Search for recent publications by M.P. Mayer.

Mayer, M.P. The Hsp70-Chaperone Machines in Bacteria. Front Mol Biosci. (2021) 8:694012. doi: 10.3389/fmolb.2021.694012. Review.

Kmiecik, S.W., Mayer, M.P. Molecular mechanisms of heat shock factor 1 regulation. Trends Biochem Sci. (2021) 19:S0968-0004(21)00230-9. doi: 10.1016/j.tibs.2021.10.004. Review.

Diehl, M., Roling, L., Rohland, L., Weber, S., Cyrklaff, M., Sanchez, C.P., Beretta, C.A., Simon, C.S., Guizetti, J., Hahn, J., Schulz, N., Mayer, M.P, Przyborski, J.M. Co-chaperone involvement in knob biogenesis implicates host-derived chaperones in malaria virulence. PLoS Pathog. (2021) 17:e1009969. doi: 10.1371/journal.ppat.1009969.

Kmiecik, S.W., Drzewicka, K., Melchior, F., Mayer, M.P. Heat shock transcription factor 1 is SUMOylated in the activated trimeric state. J Biol Chem. (2021) 296:100324. doi: 10.1016/j.jbc.2021.100324.

Diestelkoetter-Bachert, P., Beck, R., Reckmann, I., Hellwig, A., Garcia-Saez, A., Zelman-Hopf, M., Hanke, A., Nunes Alves, A., Wade, R.C., Mayer, M.P., Wieland, F. Structural characterization of an Arf dimer interface: molecular mechanism of Arf-dependent membrane scission. FEBS Lett. (2020) 594:2240-2253. doi: 10.1002/1873-3468.13808.

Malsam, J., Bärfuss, S., Trimbuch, T., Zarebidaki, F., Sonnen, A.F., Wild, K., Scheutzow, A., Rohland, L., Mayer, M.P., Sinning, I., Briggs, J.A.G., Rosenmund, C., Söllner, T.H. Complexin Suppresses Spontaneous Exocytosis by Capturing the Membrane-Proximal Regions of VAMP2 and SNAP25. Cell Rep. (2020) 32:107926. doi: 10.1016/j.celrep.2020.107926.

Serlidaki, D., van Waarde, M.A.W.H., Rohland, L., Wentink, A.S., Dekker, S.L., Kamphuis, M.J., Boertien, J.M., Brunsting, J.F., Nillegoda, N.B., Bukau, B., Mayer, M.P., Kampinga, H.H., Bergink, S. Functional diversity between HSP70 paralogs caused by variable interactions with specific co-chaperones. J Biol Chem. (2020) 295:7301-7316. doi: 10.1074/jbc.RA119.012449.

Kmiecik, S.W., Le Breton, L., Mayer, M.P. Feedback regulation of heat shock factor 1 (Hsf1) activity by Hsp70-mediated trimer unzipping and dissociation from DNA. EMBO J. (2020) 39:e104096. doi: 10.15252/embj.2019104096.

Mayer, M.P., Gierasch, L.M. Correction: Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones. J Biol Chem. (2020) 295:288. doi: 10.1074/jbc.AAC119.012167.

Amin-Wetzel, N., Neidhardt, L., Yan, Y., Mayer, M.P., Ron, D. Unstructured regions in IRE1alpha specify BiP-mediated destabilisation of the luminal domain dimer and repression of the UPR. Elife. (2019) 8:e50793. doi: 10.7554/eLife.50793.

Kampinga, H.H., Mayer, M.P., Mogk, A. Protein quality control: from mechanism to disease. EMBO Workshop, Costa de la Calma (Mallorca), Spain, April 28 - May 03, 2019. Cell Stress Chaperones. (2019) 24:1013-1026. doi: 10.1007/s12192-019-01040-9.

Rosenzweig, R., Nillegoda, N.B., Mayer, M.P., Bukau, B. The Hsp70 chaperone network. Nat Rev Mol Cell Biol (2019) doi: 10.1038/s41580-019-0133-3.

Maurer, M., Linder, D., Franke, K.B., Jäger, J., Taylor, G., Gloge, F., Gremer, S., Le Breton, L., Mayer, M.P., Weber-Ban, E., Carroni, M., Bukau, B., Mogk, A. Toxic Activation of an AAA+ Protease by the Antibacterial Drug Cyclomarin A. Cell Chem Biol (2019) pii: S2451-9456(19)30177-1. doi: 10.1016/j.chembiol.2019.05.008.

