Publications

Mandl, F.A., Kirsch, V.C., Ugur, I., Kunold, E., Vomacka, J., Fetzer, C., Schneider, S., Richter, K. Fuchs, T.M., Antes, I., Sieber, S.A. Natural-Product-Inspired Aminoepoxybenzoquinones Kill Members of the Gram-Negative Pathogen Salmonella by Attenuating Cellular Stress Response. (2016), Angewandte Chemie accepted, Manuscript.

Zierer, B.K., Rübbelke, M., Tippel, F., Madl, T., Schopf, F.H., Rutz, D., Richter, K., Sattler, M. & Buchner, J Importance of cycle timing for the function of the molecular chaperone Hsp90. (2016), Nat Struct Mol Biol 23, 1020-1028.

Rehn, A. Moroni, E., Zierer, B.K., Tippel, F., Morra, G., John, C., Richter, K., Colombo, G. & Buchner, J. Allosteric regulation points control the conformational dynamics in the molecular chaperone Hsp90. (2016), J. Mol.Biol. 428, 4559-4571.

Eckl, J., Daake, M., Schwartz, S. & Richter, K. Nucleotide-free sB-Raf is preferentially bound by Hsp90 and Cdc37 in vitro. (2016), J. Mol. Biol. Epub ahead of print, S0022-2836.

Papsdorf, K., Sima, S., Richter, G. & Richter, K. Construction and evaluation of yeast expression networks based on database-guided predictions. (2016), Microbial Cell accepted manuscript, no pages yet.

Anvarian, Z., Nojima, H., van Kappel, E.C., Madl, T., Spit, M., Viertler, M., Jordens, I., Low, T.Y., van Scherpenzeel, R.C., Kuper, I., Richter, K., Heck, A.J., Boelens, R., Vincent, J.P., Rüdiger, S.G.& Maurice, M.M. Axin cancer mutants form nanoaggregates to rewire the Wnt signaling network. (2016), Nat Struct Mol Biol. 23, 324-332.

Haslbeck, V., Eckl, J.M., Drazic, A., Rutz, D.A., Lorenz, O.R., Zimmermann, K., Kriehuber, T., Lindemann, C., Madl, T. & Richter, K. The activity of protein phosphatase 5 towards native clients is modulated by the middle- and C-terminal domains of Hsp90. (2015), Sci Rep. Nov 23, no pages yet.

Pahl, A., Lakemeyer, M., Vielberg, M.T., Hackl, M.W., Vomacka, J., Korotov, V.S., Stein, M.L., Fetzer, C., Lorenz-Baath, K., Richter, K., Waldmann, H., Groll, M. & Sieber, S.A. Reversible inhibitors Arrest ClpP in a defined Conformational State that can be Revoked by ClpX Association. (2015), Angew Chem Int Ed Engl. 54, 15892-6.

Eckl,J.M., Scherr,M.J., Freiburger, L., Daake, M.A., Sattler, M. & Richter, K. Hsp90-Cdc37 complexes with protein kinases form cooperatively with multiple distinct interaction sites. (2015), J Biol Chem. Oct 28, in press.

Papsdorf, K., Kaiser, C.J., Drazic, A., Grötzinger, S.W., Haeßner, C., Eisenreich, W. & Richter, K. Polyglutamine toxicity in yeast induces metabolic alterations and mitochondrial defects. (2015), BMC Genomics Sept 3, no page yet.

Haslbeck, V., Drazic, A., Eckl, J.M., Alte, F., Helmuth, M., Popowicz, G., Schmidt, W., Braun, F., Weiwad, M., Fischer, G., Gemmecker, G., Sattler, M., Groll, M. & Richter, K. Selective activators of protein üphosphatase 5 trget the auto-inhibitory mechanism. (2015), Biosci Rep. Apr 20, no page yet320.

Richter, K. daf-41/p23: A Small Protein Heating Up Lifespan Regulation. (2015), PLoS Genet. Jul 6, no pages yet.

Zhao, H., Ghirlando, R., Alfonso, C., Arisaka, F.......Richter, K........, Wubben, J.M. & Schuck, P. A multilaboratory comparison of calibration accuracy and the performance of external references in analytical ultracentrifugation. (2015), PLoS One May 21, no pages yet.

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. & Bcuhner, J. Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules. (2015), Nat Commun. Apr 8, no pages yet.

