
    Proc Natl Acad Sci USA 8, 201424342.

2014

  • Zierer B.K., Weiwad M., Rubbelke M., Freiburger L., Fischer G., Lorenz O.R., Sattler M., Richter K. & Buchner J. (2014)
    Artificial accelerators of the molecular chaperone hsp90 facilitate rate-limiting conformational transitions.
    Angew Chem Int Ed Engl 53, 12257 - 12262.
  • Röhl A., Tippel F., Bender E., Schmid A.B., Richter K., Madl T. & Buchner J. (2014)
    Hop/Sti1 phosphorylation inhibits its co-chaperone function.
    EMBO Rep 12.
  • Paul A., Garcia Y.A., Zierer B.K., Patwardhan C., Gutierrez O., Hildenbrand Z., Harris D.C., Balsiger H.A., Sivils J.C., Johnson J.L., Buchner J., Chadli A. & Cox M.B. (2014)
    The cochaperone SGTA (Small Glutamine-rich Tetratricopeptide Repeat-containing Protein Alpha) demonstrates regulatory specificity for the androgen, glucocorticoid, and progesterone receptors.
    J Biol Chem 289, 15297 - 15308.
  • Nokwe C.N., Zacharias M., Yagi H., Hora M., Reif B., Goto Y. & Buchner J. (2014)
    A residue-specific shift in stability and amyloidogenicity of antibody variable domains.
    J Biol Chem 289, 26829 - 26846.
  • Lorenz O.R., Freiburger L., Rutz D.A., Krause M., Zierer B.K., Alvira S., Cuellar J., Valpuesta J.M., Madl T., Sattler M. & Buchner J. (2014)
    Modulation of the Hsp90 chaperone cycle by a stringent client protein.
    Mol Cell 53, 941 - 953.
  • Jahn M., Rehn A.B., Pelz B., Hellenkamp B., Richter K., Rief M., Buchner J. & Hugel T. (2014)
    The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function.
    Proc Natl Acad Sci USA 2, 201414073.
  • Girstmair H. & Buchner J. (2014)
    GET two for one.
    Mol Cell 56, 1 - 2.
  • Feige M.J., Grawert M.A., Marcinowski M., Hennig J., Behnke J., Auslander D., Herold E.M., Peschek J., Castro C.D., Flajnik M., Hendershot L.M., Sattler M., Groll M. & Buchner J. (2014)
    The structural analysis of shark IgNAR antibodies reveals evolutionary principles of immunoglobulins.
    Proc Natl Acad Sci USA 111, 8155 - 8160.
  • Feige M.J. & Buchner J. (2014)
    Principles and engineering of antibody folding and assembly.
    Biochimica et Biophysica Acta 1844, 2024 - 2031.
  • Buchner J. & Kessler H. (2014)
    Protein folding by interaction.
    Structure 22, 936 - 937.
  • Alvira S., Cuellar J., Rohl A., Yamamoto S., Itoh H., Alfonso C., Rivas G., Buchner J. & Valpuesta J.M. (2014)
    Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop.
    Nat Commun 5, 5484.

2013

  • Röhl A., Rohrberg J. & Buchner J. (2013)
    The chaperone Hsp90: changing partners for demanding clients.
    Trends Biochem Sci 38, 253 - 262.
  • Retzlaff M., Rohrberg J., Kupper N.J., Lagleder S., Bepperling A., Manzenrieder F., Peschek J., Kessler H. & Buchner J. (2013)
    The regulatory domain stabilizes the p53 tetramer by intersubunit contacts with the DNA binding domain.
    J Mol Biol 425, 144 - 155.
  • Peschek J., Braun N., Rohrberg J., Back K.C., Kriehuber T., Kastenmüller A., Weinkauf S. & Buchner J. (2013)
    Regulated structural transitions unleash the chaperone activity of αB-crystallin.
    Proc Natl Acad Sci USA.
  • Müller R., Gräwert M.A., Kern T., Madl T., Peschek J., Sattler M., Groll M. & Buchner J. (2013)
    High-resolution structures of the IgM Fc domains reveal principles of its hexamer formation.
    Proc Natl Acad Sci USA 110, 10183 - 10188.
  • Marcinowski M., Rosam M., Seitz C., Elferich J., Behnke J., Bello C., Feige M.J., Becker C.F.W., Antes I. & Buchner J. (2013)
    Conformational selection in substrate recognition by Hsp70 chaperones.
    J Mol Biol 425, 466 - 474.
  • Li J., Zoldak G., Kriehuber T., Soroka J., Schmid F.X., Richter K. & Buchner J. (2013)
    The unique proline-rich domain regulates the chaperone function of AIPL1.
    Biochemistry 52.
  • Li J., Richter K., Reinstein J. & Buchner J. (2013)
    Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.
    Nat Struct Mol Biol 20, 326 - 331.
  • Li J. & Buchner J. (2013)
    Structure, function and regulation of the Hsp90 machinery.
    Biomed J 36, 106 - 117.
  • Kayser J., Haslbeck M., Dempfle L., Krause M., Grashoff C., Buchner J., Herrmann H. & Bausch A.R. (2013)
    The small heat shock protein Hsp27 affects assembly dynamics and structure of keratin intermediate filament networks.
    Biophys J 105, 1778 - 1785.
  • Kateb F., Perrin H., Tripsianes K., Zou P., Spadaccini R., Bottomley M., Franzmann T.M., Buchner J., Ansieau S. & Sattler M. (2013)
    Structural and functional analysis of the DEAF-1 and BS69 MYND domains.
    PloS one 8, 1 - 11.
  • Hendershot L.M., Feige M.J. & Buchner J. (2013)
    Acidification activates ERp44 -- a molecular litmus test for protein assembly.
    Mol Cell 50, 779 - 781.
  • Bertz M., Buchner J. & Rief M. (2013)
    Mechanical stability of the antibody domain CH3 homodimer in different oxidation states.
    J Am Chem Soc 135, 15085 - 15091.
  • Beebe K., Mollapour M., Scroggins B., Prodromou C., Xu W., Tokita M., Taldone T., Pullen L., Zierer B.K., Lee M.-J., Trepel J., Buchner J., Bolon D., Chiosis G. & Neckers L. (2013)
    Posttranslational modification and conformational state of Heat Shock Protein 90 differentially affect binding of chemically diverse small molecule inhibitors.
    Oncotarget 4, 1065 - 1074.

