Search for recent publications by M.P. Mayer.

Schlecht, R, Erbse, A, Bukau, B, Mayer, MP. Mechanics of Hsp70 chaperones enables differential interaction with client proteins. Nat Struct Mol Biol. (2011) 18, 345-351.

Jaiswal H, Conz C, Otto H, Wölfle T, Fitzke E, Mayer MP, Rospert S.The chaperone network connected to human ribosome-associated complex (mRAC). Mol Cell Biol. (2011) 31, 1160-1173.

Mayer MP. Gymnastics of molecular chaperones. Mol. Cell. (2010) 39, 321-331.

Stankiewicz M, Nikolay R, Rybin V, Mayer MP. CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates. FEBS J. (2010) 277, 3353-3367.

Lou X, Kirchner M, Renard BY, Köthe U, Boppel S, Graf C, Lee CT, Steen JA, Steen H, Mayer MP, Hamprecht FA. Deuteration Distribution Estimation with Improved Sequence Coverage for HX/MS Experiments. Bioinformatics (2010) 26, 1535-1541.

Favaloro V, Vilardi F, Schlecht R, Mayer MP, Dobberstein B. Asna1/TRC40-mediated membrane insertion of tail-anchored proteins. J Cell Sci. (2010) 123(Pt 9):1522-30.

Graf C, Stankiewicz M, Nikolay R, Mayer MP. Insights into the Conformational Dynamics of the E3 Ubiquitin Ligase CHIP in Complex with Chaperones and E2 Enzymes. Biochemistry. (2010) 49, 2121-2129.

Mayer MP. Phosphotyrosine confers client specificity to Hsp90. Mol Cell. (2010) 37, 295-296.

Tsutsumi S, Mollapour M, Graf C, Lee CT, Scroggins BT, Xu W, Haslerova L, Hessling M, Konstantinova AA, Trepel JB, Panaretou B, Buchner J, Mayer MP, Prodromou C, Neckers L. Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain. Nat Struct Mol Biol. (2009) 16, 1141-1147.

Torrado LC, Temmerman K, Müller HM, Mayer MP, Seelenmeyer C, Backhaus R, Nickel W. An intrinsic quality-control mechanism ensures unconventional secretion of fibroblast growth factor 2 in a folded conformation. J Cell Sci. (2009) 122, 3322-3329.

Graf C, Stankiewicz M, Kramer G, Mayer MP. Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine. EMBO J. (2009) 28, 602-613.

Mayer MP, Prodromou C, Frydman J. The Hsp90 mosaic: a picture emerges. Nat Struct Mol Biol (2009) 16, 2-6 .

Rodriguez F, Arsene-Ploetze F, Rist W, Rüdiger S, Schneider-Mergener J, Mayer MP, Bukau B. Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones. Mol Cell (2008) 32, 347-358.

Andreasson, C., Fiaux, J., Rampelt, H., Mayer, M. P., Bukau, B. Hsp110 is a nucleotide-activated exchange factor for Hsp70. J. Biol. Chem. (2008), 283, 8877-8884.

Vogel, M., Mayer, M.P., Bukau, B. Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker. J Biol Chem. (2006), 281, 38705-38711.

Michelsen, K., Mrowiec, T., Duderstadt, K.E., Frey, S., Minor, D.L., Mayer, M.P., Schwappach B. A multimeric membrane protein reveals 14-3-3 isoform specificity in forward transport in yeast. Traffic (2006), 7, 903-916.

Pastore, C., Adinolfi, S., Huynen, M.A., Rybin, V., Martin, S., Mayer, M., Bukau, B., Pastore, A. YfhJ, a molecular adaptor in iron-sulfur cluster formation or a frataxin-like protein? Structure (2006), 14, 857-867.

Rist, W., Graf, C., Bukau, B., and Mayer, M. P. Amide hydrogen exchange reveals conformational changes in Hsp70 chaperones important for allosteric regulation. J Biol Chem. (2006) 281, 16493-16501.

Raviol, H., Sadlish, H., Rodriguez, F., Mayer, M.P., Bukau, B. (2006). Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J. 25, 2510-2518.

Raviol, H., Bukau, B., Mayer, M.P. Human and yeast Hsp110 chaperones exhibit functional differences. FEBS Lett. (2006) 580, 168-174.

Vogel, M., Bukau, B., Mayer, M.P. Allosteric regulation of Hsp70 chaperones by a proline switch. Mol. Cell (2006). 21, 359-367.

Mayer, M.P. (2005) Recruitment of Hsp70 chaperones: a crucial part of viral survival strategies. Rev. Phys. Biochem. Pharmacol. 153:1-46.