Boysen, M., Kityk, R., Mayer, M.P. Hsp70- and Hsp90-Mediated Regulation of the Conformation of p53 DNA Binding Domain and p53 Cancer Variants. Mol Cell (2019) 74:831-843.e4. doi: 10.1016/j.molcel.2019.03.032.

Morán Luengo, T., Mayer, M.P., Rüdiger, S.G.D. The Hsp70-Hsp90 Chaperone Cascade in Protein Folding. Trends Cell Biol (2019) 29:164-177.

Kampinga, H.H., Andreasson, C., Barducci, A., Cheetham, M.E., Cyr, D., Emanuelsson, C., Genevaux, P., Gestwicki, J.E., Goloubinoff, P., Huerta-Cepas, J,, Kirstein, J., Liberek, K., Mayer, M.P., Nagata, K., Nillegoda, N.B., Pulido, P., Ramos, C., De Los Rios, P., Rospert, S., Rosenzweig, R., Sahi, C., Taipale, M., Tomiczek, B., Ushioda, R., Young, J.C., Zimmermann, R., Zylicz, A., Zylicz, M., Craig, E.A., Marszalek, J. Function, evolution, and structure of J-domain proteins. Cell Stress Chaperones (2019) 24:7-15. doi: 10.1007/s12192-018-0948-4.

Mayer, M.P., Gierasch, L.M. Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones. J Biol Chem (2019) 294:2085-2097. doi: 10.1074/jbc.REV118.002810.

Xu, W., Beebe, K., Chavez, J.D., Boysen, M., Lu, Y., Zuehlke, A.D., Keramisanou, D., Trepel, J.B., Prodromou, C., Mayer, M.P., Bruce, J.E., Gelis, I., Neckers, L. Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1. Nat Commun (2019) 10:2574. doi: 10.1038/s41467-019-10463-y.

Wen, Y., Zhou, X., Lu, M., He, M., Tian, Y., Liu, L., Wang, M., Tan, W., Deng, Y., Yang, X., Mayer, M.P., Zou, F., Chen, X. Bclaf1 promotes angiogenesis by regulating HIF-1α transcription in hepatocellular carcinoma. Oncogene (2019) 38:1845-1859. doi: 10.1038/s41388-018-0552-1.

Zhou, X., Wen, Y., Tian, Y., He, M., Ke, X., Huang, Z., He, Y., Liu, L., Scharf, A., Lu, M., Zhang, G., Deng, Y., Yan, Y., Mayer, M.P., Chen, X., Zou, F. Heat Shock Protein 90α-Dependent B-Cell-2-Associated Transcription Factor 1 Promotes Hepatocellular Carcinoma Proliferation by Regulating MYC Proto-Oncogene c-MYC mRNA Stability. Hepatology (2019) 69:1564-1581.doi: 10.1002/hep.30172.

Mayer MP. Intra-molecular pathways of allosteric control in Hsp70s. Philos Trans R Soc Lond B Biol Sci (2018) 373(1749). pii: 20170183. doi: 10.1098/rstb.2017.0183.

Morán Luengo T, Kityk R, Mayer MP, Rüdiger SGD. Hsp90 Breaks the Deadlock of the Hsp70 Chaperone System. Mol Cell (2018) 70:545-552.e9. doi: 10.1016/j.molcel.2018.03.028.

Kityk R, Kopp J, Mayer MP. Molecular Mechanism of J-Domain-Triggered ATP Hydrolysis by Hsp70 Chaperones. Mol Cell (2018) 69:227-237.e4. doi: 10.1016/j.molcel.2017.12.003. (full paper).

Gowda NKC, Kaimal JM, Kityk R, Daniel C, Liebau J, Öhman M, Mayer MP, Andréasson C. Nucleotide Exchange Factors for Hsp70 Chaperones. Nat Struct Mol Biol (2018) 25(1):83-89. doi: 10.1038/s41594-017-0008-2.

Grousl T, Ungelenk S, Miller S, Ho CT, Khokhrina M, Mayer MP, Bukau B, Mogk A. A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins. J Cell Biol (2018) pii: jcb.201708116. doi: 10.1083/jcb.201708116.