2012

  • Zierer B.K. & Buchner J. (2012)
    Hsp90 Chaperones.
    eLS - Structural Biology.
  • Soroka J., Wandinger S.K., Mäusbacher N., Schreiber T.B., Richter K., Daub H. & Buchner J. (2012)
    Conformational switching of the molecular chaperone Hsp90 via regulated phosphorylation.
    Mol Cell 45, 517 - 528.
  • Soroka J. & Buchner J. (2012)
    Mechanistic aspects of the Hsp90 phosphoregulation.
    Cell Cycle 11, 1870 - 1871.
  • Schreiber T.B., Mäusbacher N., Soroka J., Wandinger S.K., Buchner J. & Daub H. (2012)
    Global analysis of phosphoproteome regulation by the Ser/Thr phosphatase Ppt1 in Saccharomyces cerevisiae.
    J Proteome Res 11, 2397 - 408.
  • Schmid A.B., Lagleder S., Grawert M.A., Röhl A., Hagn F., Wandinger S.K., Cox M.B., Demmer O., Richter K., Groll M., Kessler H. & Buchner J. (2012)
    The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop.
    EMBO J 31, 1506 - 1517.
  • Li J., Soroka J. & Buchner J. (2012)
    The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones.
    Biochimica et Biophysica Acta 1823, 624 - 635.
  • Kayser J., Haslbeck M., Herrmann H., Buchner J. & Bausch A.R. (2012)
    Heat shock proteins regulate structure of Intermediate filament networks.
    Biophysical Journal 102, 696a.
  • Buchner J., Smock R.G., Gierasch L.M. & Horwich A.L.
    Chaperones and protein folding.
    in Comprehensive Biophysics, E. Egelman, Ed. (Academic Pr, 2012).
  • Bepperling A., Alte F., Kriehuber T., Braun N., Weinkauf S., Groll M., Haslbeck M. & Buchner J. (2012)
    Alternative bacterial two-component small heat shock protein systems.
    Proc Natl Acad Sci USA 109, 20407 - 20412.

2011

  • Schroeder B.O., Wu Z., Nuding S., Groscurth S., Marcinowski M., Beisner J., Buchner J., Schaller M., Stange E.F. & Wehkamp J. (2011)
    Reduction of disulphide bonds unmasks potent antimicrobial activity of human β-defensin 1.
    Nature 469, 419 - 423.
  • Richter K. & Buchner J. (2011)
    Closing in on the Hsp90 chaperone-client relationship.
    Structure 19, 445 - 446.
  • Marcinowski M., Höller M., Feige M.J., Baerend D., Lamb D.C. & Buchner J. (2011)
    Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions.
    Nat Struct Mol Biol 18, 150 - 158.
  • Li J., Richter K. & Buchner J. (2011)
    Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle.
    Nat Struct Mol Biol 18, 61 - 66.
  • Kaiser E., Kroll C., Ernst K., Schwan C., Popoff M., Fischer G., Buchner J., Aktories K. & Barth H. (2011)
    Membrane translocation of binary actin-ADP-ribosylating toxins from Clostridium difficile and Clostridium perfringens is facilitated by cyclophilin A and Hsp90.
    Infect Immun 79, 3913 - 3921.
  • Hagn F., Lagleder S., Retzlaff M., Rohrberg J., Demmer O., Richter K., Buchner J. & Kessler H. (2011)
    Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53.
    Nat Struct Mol Biol 18, 1086 - 1093.
  • Dmochewitz L., Lillich M., Kaiser E., Jennings L.D., Lang A.E., Buchner J., Fischer G., Aktories K., Collier R.J. & Barth H. (2011)
    Role of CypA and Hsp90 in membrane translocation mediated by anthrax protective antigen.
    Cell Microbiol 13, 359 - 373.
  • Braun N., Zacharias M., Peschek J., Kastenmuller A., Zou J., Hanzlik M., Haslbeck M., Rappsilber J., Buchner J. & Weinkauf S. (2011)
    Multiple molecular architectures of the eye lens chaperone alphaB-crystallin elucidated by a triple hybrid approach.
    Proc Natl Acad Sci USA 108, 20491 - 20496.

2010

  • Welker S., Rudolph B., Frenzel E., Hagn F., Liebisch G., Schmitz G., Scheuring J., Kerth A., Blume A., Weinkauf S., Haslbeck M., Kessler H. & Buchner J. (2010)
    Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function.
    Mol Cell 39, 507 - 520.
  • Rudolph B., Gebendorfer K.M., Buchner J. & Winter J. (2010)
    Evolution of Escherichia coli for growth at high temperatures.
    J Biol Chem 285, 19029 - 19034.
  • Richter K., Haslbeck M. & Buchner J. (2010)
    The heat shock response: life on the verge of death.
    Mol Cell 40, 253 - 266.
  • Retzlaff M., Hagn F., Mitschke L., Hessling M., Gugel F., Kessler H., Richter K. & Buchner J. (2010)
    Asymmetric activation of the Hsp90 dimer by its cochaperone Aha1.
    Mol Cell 37, 344 - 354.
  • Ratzke C., Mickler M., Hellenkamp B., Buchner J. & Hugel T. (2010)
    Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle.
    Proc Natl Acad Sci USA 107, 16101 - 16106.
  • Kriehuber T., Rattei T., Weinmaier T., Bepperling A., Haslbeck M. & Buchner J. (2010)
    Independent evolution of the core domain and its flanking sequences in small heat shock proteins.
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology 24, 3633 - 3642.
  • Jinwal U.K., Koren J.r., Borysov S.I., Schmid A.B., Abisambra J.F., Blair L.J., Johnson A.G., Jones J.R., Shults C.L., O'Leary J.C.r., Jin Y., Buchner J., Cox M.B. & Dickey C.A. (2010)
    The Hsp90 cochaperone, FKBP51, increases tau stability and polymerizes microtubules.
    The Journal of neuroscience : the official journal of the Society for Neuroscience 30, 591 - 599.
  • Feige M.J., Simpson E.R., Herold E.M., Bepperling A., Heger K. & Buchner J. (2010)
    Dissecting the alternatively folded state of the antibody Fab fragment.
    J Mol Biol 399, 719 - 730.
  • Feige M.J., Hendershot L.M. & Buchner J. (2010)
    Response to corcos: exceptions to the rules.
    Trends Biochem Sci 35, 594.
  • Feige M.J., Hendershot L.M. & Buchner J. (2010)
    How antibodies fold.
    Trends Biochem Sci 35, 189 - 198.
  • Echeverria P.C., Figueras M.J., Vogler M., Kriehuber T., de Miguel N., Deng B., Dalmasso M.C., Matthews D.E., Matrajt M., Haslbeck M., Buchner J. & Angel S.O. (2010)
    The Hsp90 co-chaperone p23 of Toxoplasma gondii: Identification, functional analysis and dynamic interactome determination.
    Molecular and biochemical parasitology 172, 129 - 140.
  • Chen J., Feige M.J., Franzmann T.M., Bepperling A. & Buchner J. (2010)
    Regions outside the alpha-crystallin domain of the small heat shock protein Hsp26 are required for its dimerization.
    J Mol Biol 398, 122 - 131.
  • Buchner J. (2010)
    Bacterial Hsp90 – desperately seeking clients.
    Mol Microbiol 76, 540 - 544.
  • Bertz M., Chen J., Feige M.J., Franzmann T.M., Buchner J. & Rief M. (2010)
    Structural and mechanical hierarchies in the alpha-crystallin domain dimer of the hyperthermophilic small heat shock protein Hsp16.5.
    J Mol Biol 400, 1046 - 1056.
  • Anselment B., Baerend D., Mey E., Buchner J., Weuster-Botz D. & Haslbeck M. (2010)
    Experimental optimization of protein refolding with a genetic algorithm.
    Protein science : a publication of the Protein Society 19, 2085 - 2095.