Rist, W., F. Rodriguez, T. J. D. Jørgensen, & M. P. Mayer (2005) Analysis of sub-second protein dynamics by amide hydrogen exchange and mass spectrometry using a quenched-flow setup. Protein Sci. 14:626-632.

Rist, W., M. P. Mayer, J.S. Andersen, P. Roepstorff & T. J. D. Jørgensen (2005) Rapid desalting of protein samples for on-line microflow electrospray ionization mass spectrometry. Anal. Biochem. 342:160-162.

Mayer, M.P. & B. Bukau (2005) Hsp70 chaperones: Cellular functions and molecular Mechanism. Cell. Mol. Life Sci. 62:670-684.

Nikolay R., T. Wiederkehr, W. Rist, G. Kramer, M. P. Mayer, & B. Bukau (2004) Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity. J. Biol. Chem. 279:2673-8.

Brehmer, D., C. Gaessler, W. Rist, M. P. Mayer & B. Bukau (2004) Influence of GrpE on the DnaK-substrate interactions. J. Biol. Chem. 279:27957-64.

Mayer, M. P. (2004) Timing the catch. Nat Struct Mol Biol 11:6-8.

Mayer, M. P. & B. Bukau (2004) Regulation of Hsp70 chaperones by cochaperones. In Handbook of Protein Folding, Part II (J. Buchner & T. Kiefhaber, eds.) Wiley/Verlag Chemie, Weinheim, pp 516-562.

Erbse, A., M.P. Mayer & B. Bukau (2004) Mechanism of substrate recognition by Hsp70 chaperones. Biochem. Soc. Trans. 32(Pt 4):617-21.

Jude, F., T. Koehler, P. Branny, K. Perron, M. P. Mayer, R. Comte & C. van Delden (2003) Postranscriptional control of quorum-sensing dependent virulence genes by DksA in Pseudomonas aeruginosa. J. Bacteriol. 185:3558-3566.

Noack, C., F. Prols, A. J. Gamel, W. Rist, M. P. Mayer & B. Brand-Saberi (2003) Revisiting vimentin expression in early chick development. Anat Embryol (Berl). 206:391-7.

Rist, W., T. J. D. Jørgensen, P. Roepstorff, B. Bukau & M. P. Mayer (2003) Mapping temperature induced conformational changes in the E. coli heat shock transcription factor s32 by amide hydrogen exchange. J. Biol. Chem. 278:51415-21.

Mogk, A., M. P. Mayer & E. Deuerling (2002) Mechanism of Proteinfolding: Molekular Chaperones and their Application in Biotechnology. ChemBioChem 3:807-814.

Mayer, M. P., T. Tomoyasu & B. Bukau (2002) Molecular mechanism of Hsp70 chaperones. Tanpakusitu-Kakusan-Kouso 47: 1189-1195.

Mayer, M. P., R. Nikolay & B. Bukau (2002) Aha, another regulator for Hsp90 chaperones. Mol Cell 10:1255-1256.

Roth, S., N. Willcox, R. Rzepka, M. P. Mayer & I. Melchers (2002) Major differences in antigen-processing correlate with a single 71Arg´Lys. substitution in HLA-DR molecules predisposing to rheumatoid arthritis and with their selective interactions with Hsp70 chaperones. J. Immunol. 169:3015-3020.

Kluck, C., H. Patzelt, P. Genevaux, D. Brehmer, W. Rist, J. Schneider-Mergener, B. Bukau & M. P. Mayer (2002) Structur-function analysis of HscC, the Escherichia coli member of a novel subfamily of specialized Hsp70 chaperones. J. Biol. Chem. 277:41060-41069.

Mogk, A., M. P. Mayer & E. Deuerling (2001) Mechanismen der Proteinfaltung: Molekulare Chaperone und ihr biotechnologisches Potential. Biologie in unserer Zeit 31:182-192.

Mayer, M. P., D. Brehmer, C. S. Gaessler & B. Bukau (2001) Hsp70 Chaperone Machines. In A. Horwich (ed.), Advances in Protein Chemistry: Protein Folding in the Cell, vol. 59. Academic Press, San Diego, p. 1-44.

Ang, D., A. Richardson, M. P. Mayer, F. Keppel, H. Krisch & C. Georgopoulos (2001) Pseudo T-even bacteriophage RB49 encodes CocO, a cochaperonin for GroEL, which can substitute for Escherichia coli's GroES and bacteriophage T4's Gp31. J. Biol. Chem. 276:8720-8726.