Gersch, M., Famulla, K., Dahmen, M., Göbl, C., Malik, I., Richter, K., Korotkov, V.S., Sass, P., Rübsamen-Schaeff, H., Madl, T., Brötz-Oesterhelt, H. & Sieber, S.A. AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control. (2015), Nat Commun. 6, 6320.

Röhl, A., Tippel, F., Bender, E., Schmid, A.B., Richter, K., Madl, T. & Buchner, J. Hop/Sti1 phosphorylation inhibits its co-chaperone function. (2015), EMBO Rep. 16, 240-9.

Jahn, M., Rehn, A., Pelz, B., Hellenkamp, B., Richter, K., Rief, M., Buchner, J. & Hugel T. The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function. (2014), Proc Natl Acad Sci U S A. 111, 17881-6.

Zierer, B.K., Weiwad, M., Rübbelke, M., Freiburger, L., Fischer, G., Lorenz, O.R., Sattler, M., Richter, K. & Buchner, J. Artificial accelerators of the molecular chaperone Hsp90 facilitate rate-limiting conformational transitions. (2014), Angew Chem Int Ed Engl. 53, 12257-62.

Papsdorf, K. & Richter, K. Protein folding, misfolding and quality control: the role of molecular chaperones. (2014), Essays Biochem. 56, 53-68. PDF (submitted manuscript)

Papsdorf, K., Sacherl, J. & Richter, K. The balanced regulation of Hsc70 by DNJ-13 and UNC-23 is required for muscle functionality. (2014), J Biol Chem. 289, 25250-25261.

Eckl, J.M., Drazic, A., Rutz, D.A. & Richter, K. Nematode Sgt1-homologue D1054.3 binds open and closed conformations of Hsp90 via distinct binding sites. (2014), Biochemistry 53, 2505-2514.

Eckl, J.M. & Richter, K. Functions of the Hsp90 chaperone system: lifting client proteins to new heights. (2014), Int J Biochem Mol Biol. 4, 157-165.

Haslbeck V., Eckl J.M., Kaiser C.J., Papsdorf K., Hessling M. & Richter, K. Chaperone-interacting TPR proteins in Caenorhabditis elegans.. (2013), J Mol Biol. 425, 2922-2939.

Guisbert, E., Czyz, D.M., Richter, K. & McMullen, P.D. & Morimoto, R.I. Identification of a tissue-selective heat shock response regulatory network. (2013), PlOS Genet., 2013 April 9 [Epub ahead of print].

Eckl, J.M., Rutz, D.A., Haslbeck, V., Zierer, B.K., Reinstein, J., & Richter, K. Cdc37 (Cell division cycle 37) restricts Hsp90 (Heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites.(2013), J. Biol. Chem., 2013 April 8 [Epub ahead of print].

Kaiser, C.J., Grötzinger, S.W,, Eckl, J.W., Papsdorf, K., Jordan, S. & Richter, K. A network of genes connects polyglutamine toxicity to ploidy control in yeast. (2013), Nat Commun 4, 1571.

Li, J., Zoldak, G., Kriehuber, T., Soroka, J., Schmid, F.X., Richter, K. & Buchner, J. Unique Proline-Rich Domain Regulates the Chaperone Function of AIPL1. (2013), Biochemistry , March 13 [Epub ahead of print].

Li, J., Richter, K., Reinstein, J. & Buchner, J. Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle. (2013), Nat Struct Mol Biol 20, 326-331.

Eckert, T., Link, S., Le, D.T., Sobczak, J.P., Giesecke, A., Richter, K. & Woehlke, G. (2012), J. Biol. Chem., 2012 May 27 [Epub ahead of print].

Richter, K., Schubert, D. & Urbanke, C. (2012), Analytische Ultrazentrifugation in Bioanalytik, Edts: Lottspeich und Engels, Springer Spektrum, Berlin.

Sun, L., Edelmann, F., Kaiser, C.J.O., Gaiser, A. & Richter, K. The lid domain of Caenorhabditis elegans Hsc70 influences ATP turnover, cofactor binding and protein folding activity. (2012), PLoS ONE 7, e33980 Epub 2012 Mar 29.

Schmid, A.B., Lagleder, S., Gräwert, M.A., Röhl, A., Hagn, F., Wandinger, S.K., Cox, M.B., Demmer, O. Richter, K., Groll, M., Kessler, H. & Buchner, J. The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop. (2012), EMBO 31, 1506-1517.