2009

  • Tsutsumi S., Mollapour M., Graf C., Lee C.-T., Scroggins B.T., Xu W., Haslerova L., Hessling M., Konstantinova A.A., Trepel J.B., Panaretou B., Buchner J., Mayer M.P., Prodromou C. & Neckers L. (2009)
    Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain.
    Nat Struct Mol Biol 16, 1141 - 1147.
  • Simpson E.R., Herold E.M. & Buchner J. (2009)
    The folding pathway of the antibody VL domain.
    J Mol Biol 392, 1326 - 1338.
  • Retzlaff M., Stahl M., Eberl H.C., Lagleder S., Beck J., Kessler H. & Buchner J. (2009)
    Hsp90 is regulated by a switch point in the C-terminal domain.
    EMBO Reports 10, 1147 - 1153.
  • Peschek J., Braun N., Franzmann T.M., Georgalis Y., Haslbeck M., Weinkauf S. & Buchner J. (2009)
    The eye lens chaperone alpha-crystallin forms defined globular assemblies.
    Proc Natl Acad Sci USA 106, 13272 - 13277.
  • Pandya M.J., Bendz H., Manzenrieder F., Noessner E., Kessler H., Buchner J. & Issels R.D. (2009)
    Interaction of human heat shock protein 70 with tumor-associated peptides.
    Biol Chem 390, 305 - 312.
  • Müller M., Richter K., Heuck A., Kremmer E., Buchner J., Jansen R.-P. & Niessing D. (2009)
    Formation of She2p tetramers is required form RNA binding, mRNP assembly and localization.
    RNA 15, 2002 - 2012.
  • Moroder L., Buchner J., Bulaj G., Craik D., Alewood P., Wade J.D., Allemann R.K., Rabenstein D.L., Hilvert D., Adermann K., Haehnel W., Bulleid N., Fass D., Freedman R.B. & Glockshuber R.
    Oxidative folding of peptides and proteins
    Neidle S., Ed., RSC Biomolecular Sciences (Royal Society of Chemistry Publishing, Cambridge, England, 2009), pp. 448.
  • Mickler M., Hessling M., Ratzke C., Buchner J. & Hugel T. (2009)
    The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis.
    Nat Struct Mol Biol 16, 281 - 286.
  • Hessling M., Richter K. & Buchner J. (2009)
    Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90.
    Nat Struct Mol Biol 16, 287 - 293.
  • Hainzl O., Lapina M.C., Buchner J. & Richter K. (2009)
    The charged linker region is an important regulator of Hsp90 function.
    J Biol Chem 284, 22559 - 22567.
  • Feige M.J., Nath S., Catharino S.R., Weinfurtner D., Steinbacher S. & Buchner J. (2009)
    Structure of the murine unglycosylated IgG1 Fc fragment.
    J Mol Biol 391, 599 - 608.
  • Feige M.J., Groscurth S., Marcinowski M., Shimizu Y., Kessler H., Hendershot L.M. & Buchner J. (2009)
    An unfolded CH1 domain controls the assembly and secretion of IgG antibodies.
    Mol Cell 34, 569 - 579.
  • Feige M.J. & Buchner J.
    The role of disulfide bonds in protein folding and stability.
    in Oxidative folding of peptides and proteins, L. Moroder, and J. Buchner, Eds. (Royal Society of Chemistry Publishing, Cambridge, England 2009), pp. 179 - 191.
  • de Miguel N., Braun N., Bepperling A., Kriehuber T., Kastenmüller A., Buchner J., Angel S.O. & Haslbeck M. (2009)
    Structural and functional diversity in the family of small heat shock proteins from the parasite Toxoplasma gondii.
    Biochimica et Biophysica Acta 1793, 1738 - 1748.
  • Dashivets T., Wood N., Hergersberg C., Buchner J. & Haslbeck M. (2009)
    Rapid matrix-assisted refolding of histidine-tagged proteins.
    ChemBioChem 10, 869 - 876.

2008

  • Wandinger S.K., Richter K. & Buchner J. (2008)
    The Hsp90 chaperone machinery.
    J Biol Chem 283, 18473 - 18477.
  • Schmid K., Haslbeck M., Buchner J. & Somoza V. (2008)
    Induction of heat shock proteins and the proteasome system by casein-N epsilon-(carboxymethyl)lysine and N epsilon-(carboxymethyl)lysine in Caco-2 cells.
    Ann N Y Acad Sci 1126, 257 - 261.
  • Richter K., Soroka J., Skalniak L., Leskovar A., Hessling M., Reinstein J. & Buchner J. (2008)
    Conserved conformational changes in the ATPase cycle of human Hsp90.
    J Biol Chem 283, 17757 - 17765.
  • Leskovar A., Wegele H., Werbeck N.D., Buchner J. & Reinstein J. (2008)
    The ATPase cycle of the mitochondrial Hsp90 analog Trap1.
    J Biol Chem 283, 11677 - 11688.
  • Haslbeck M., Kastenmüller A., Buchner J., Weinkauf S. & Braun N. (2008)
    Structural dynamics of archaeal small heat shock proteins.
    J Mol Biol 378, 362-74.
  • Frey S., Haslbeck M., Hainzl O. & Buchner J. (2008)
    Synthesis and characterization of a functional intact IgG in a prokaryotic cell-free expression system.
    Biol Chem 389, 37 - 45.
  • Franzmann T.M., Menhorn P., Walter S. & Buchner J. (2008)
    Activation of the chaperone Hsp26 is controlled by the rearrangement of its thermosensor domain.
    Mol Cell 29, 207-16.
  • Feige M.J., Groscurth S., Marcinowski M., Yew Z.T., Truffault V., Paci E., Kessler H. & Buchner J. (2008)
    The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicity.
    Proc Natl Acad Sci USA 105, 13373 - 13378.