Brehmer, D., S. Ruediger, C. S. Gässler, D. Klostermeier, L. Packschies, J. Reinstein, M. P. Mayer & B. Bukau (2001) Tuning of Hsp70 chaperone activity by modulation of nucleotide exchange. Nature Struct. Biol. 8:427-432.

Gaessler, C. S., T. Wiederkehr, D. Brehmer, B. Bukau & M. P. Mayer (2001) Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration dependent as positive and negative cofactor. J. Biol. Chem. 276:32538-32544.

Proels, F., M. P. Mayer, P. Czarnecki, M. Ast, O. Renner, H. Kurz, C. S. Gässler & B. Christ (2001) Regulation and subcellular localization of Mdg1 in cell differetiation and stress response. Exp. Cell Res. 269:42-53.

Mayer, M. P., S. Ruediger & B. Bukau (2000) Molecular basis for interactions of DnaK chaperone with substrates. Biol. Chem. 381:877-885.

Mayer, M. P., H. Schroeder, S. Rüdiger, K. Paal, T. Laufen & B. Bukau (2000) Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nature Struct. Biol. 7:586-583.

Ruediger, S., M. P. Mayer, J. Schneider-Mergener & B. Bukau (2000) Modulation of the specificity of the Hsp70 chaperone DnaK by alterating a hydrophobic arch. J. Mol. Biol. 304:245-251.

Mayer, M. P. & B. Bukau (1999) Molecular Chaperones: The busy life of Hsp90. Curr. Biol. 9:R322-R325.

Laufen, T., M. P. Mayer, C. Beisel, D. Klostermeier, J. Reinstein & B. Bukau (1999) Mechanism of reguluation of Hsp70 chaperones by DnaJ co-chaperones. Proc. Natl. Acad. Sci. USA. 96:5452-5457.

Mayer, M. P., T. Laufen, K. Paal, J. S. McCarty & B. Bukau (1999) Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance. J. Mol. Biol. 289:1131-1144.

Mayer, M. P. & B. Bukau (1998) Hsp70 Chaperone systems: Diversity of Cellular Functions and Mechanism of Action. Biol. Chem. 379:261-268.

Gässler, C. S., A. Buchberger, T. Laufen, M. P. Mayer, H. Schröder, A. Valencia & B. Bukau (1998) Mutations in the DnaK chaperone affecting interaction with the DnaJ co-chaperone. Proc. Natl. Acad. Sci. USA. 95:15229-15234.

Missiakas, D., M. P. Mayer, M. Lemaire, C. Georgopoulos & S. Raina (1997) Modulation of the Escherichia coli sE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins. Mol. Microbiol. 24:355-371.

Mayer, M. P. (1995) A new set of useful cloning and expression vectors derived from pBlueScript. Gene. 163:41-46.

Mayer, M. P., G. D. Prestwich, J. M. Dolence, P. D. Bond, H. Y. Wu & C. D. Poulter (1993) Proteinfarnesyltransferase - Production in Escherichia coli and immunoaffinity purification of the heterodimer from Saccharomyces cerevisiae. Gene. 132:41-47.

Mayer, M. P., F. M. Hahn, D. J. Stillman & C. D. Poulter (1992) Disruption and mapping of IDI, the gene for the isopentenyl diphosphate isomerase in Saccharomyces cerevisiae. Yeast. 8:743-748.

Mayer, M. P., V. Nievelstein & P. Beyer (1992) Purification and characterization of a NADPH dependent oxidoreductase from chromoplasts of Narcissus pseudonarcissus L.: a redox-mediator possibly involved in carotene desaturation. Plant Physiol. Biochem. 30:389-398.

Mayer, M. P., P. Beyer & H. Kleinig (1990) Quinone compounds are able to replace oxygen as terminal electron acceptor in phytoene desaturation in Narcissus pseudonarcissus. Eur. J. Biochem. 191:359-363.

Schafer, W. R., C. E. Trueblood, C.-C. Yang, M. P. Mayer, S. Rosenberg, C. D. Poulter, S. H. Kim & J. Rine (1990) Enzymatic coupling of cholesterol intermediates to a mating pheromone precursor and to the ras protein. Science. 249:1133-1139.

Beyer, P., M. Mayer & H. Kleinig (1989) Molecular oxygen and the state of geometric isomerism of intermediates are essential in the carotene desaturation and cyclization reactions in daffodil chromoplasts. Eur. J. Biochem. 184:141-150.

Mayer, M. P., D. L. Bartlett, P. Beyer & H. Kleinig (1989) The in vitro mode of action of bleaching herbicides on the desaturation of 15-cis-phytoen and cis-z-carotene in isolated daffodil chromoplasts. Pest. Biochem. Physiol. 34:111-117.