Soroka, J., Wandinger, S.K., Schreiber, T., Mäusbacher, N., Richter, K., Daub, H. & Buchner, J. Conformational switching of the molecular chaperone Hsp90 via regulated phosphorylation. (2012), Mol Cell 45, 517-528.

Haslbeck, V., Kaiser, C.J. & Richter, K. Hsp90 in non-mammalian metazoan model systems. (2012), Biochim. Biophys. Acta 1823, 712-721.

Gaiser, A.M., Kaiser, C.J., Haslbeck, V. & Richter, K. Downregulation of the Hsp90 system causes defects in muscle cells of Caenorhabditis elegans. (2011), PLoS ONE 6, e25485 Epub 2011 Sep 28.

Hagn, F., Lagleder, S., Retzlaff, M., Rohrberg, J., Demmer, O., Richter, K., Buchner, J. & Kessler, H. Structural analysis of the interaction netween Hsp90 and the tumor suppressor protein p53. (2011), Nat Struct Mol Biol. 18, 1086-1093

Richter, K. & Buchner, J. Closing in on the Hsp90 chaperone client relationship. (2011), Structure 4, 445-446

Tochowicz, A., Goettig, P., Evans, R., Visse, R., Shitomi, Y., Palmisano, R., Ito, N., Richter, K., Maskos, K., Franke, D., Svergun, D., Nagase, H., Bode, W. & Itoh, Y. The dimer interface of the MT1-MMP hemopexin domain: crystal structure and biological functions. (2011), J. Biol. Chem. 286, 7587-7600

Li, J., Richter, K. & Buchner J. Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle. (2011), Nat Struct Mol Biol. 18, 61-66.

Ehrmann, A., Richter, K., Busch, F., Reimann, J., Albers, S.V. & Sterner, R. Ligand-induced formation of a transient tryptophan synthase complex with αββ subunit stoichiometry. (2010), Biochemistry 49, 10842-10853.

Richter, K., Haslbeck, M. & Buchner J. The heat shock response: life on the verge of death. (2010), Mol Cell. 40, 253-266.

Gaiser, A.M., Kretzschmar, A. & Richter, K. Cdc37-Hsp90 complexes are responsive to nucleotide-induced conformational changes and binding of further cofactors. (2010), J Biol Chem. 285, 40921-40932.

Retzlaff, M., Hagn, F., Mitschke, L., Hessling, M., Gugel, F., Kessler, H., Richter, K. & Buchner, J. Asymmetric activation of the hsp90 dimer by its cochaperone aha1. (2010), Mol Cell. 12, 344-354.

Szostkiewicz I., Richter, K., Kepka, M., Demmel, S., Ma, Y., Korte, A., Assaad, F.F., Christmann, A. & Grill, E. Closely related receptor complexes differ in their ABA selectivity and sensitivity (2010), Plant J. 61, 25-35.

Müller M., Richter, K., Heuck, A., Kremmer, E., Buchner, J., Jansen, R.P. & Niessing, D. Formation of She2p tetramers is required for mRNA binding, mRNP assembly, and localization (2009), RNA 15, 2002-2012.

Kaplon, T.M., Michnik, A., Drzazga, Z., Richter, K., Kochman, M. & Ozyhar, A. The rod-shaped conformation of Starmaker (2009), Biochim. Biophys. Acta 1794, 1616-1624.

Gaiser, A.M., Brandt, F. & Richter, K. The Non-canonical Hop Protein from Caenorhabditis elegans exerrts essential functions and forms binary complexes with either Hsc70 or Hsp90 (2009), J. Mol. Biol. 391, 621-634.

Hainzl, O., Lapina, M.C., Buchner, J. & Richter, K. The charged linker is an important regulator of Hsp90 function (2009), J. Biol. Chem. 284, 22559-22567.

Hessling, M., Richter, K. & Buchner, J. Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90 (2009), Nat. Struct. Mol. Biol. 16, 287-293

Franzmann, T.M. & Richter, K. Analytische Ultrazentrifugation und Fluoreszenzdetektion (2009), Biospektrum 15, 47-49.