2007

  • Riggs D.L., Cox M.B., Tardif H.L., Hessling M., Buchner J. & Smith D.F. (2007)
    Noncatalytic role of the FKBP52 peptidyl-prolyl isomerase domain in the regulation of steroid hormone signaling.
    Mol Cell Biol 27, 8658 - 8669.
  • Richter K., Reinstein J. & Buchner J. (2007)
    A Grp on the Hsp90 mechanism.
    Mol Cell 28, 177 - 179.
  • Janig E., Haslbeck M., Aigelsreiter A., Braun N., Unterthor D., Wolf P., Khaskhely N.M., Buchner J., Denk H. & Zatloukal K. (2007)
    Clusterin associates with altered elastic fibers in human photoaged skin and prevents elastin from UV-induced aggregation in vitro.
    The American Journal of Pathology 171, 1474 - 1482.
  • Heuck A., Du T.-G., Jellbauer S., Richter K., Kruse C., Jaklin S., Müller M., Buchner J., Jansen R.-P. & Niessing D. (2007)
    Monomeric myosin V uses two binding regions for the assembly of stable translocation complexes.
    Proc Natl Acad Sci USA 104, 19778 - 19783.
  • Haslbeck M., Frey S. & Buchner J.
    Protein production in the test tube: In vitro transcription / translation systems in protein expression and folding
    in Protein folding-misfolding: Some current concepts of protein chemistry, Joseph P. Zbilut, and Thomas Scheibel, Eds. (Nova Science Publishers Inc, Hauppauge, USA, 2007), pp. 93 - 116.
  • Frey S., Leskovar A., Reinstein J. & Buchner J. (2007)
    The ATPase cycle of the endoplasmic chaperone Grp94.
    J Biol Chem 282, 35612 - 35620.
  • Feige M.J., Hagn F., Esser J., Kessler H. & Buchner J. (2007)
    Influence of the internal disulfide bridge on the folding pathway of the CL antibody domain.
    J Mol Biol 365, 1232 - 1244.
  • Cox M.B., Riggs D.L., Hessling M., Schumacher F., Buchner J. & Smith D.F. (2007)
    FK506-binding protein 52 phosphorylation: a potential mechanism for regulating steroid hormone receptor activity.
    Mol Endocrinol 21, 2956 - 2967.
  • Bendz H., Ruhland S.C., Pandya M.J., Hainzl O., Riegelsberger S., Brauchle C., Mayer M.P., Buchner J., Issels R.D. & Noessner E. (2007)
    Human heat shock protein 70 enhances tumor antigen presentation through complex formation and intracellular antigen delivery without innate immune signaling.
    J Biol Chem 282, 31688 - 31702.

2006

  • White H.E., Orlova E.V., Chen S., Wang L., Ignatiou A., Gowen B., Stromer T., Franzmann T.M., Haslbeck M., Buchner J. & Saibil H.R. (2006)
    Multiple distinct assemblies reveal conformational flexibility in the small heat shock protein Hsp26.
    Structure 14, 1197 - 1204.
  • Wegele H., Wandinger S.K., Schmid A.B., Reinstein J. & Buchner J. (2006)
    Substrate transfer from the chaperone Hsp70 to Hsp90.
    J Mol Biol 356, 802 - 811.
  • Wandinger S.K., Suhre M.H., Wegele H. & Buchner J. (2006)
    The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90.
    EMBO J 25, 367 - 376.
  • Scheibel T. & Buchner J.
    Protein aggregation as a cause for disease.
    in Molecular chaperones in health and disease, K. Starke, and Matthias Gaestel, Eds. (Springer Berlin Heidelberg, 2006), vol. 172, pp. 199 - 219.
  • Römer L., Klein C., Dehner A., Kessler H. & Buchner J. (2006)
    p53 – a natural cancer killer: structural insights and therapeutic concepts.
    Angew Chem Int Ed Engl 45, 6440 - 6460.
  • Richter K., Moser S., Hagn F., Friedrich R., Hainzl O., Heller M., Schlee S., Kessler H., Reinstein J. & Buchner J. (2006)
    Intrinsic inhibition of the Hsp90 ATPase activity.
    J Biol Chem 281, 11301 - 11311.
  • Richter K. & Buchner J. (2006)
    Hsp90: twist and fold.
    Cell 127, 251 - 253.

2005

  • Shaner L., Wegele H., Buchner J. & Morano K.A. (2005)
    The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb.
    J Biol Chem 280, 41262 - 41269.
  • Richter K., Meinlschmidt B. & Buchner J.
    Hsp90: from dispensable heat shock protein to global player.
    in Protein Folding Handbook, & T. Kiefhaber J. Buchner, Ed. (Wiley-VCH Verlag GmbH, Weinheim, Germany 2005), pp. 768 - 829.
  • Haslbeck M., Miess A., Stromer T., Walter S. & Buchner J. (2005)
    Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104.
    J Biol Chem 280, 23861 - 23868.
  • Haslbeck M., Franzmann T., Weinfurtner D. & Buchner J. (2005)
    Some like it hot: the structure and function of small heat-shock proteins.
    Nat Struct Mol Biol 12, 842 - 846.
  • Franzmann T.M., Wühr M., Richter K., Walter S. & Buchner J. (2005)
    The activation mechanism of Hsp26 does not require dissociation of the oligomer.
    J Mol Biol 350, 1083 - 1093.
  • Dehner A., Klein C., Hansen S., Müller L., Buchner J., Schwaiger M. & Kessler H. (2005)
    Cooperative binding of p53 to DNA: regulation by protein-protein interactions through a double salt bridge.
    Angew Chem Int Ed Engl 44, 5247 - 5251.
  • Catharino S.R., Buchner J. & Walter S. (2005)
    Characterization of oligomeric species in the fibrillization pathway of the yeast prion Ure2p.
    Biol Chem 386, 633 - 641.
  • Buchner J. & Walter S.
    Analysis of chaperone function in vitro.
    in Protein Folding Handbook, & T. Kiefhaber J. Buchner, Ed. (Wiley-VCH Verlag GmbH, Weinheim, Germany 2005), pp. 162 - 196.
  • Buchner J. & Kiefhaber T.
    Protein Folding Handbook
    Johannes Buchner, and Thomas Kiefhaber, Eds., Protein Folding Handbook (Wiley-VCH, Weinheim, Germany, 2005).

2004

  • Wegele H., Müller L. & Buchner J. (2004)
    Hsp70 and Hsp90--a relay team for protein folding.
    Rev Physiol Biochem Pharmacol 151, 1-44.
  • Vinci F., Catharino S.R., Frey S., Buchner J., Marino G., Pucci P. & Ruoppolo M. (2004)
    Hierarchical formation of disulfide bonds in the immunoglobulin Fc fragment is assisted by protein-disulfide isomerase.
    J Biol Chem 279, 15059 - 15066.
  • Stromer T., Fischer E., Richter K., Haslbeck M. & Buchner J. (2004)
    Analysis of the regulation of the molecular chaperone Hsp26 by temperature-induced dissociation: the N-terminal domail is important for oligomer assembly and the binding of unfolding proteins.
    J Biol Chem 279, 11222 - 11228.
  • Richter K., Walter S. & Buchner J. (2004)
    The co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle.
    J Mol Biol 342, 1403 - 1413.
  • Müller L., Schaupp A., Walerych D., Wegele H. & Buchner J. (2004)
    Hsp90 regulates the activity of wild type p53 under physiological and elevated temperatures.
    J Biol Chem 279, 48846 - 48854.
  • Mayer M., Frey S., Koivunen P., Myllyharju J. & Buchner J. (2004)
    Influence of the oxidoreductase ERp57 on the folding of an antibody Fab fragment.
    J Mol Biol 341, 1077 - 1084.
  • Haslbeck M., Ignatiou A., Saibil H., Helmich S., Frenzl E., Stromer T. & Buchner J. (2004)
    A domain in the N-terminal part of Hsp26 is essential for chaperone function and oligomerization.
    J Mol Biol 343, 445 - 455.
  • Haslbeck M., Braun N., Stromer T., Richter B., Model N., Weinkauf S. & Buchner J. (2004)
    Hsp42 is the general small heat shock protein in the cytosol of Saccharomyces cerevisiae.
    EMBO J 23, 638 - 649.
  • Hainzl O., Wegele H., Richter K. & Buchner J. (2004)
    Cns1 is an activator of the Ssa1 ATPase activity.
    J Biol Chem 279, 23267 - 23273.
  • Grimminger V., Richter K., Imhof A., Buchner J. & Walter S. (2004)
    The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104.
    J Biol Chem 279, 7378 - 7383.
  • Grawert T., Kaiser J., Zepeck F., Laupitz R., Hecht S., Amslinger S., Schramek N., Schleicher E., Weber S., Haslbeck M., Buchner J., Rieder C., Arigoni D., Bacher A., Eisenreich W. & Rohdich F. (2004)
    IspH protein of Escherichia coli: studies on iron-sulfur cluster implementation and catalysis.
    J Am Chem Soc 126, 12847 - 12855.
  • Feige M.J., Walter S. & Buchner J. (2004)
    Folding mechanism of the CH2 antibody domain.
    J Mol Biol 344, 107 - 118.
  • Falsone S.F., Leptihn S., Osterauer A., Haslbeck M. & Buchner J. (2004)
    Oncogenic mutations reduce the stability of SRC kinase.
    J Mol Biol 344, 281 - 291.

2003

  • Wegele H., Muschler P., Bunck M., Reinstein J. & Buchner J. (2003)
    Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90.
    J Biol Chem 278, 39303 - 39310.
  • Wegele H., Haslbeck M., Reinstein J. & Buchner J. (2003)
    Sti1 is a novel activator of the Ssa proteins.
    J Biol Chem 278, 25970 - 25976.
  • Stromer T., Ehrnsperger M., Gaestel M. & Buchner J. (2003)
    Analysis of the interaction of small heat shock proteins with unfolding proteins.
    J Biol Chem 278, 18015 - 18021.
  • Richter K., Muschler P., Hainzl O., Reinstein J. & Buchner J. (2003)
    Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the ATPase cycle.
    J Biol Chem 278, 10328 - 10333.
  • Mayer M., Reinstein J. & Buchner J. (2003)
    Modulation of the ATPase cycle of BiP by peptides and proteins.
    J Mol Biol 330, 137 - 144.
  • Mayer M. & Buchner J.
    Refolding of inclusion body proteins.
    in Methods in Molecular Medicine, Udo Reischl Jochen Decker, Ed. (2003), vol. 94, pp. 239 - 254.
  • Dehner A., Furrer J., Richter K., Schuster I., Buchner J. & Kessler H. (2003)
    NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol.
    ChemBioChem 4, 870 - 877.
  • Dawson R., Müller L., Dehner A., Klein C., Kessler H. & Buchner J. (2003)
    The N-terminal domain of p53 is natively unfolded.
    J Mol Biol 332, 1131 - 1141.

2002

  • Walter S. & Buchner J. (2002)
    Molecular chaperones – cellular machines for protein folding.
    Angew Chem Int Ed Engl 41, 1098 - 1113.
  • Thies M.J.W., Talamo F., Mayer M., Bell S., Ruoppolo M., Marino G. & Buchner J. (2002)
    Folding and oxidation of the antibody domain CH3.
    J Mol Biol 319, 1267 - 1277.
  • Richter K., Reinstein J. & Buchner J. (2002)
    N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.
    J Biol Chem 277, 44905 - 44910.
  • Kurek I., Pirkl F., Fischer E., Buchner J. & Breiman A. (2002)
    Wheat FKBP73 functions in vitro as a molecular chaperone independently of its peptidyl prolyl cis-trans isomerase activity.
    Planta 215, 119 - 126.
  • Knarr G., Kies U., Bell S., Mayer M. & Buchner J. (2002)
    Interaction of the chaperone BiP with an antibody domain: implications for the chaperone cycle.
    J Mol Biol 318, 611 - 620.
  • Haslbeck M. & Buchner J.
    Chaperone function of small heat shock proteins.
    in Progress in molecular and subcellular biology, A.-P. Arrigo & W. E. G. Müller, Ed. (Springer Verlag, Berlin / Heidelberg, Germany, 2002), vol. Vol. 28, pp. 37 - 59.
  • Buchner J., Rudolph R. & Lilie H. (2002)
    Intradomain disulfide bonds impede formation of the alternatively folded state of antibody chains.
    J Mol Biol 318, 829 - 836.
  • Buchner J. (2002)
    Introduction: the cellular protein folding machinery.
    Cellular and molecular life sciences : CMLS 59, 1587 - 158.
  • Bell S., Klein C., Müller L., Hansen S. & Buchner J. (2002)
    p53 contains large unstructured regions in its native state.
    J Mol Biol 322, 917 - 927.
  • Bell S., Hansen S. & Buchner J. (2002)
    Refolding and structural characterization of the human p53 tumor suppressor protein.
    Biophys Chem 96, 243 - 257.