Wandinger, S.K., Richter, K. & Buchner, J. The Hsp90 chaperone machinery (2008), J. Biol. Chem. 283, 18473-18477

Richter K., Soroka, J., Salniak, L., Leskovar, A., Hessling, M., Reinstein, J. & Buchner, J.  Conserved conformational changes during the ATPase-cycle of human Hsp90 (2008), J. Biol. Chem. 283, 17757-17765.

Richter K., Hendershot L. & Freeman B.C. The cellular world according to Hsp90 (2007), Nat. Struct. Mol. Biol. 14, 90-94.

Richter K., Reinstein J, Buchner J. A Grp on the Hsp90 mechanism (2007), Mol Cell. 28, 177-179

Heuck A., Du T.G., Jellbauer S., Richter K., Kruse C., Jaklin S., Müller M., Buchner J., Jansen R.P., Niessing D. Monomeric myosin V uses two binding regions for the assembly of stable translocation complexes (2007), Proc. Natl. Acad. Sci. U S A. 104, 19778-19783.

Richter K. & Buchner J. Hsp90: Twist and Fold! (2006), Cell 127, 251-253.

Richter K., Moser S., Hagn F., Friedrich R., Hainzl O., Schlee S., Haller K., Reinstein J., Kessler H. & Buchner J., Intrinsic inhibition of the Hsp90 ATPase activity (2006), J. Biol. Chem. 281, 11301-11311.

Panizzi P., Friedrich R., Fuentes-Prior P., Richter K., Bock P.E. & Bode W. Fibrinogen substrate recognition by staphylocoagulase.(pro)thrombin complexes (2006), J. Biol. Chem. 281, 1179-1187.

Franzmann T.M., Wuhr M., Richter K., Walter S. & Buchner J., The activation mechanism of Hsp26 does not require dissociation of the oligomer (2005), J. Mol. Biol. 350, 1083-1093.

Richter K., Meinlschmidt, B. & Buchner J. Hsp90: From dispensable heat-shock protein to global player (2005) in Protein Folding Handbook, Edts: Buchner & Kiefhaber, Wiley-VCH, Weinheim, New York.

Richter K., Walter S. & Buchner J., The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle (2004). J. Mol. Biol. 342, 1403-1413.

Hainzl O., Wegele H., Richter K. & Buchner J. Cns1 is an activator of the Ssa1 ATPase activity (2004). J. Biol. Chem. 279, 23267-23273.

Stromer T., Fischer E., Richter K., Haslbeck M. & Buchner J. 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 (2004). J. Biol. Chem. 279, 11222-11228.

Grimminger V., Richter K., Imhof A., Buchner J. & Walter S. The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104 (2004). J. Biol. Chem. 279, 7378-7383.

Friedrich R., Panizzi P., Fuentes-Prior P., Richter K., Verhamme I., Anderson P.J., Kawabata S., Huber R., Bode W. & Bock P.E. Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation (2003). Nature 425, 535-539.

Dehner A., Furrer J., Richter K., Schuster I., Buchner J. & Kessler H. NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol (2003). Chembiochem 4, 870-877.

Richter K., Muschler P., Hainzl O., Reinstein J. & Buchner J. Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle (2003). J. Biol. Chem. 278, 10328-10333.

Richter K., Reinstein J. & Buchner J. N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle (2002), J. Biol. Chem. 277, 44905-44910.

Tochtrop G.P., Richter K., Tang C., Toner J.J., Covey D.F. & Cistola D.P. Energetics by NMR: site-specific binding in a positively cooperative system (2002), Proc. Natl. Acad. Sci. U. S. A. 99, 1847-1852.

Richter K. & Buchner J. Hsp90: chaperoning signal transduction (2001), J. Cell. Physiol. 188, 281-290.

Richter K., Muschler P., Hainzl O. & Buchner J. Coordinated ATP hydrolysis by the Hsp90 dimer (2001), J. Biol. Chem. 276, 33689-33696.

Thies M.J., Kammermeier R., Richter K. & Buchner J. The alternatively folded state of the antibody C(H)3 domain (2001). J. Mol. Biol. 309, 1077-1085.

Weikl T., Muschler P., Richter K., Veit T., Reinstein J. & Buchner J. C-terminal regions of Hsp90 are important for trapping the nucleotide during the ATPase cycle (2000). J. Mol. Biol. 303, 583-592.

 Mayr C., Richter K., Lilie H. & Buchner J. Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties (2000). J. Biol. Chem. 275, 34140-34146.