2001

  • Thual C., Bousset L., Komar A.A., Walter S., Buchner J., Cullin C. & Melki R. (2001)
    Stability, folding, dimerization, and assembly properties of the yeast prion Ure2p.
    Biochemistry 40, 1764 - 1773.
  • Thies M.J.W., Kammermeier R., Richter K. & Buchner J. (2001)
    The alternatively folded state of the antibody CH3 domain.
    J Mol Biol 309, 1077 - 1085.
  • Richter K., Muschler P., Hainzl O. & Buchner J. (2001)
    Coordinated ATP hydrolysis by the Hsp90 dimer.
    J Biol Chem 276, 33689 - 33696.
  • Richter K. & Buchner J. (2001)
    Hsp90: chaperoning signal transduction.
    J Cell Physiol 188, 281 - 290.
  • Pirkl F., Fischer E., Modrow S. & Buchner J. (2001)
    Localization of the chaperone domain of FKBP52.
    J Biol Chem 276, 37034 - 37041.
  • Pirkl F. & Buchner J. (2001)
    Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40.
    J Mol Biol 308, 795 - 806.
  • Grallert H. & Buchner J. (2001)
    Review: a structural view of the GroE chaperone cycle.
    J Struct Biol 135, 95 - 103.
  • Augustine J.G., de La Calle A., Knarr G., Buchner J. & Frederick C.A. (2001)
    The crystal structure of the Fab fragment of the monoclonal antibody MAK33. Implications for folding and interaction with the chaperone Bip.
    J Biol Chem 276, 3287 - 3294.

2000

  • Weikl T., Muschler P., Richter K., Veit T., Reinstein J. & Buchner J. (2000)
    C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle.
    J Mol Biol 303, 583 - 592.
  • Mayr C., Richter K., Lilie H. & Buchner J. (2000)
    Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties.
    J Biol Chem 275, 34140 - 34146.
  • Mayer M., Kies U., Kammermeier R. & Buchner J. (2000)
    BiP and PDI cooperate in the oxidative folding of antibodies in vitro.
    J Biol Chem 275, 29421 - 29425.
  • Lindner R.A., Carver J.A., Ehrnsperger M., Buchner J., Esposito G., Behlke J., Lutsch G., Kotlyarov A. & Gaestel M. (2000)
    Mouse Hsp25, a small heat shock protein.
    European Journal of Biochemistry 267, 1923 - 1932.
  • Grallert H., Rutkat K. & Buchner J. (2000)
    Limits of protein folding inside GroE complexes.
    J Biol Chem 275, 20424 - 20430.
  • Ehrnsperger M., Gaestel M. & Buchner J.
    Analysis of chaperone properties of small Hsp's.
    in Stress response, Stephen M. Keyse, Ed. (Humana Press, 2000), vol. 99, pp. 421 - 429.

1999

  • Weikl T., Abelmann K. & Buchner J. (1999)
    An unstructured C-terminal region of the Hsp90 co-chaperone p23 is important for its chaperone function.
    J Mol Biol 293, 685 - 691.
  • Thies M.J.W., Mayer J., Augustine J.G., Frederick C.A., Lilie H. & Buchner J. (1999)
    Folding and association of the antibody domain CH3: prolyl isomerization preceeds dimerization.
    J Mol Biol 293, 67 - 79.
  • Scheibel T., Weikl T., Rimerman R., Smith D., Lindquist S. & Buchner J. (1999)
    Contribution of N- and C-terminal domains to the function of Hsp90 in Saccharomyces cerevisiae.
    Mol Microbiol 34, 701 - 713.
  • Scheibel T., Siegmund H.I., Jaenicke R., Ganz P., Lilie H. & Buchner J. (1999)
    The charged region of Hsp90 modulates the function of the N-terminal domain.
    Proc Natl Acad Sci USA 96, 1297 - 302.
  • Rogalla T., Ehrnsperger M., Preville X., Kotlyarov A., Lutsch G., Ducasse C., Paul C., Wieske M., Arrigo A.-P., Buchner J. & Gaestel M. (1999)
    Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation.
    J Biol Chem 274, 18947 - 18956.
  • Knarr G., Modrow S., Todd A., Gething M.-J. & Buchner J. (1999)
    BiP-binding sequences in HIV gp160. Implications for the binding specificity of bip.
    J Biol Chem 274, 29850 - 29857.
  • Haslbeck M., Walke S., Stromer T., Ehrnsperger M., White H.E., Chen S., Saibil H.R. & Buchner J. (1999)
    Hsp26: a temperature-regulated chaperone.
    EMBO J 18, 6744 - 6751.
  • Grallert H. & Buchner J. (1999)
    Analysis of GroE-assisted folding under nonpermissive conditions.
    J Biol Chem 274, 20171 - 20177.
  • Ehrnsperger M., Lilie H., Gaestel M. & Buchner J. (1999)
    The dynamics of Hsp25 quaternary structure. Structure and function of different oligomeric species.
    J Biol Chem 274, 14867 - 14874.
  • Bukau B., Schmid F.X. & Buchner J.
    Molecular chaperones - an overview.
    in Molecular Biology of chaperones, B. Bukau, Ed. (Harwood Academic Publishers, Chur, Switzerland, 1999), pp. 3 - 10.
  • Buchner J. (1999)
    Hsp90 & Co. - a holding for folding.
    Trends Biochem Sci 24, 136 - 141.
  • Bose S., Ehrnsperger M. & Buchner J.
    Mechanisms of ATP-independent vs. ATP-dependent chaperones.
    in Molecular chaperones and folding catalysts: Regulation, cellular function and mechanisms, B. Bukau, Ed. (Harwood Academic Publishers, Chur, Switzerland, 1999), pp. 637 - 660.
  • Beissinger M., Rutkat K. & Buchner J. (1999)
    Catalysis, commitment and encapsulation during GroE-mediated folding.
    J Mol Biol 289, 1075 - 1092.

1998

  • Zavialov A., Benndorf R., Ehrnsperger M., Zav’yalov V., Dudich I., Buchner J. & Gaestel M. (1998)
    The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25.
    Int J Biol Macromol 22, 163 - 173.
  • Veinger L., Diamant S., Buchner J. & Goloubinoff P. (1998)
    The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network.
    J Biol Chem 273, 11032 - 11037.
  • Scheibel T., Weikl T. & Buchner J. (1998)
    Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence.
    Proc Natl Acad Sci USA 95, 1495 - 1499.
  • Scheibel T. & Buchner J. (1998)
    The Hsp90 complex — a super-chaperone machine as a novel drug target.
    Biochemical Pharmacology 56, 675 - 682.
  • Nichtl A., Buchner J., Jaenicke R., Rudolph R. & Scheibel T. (1998)
    Folding and association of β-galactosidase.
    J Mol Biol 282, 1083 - 1091.
  • Grallert H., Rutkat K. & Buchner J. (1998)
    GroEL traps dimeric and monomeric unfolding intermediates of citrate synthase.
    J Biol Chem 273, 33305 - 33310.
  • Ehrnsperger M., Hergersberg C., Wienhues U., Nichtl A. & Buchner J. (1998)
    Stabilization of proteins and peptides in diagnostic immunological assays by the molecular chaperone Hsp25.
    Anal Biochem 259, 218 - 225.
  • Buchner J., Weikl T., Bügl H., Pirkl F. & Bose S.
    Purification of Hsp90 partner proteins Hop/p60, p23, and FKBP52.
    in Methods in Enzymology, Thomas O. Baldwin George H. Lorimer, Ed. (Academic Press, 1998), vol. 290, pp. 418 - 429.
  • Buchner J., Grallert H. & Jakob U.
    Analysis of chaperone function using citrate synthase as nonnative substrate protein.
    in Methods in Enzymology, Thomas O. Baldwin George H. Lorimer, Ed. (Academic Press, 1998), vol. Volume 290, pp. 323 - 338.
  • Buchner J., Ehrnsperger M., Gaestel M. & Walke S.
    Purification and characterization of small heat shock proteins.
    in Methods in Enzymology, Thomas O. Baldwin George H. Lorimer, Ed. (Academic Press, 1998), vol. 290, pp. 339 - 349.
  • Buchner J., Bose S., Mayr C. & Jakob U.
    Purification and characterization of prokaryotic and eukaryotic Hsp90.
    in Methods in Enzymology, Thomas O. Baldwin George H. Lorimer, Ed. (Academic Press, 1998), vol. 290, pp. 409 - 418.
  • Beissinger M. & Buchner J. (1998)
    How chaperones fold proteins.
    Biol Chem 379, 245 - 259.

1997

  • Sparrer H., Rutkat K. & Buchner J. (1997)
    Catalysis of protein folding by symmetric chaperone complexes.
    Proc Natl Acad Sci USA 94, 1096-1100.
  • Sparrer H. & Buchner J. (1997)
    How GroES regulates binding of nonnative protein to GroEL.
    J Biol Chem 272, 14080 - 14086.
  • Scheibel T., Neuhofen S., Weikl T., Mayr C., Reinstein J., Vogel P.D. & Buchner J. (1997)
    ATP-binding properties of human Hsp90.
    J Biol Chem 272, 18608-13.
  • Scheibel T. & Buchner J.
    The Hsp90 family - an overview.
    in Guidebook to molecular chaperones and protein folding catalysts, M.-J. Gething, Ed. (Oxford University Press, Oxford, England, 1997), pp. 147 - 150.
  • Jakob U. & Buchner J.
    Mammalian Hsp90s.
    in Guidebook to molecular chaperones and protein folding catalysts, M.-J. Gething, Ed. (Oxford University Press, Oxford, England, 1997), pp. 269 - 272.
  • Gaestel M., Vierling E. & Buchner J.
    The small Hsps - an overview.
    in Guidebook to molecular chaperones and protein folding catalysts, M.-J. Gething, Ed. (Oxford University Press, Oxford, England 1997), pp. 269 - 272.
  • Gaestel M. & Buchner J.
    Escherichia coli small heat shock proteins IbpA and IbpB.
    in Guidebook to molecular chaperones and protein folding catalysts, M.-J. Gething, Ed. (Oxford University Press, Oxford, England, 1997), pp. 273 - 274.
  • Gaestel M. & Buchner J.
    Small heat shock protein Hsp25 from mouse and rat.
    in Guidebook to molecular chaperones and protein-folding catalysts, M.-J. Gething, Ed. (Oxford University Press, Oxford; New York, 1997), pp. 285 - 287.
  • Ehrnsperger M., Gräber S., Gaestel M. & Buchner J. (1997)
    Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.
    EMBO J 16, 221 - 229.
  • Ehrnsperger M., Gaestel M. & Buchner J.
    Chaperone function of small heat shock proteins and α-crystallin.
    in Molecular chaperones in the life cycle of proteins: structure, function, and mode of action, A. L. Fink & Y. Goto, Ed. (Marcel Dekker, New York, USA, 1997), pp. 533 - 576.

1996

  • Sparrer H., Lilie H. & Buchner J. (1996)
    Dynamics of the GroEL-protein complex: effects of nucleotides and folding mutants.
    J Mol Biol 258, 74 - 87.
  • Jakob U., Scheibel T., Bose S., Reinstein J. & Buchner J. (1996)
    Assessment of the ATP binding properties of Hsp90.
    J Biol Chem 271, 10035 - 10041.
  • Buchner J. (1996)
    Supervising the fold: functional principles of molecular chaperones.
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology 10, 10 - 19.
  • Bose S., Weikl T., Bugl H. & Buchner J. (1996)
    Chaperone function of Hsp90-associated proteins.
    Science 274, 1715 - 1717.

1995

  • Viitanen P.V., Schmidt M., Buchner J., Suzuki T., Vierling E., Dickson R., Lorimer G.H., Gatenby A. & Soll J. (1995)
    Functional characterization of the higher plant chloroplast chaperonins.
    J Biol Chem 270, 18158 - 18164.
  • Seckler R., Buchner J. & Jaenicke R. (1995)
    Welcome to the fold.
    Odyssey 1, 2 - 8.
  • Lilie H., Rudolph R. & Buchner J. (1995)
    Association of antibody chains at different stages of folding: prolyl isomerization occurs after formation of quaternary structure.
    J Mol Biol 248, 190 - 201.
  • Lilie H., Jaenicke R. & Buchner J. (1995)
    Characterization of a quaternary-structured folding intermediate of an antibody Fab-fragment.
    Protein science : a publication of the Protein Society 4, 917-24.
  • Lilie H. & Buchner J. (1995)
    Interaction of GroEL with a highly structured folding intermediate: iterative binding cycles do not involve unfolding.
    Proc Natl Acad Sci USA 92, 8100 - 8104.
  • Lilie H. & Buchner J. (1995)
    Domain interactions stabilize the alternatively folded state of an antibody Fab fragment.
    FEBS Lett 362, 43 - 46.
  • Knarr G., Gething M.-J., Modrow S. & Buchner J. (1995)
    BiP binding sequences in antibodies.
    J Biol Chem 270, 27589 - 27594.
  • Jakob U., Meyer I., Bügl H., André S., Bardwell J.C.A. & Buchner J. (1995)
    Structural organization of procaryotic and eucaryotic Hsp90. Influence of divalent cations on structure and function.
    J Biol Chem 270, 14412 - 1419.
  • Jakob U., Lilie H., Meyer I. & Buchner J. (1995)
    Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo.
    J Biol Chem 270, 7288 - 7294.
  • Gething M.-J., Blond-Elguindi S., Buchner J., Fourie A., Knarr G., Modrow S., Nanu L., Segal M. & Sambrook J. (1995)
    Binding sites for Hsp70 molecular chaperones in natural proteins.
    Cold Spring Harb Symp Quant Biol 60, 417 - 428.

1994

  • Schmidt M., Rutkat K., Rachel R., Pfeifer G., Jaenicke R., Viitanen P.V., Lorimer G.H. & Buchner J. (1994)
    Symmetric complexes of GroE chaperonins as part of the functional cycle.
    Science 265, 656 - 659.
  • Schmidt M., Buchner J., Todd M.J., Lorimer G.H. & Viitanen P.V. (1994)
    On the role of GroES in the chaperonin-assisted folding reaction. Three case studies.
    J Biol Chem 269, 10304 - 10311.
  • Schmidt M., Bücheler U., Kaluza B. & Buchner J. (1994)
    Correlation between the stability of the GroEL-protein ligand complex and the release mechanism.
    J Biol Chem 269, 27964 - 27972.
  • Lilie H., McLaughlin S., Freedman R. & Buchner J. (1994)
    Influence of protein disulfide isomerase (PDI) on antibody folding in vitro.
    J Biol Chem 269, 14290 - 14296.
  • Knauf U., Jakob U., Engel K., Buchner J. & Gaestel M. (1994)
    Stress- and mitogen-induced phosphorylation of the small heat shock protein Hsp25 by MAPKAP kinase 2 is not essential for chaperone properties and cellular thermoresistance.
    EMBO J 13, 54 - 60.
  • Jakob U. & Buchner J. (1994)
    Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones.
    Trends Biochem Sci 19, 205 - 211.

1993

  • Wiech H., Buchner J., Zimmermann M., Zimmermann R. & Jakob U. (1993)
    Hsc70, immunoglobulin heavy chain binding protein, and Hsp90 differ in their ability to stimulate transport of precursor proteins into mammalian microsomes.
    J Biol Chem 268, 7414-7421.
  • Theuer C.P., Buchner J., FitzGerald D. & Pastan I. (1993)
    The N-terminal region of the 37-kDa translocated fragment of Pseudomonas exotoxin A aborts translocation by promoting its own export after microsomal membrane insertion.
    Proc Natl Acad Sci USA 90, 7774 - 7778.
  • Lilie H., Lang K., Rudolph R. & Buchner J. (1993)
    Prolyl isomerases catalyze antibody folding in vitro.
    Protein science : a publication of the Protein Society 2, 1490 - 1496.
  • Jakob U., Gaestel M., Engel K. & Buchner J. (1993)
    Small heat shock proteins are molecular chaperones.
    J Biol Chem 268, 1517 - 1520.
  • Jaenicke R. & Buchner J. (1993)
    From unboiling of an egg to catalysis of folding.
    Chemtracts 4, 1 - 30.

1992

  • Wiech H., Buchner J., Zimmermann R. & Jakob U. (1992)
    Hsp90 chaperones protein folding in vitro.
    Nature 358, 169 - 170.
  • Schmidt M. & Buchner J. (1992)
    Interaction of GroE with an all-beta-protein.
    J Biol Chem 267, 16829 - 16833.
  • Kern G., Schmidt M., Buchner J. & Jaenicke R. (1992)
    Glycosylation inhibits the interaction of invertase with the chaperone GroEL.
    FEBS Lett 305, 203 - 205.
  • Buchner J., Pastan I. & Brinkmann U. (1992)
    A method for increasing the yield of properly folded recombinant fusion proteins: single-chain immunotoxins from renaturation of bacterial inclusion bodies.
    Anal Biochem 205, 263 - 270.
  • Buchner J., Brinkmann U. & Pastan I. (1992)
    Renaturation of a single-chain immunotoxin facilitated by chaperones and protein disulfide isomerase.
    Bio/technology 10, 682 - 685.
  • Brinkmann U., Buchner J. & Pastan I. (1992)
    Independent domain folding of Pseudomonas exotoxin and single-chain immunotoxins: influence of interdomain connections.
    Proc Natl Acad Sci USA 89, 3075 - 3079.
  • Brandsch R., Bichler V., Schmidt M. & Buchner J. (1992)
    GroE dependence of refolding and holoenzyme formation of 6-hydroxy-D-nicotine oxidase.
    J Biol Chem 267, 20844 - 20849.

1991

  • Kiefhaber T., Rudolph R., Kohler H.-H. & Buchner J. (1991)
    Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation.
    Bio/technology 9, 825 - 829.
  • Höll-Neugebauer B., Rudolph R., Schmidt M. & Buchner J. (1991)
    Reconstitution of a heat shock effect in vitro: influence of GroE on the thermal aggregation of .alpha.-glucosidase from yeast.
    Biochemistry 30, 11609-11614.
  • Buchner J., Schmidt M., Fuchs M., Jaenicke R., Rudolph R., Schmid F.X. & Kiefhaber T. (1991)
    GroE facilitates refolding of citrate synthase by suppressing aggregation.
    Biochemistry 30, 1586 - 1591.
  • Buchner J. & Rudolph R. (1991)
    Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli.
    Bio/technology 9, 157 - 162.
  • Buchner J. & Rudolph R. (1991)
    Routes to active proteins from transformed microorganisms.
    Curr Opin Biotechnol 2, 532 - 538.
  • Buchner J., Renner M., Lilie H., Hinz H.-J., Jaenicke R., Kiefhaber T. & Rudolph R. (1991)
    Alternatively folded states of an immunoglobulin.
    Biochemistry 30, 6922 - 6929.

1990

  • Buchner J. & Kiefhaber T. (1990)
    Folding pathway enigma.
    Nature 343, 601 - 602.