Zemva J, Fink CA, Fleming TH, Schmidt L, Loft A, Herzig S, Knieß RA, Mayer M, Bukau B, Nawroth PP, Tyedmers J. Hormesis enables cells to handle accumulating toxic metabolites during increased energy flux. Redox Biol (2018) 13:674-686. doi: 10.1016/j.redox.2017.08.007.

Rampelt H, Mayer MP, Bukau B. Nucleotide Exchange Factors for Hsp70 Chaperones. Methods Mol Biol (2018) 1709:179-188. doi: 10.1007/978-1-4939-7477-1_13.

Mudholkar K, Fitzke E, Prinz C, Mayer MP, Rospert S. The Hsp70 homolog Ssb affects ribosome biogenesis via the TORC1-Sch9 signaling pathway. Nat Commun (2017) 8:937. doi: 10.1038/s41467-017-00635-z.

Wruck, F, Avellaneda, MJ, Koers, EJ, Minde, DP, Mayer, MP, Kramer, G, Mashaghi, A, Tans, SJ. Protein Folding Mediated by Trigger Factor and Hsp70: New Insights from Single-Molecule Approaches. J Mol Biol (2017) doi: 10.1016/j.jmb.2017.09.004.

Döring, K, Ahmed, N, Riemer, T, Suresh, HG, Vainshtein, Y, Habich, M, Riemer, J, Mayer, MP, O'Brien, EP, Kramer, G, Bukau, B. Profiling Ssb-Nascent Chain Interactions Reveals Principles of Hsp70-Assisted Folding. Cell 170:298-311.e20. doi: 10.1016/j.jmb.2017.03.025.

Bascos, NAD, Mayer, MP, Bukau, B, Landry, SJ. The Hsp40 J-domain modulates Hsp70 conformation and ATPase activity with a semi-elliptical spring. Protein Sci (2017) 26:1838-1851. doi: 10.1002/pro.3223.

Daturpalli, S, Knieß, RA, Lee, CT, Mayer, MP. Large rotation of the N-terminal domain of Hsp90 is important for interaction with some but not all client proteins. J Mol Biol (2017) 429:1406-1423. doi: 10.1016/j.jmb.2017.03.025.

Nguyen MT, Knieß RA, Daturpalli S, Le Breton L, Ke X, Chen X, Mayer MP. Isoform-Specific Phosphorylation in Human Hsp90ß Affects Interaction with Clients and the Cochaperone Cdc37. J Mol Biol (2017) 429:732-752. doi: 10.1016/j.jmb.2017.01.011.

Knieß, RA, Mayer, MP. The oxidation state of the cytoplasmic glutathione redox system does not correlate with replicative lifespan in yeast. NPJ Aging and Mechanisms of Disease (2016) doi:10.1038/npjamd.2016.28

Hanebuth MA, Kityk R, Fries SJ, Jain A, Kriel A, Albanese V, Frickey T, Peter C, Mayer MP, Frydman J, Deuerling E. Multivalent contacts of the Hsp70 Ssb contribute to its architecture on ribosomes and nascent chain interaction. Nat Commun (2016) 7:13695. doi: 10.1038/ncomms13695.

Ungelenk S, Moayed F, Ho CT, Grousl T, Scharf A, Mashaghi A, Tans S, Mayer MP, Mogk A, Bukau B. Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding. Nat Commun (2016) 7:13673. doi: 10.1038/ncomms13673.

Le Breton L, Mayer MP. A model for handling cell stress. Elife (2016) pii: e22850. doi: 10.7554/eLife.22850.

La Venuta, G, Wegehingel, S, Sehr, P, Müller, HM, Dimou, E, Steringer, JP, Grotwinkel, M, Hentze, N, Mayer, MP, Will, DW, Uhrig, U, Lewis, JD, Nickel, W. Small molecule inhibitors targeting Tec kinase block unconventional secretion of fibroblast growth factor 2. J Biol Chem (2016) 291:17787-803. doi: 10.1074/jbc.M116.729384.

Mashaghi A, Bezrukavnikov S, Minde DP, Wentink AS, Kityk R, Zachmann-Brand B, Mayer MP, Kramer G, Bukau B, Tans SJ. Alternative modes of client binding enable functional plasticity of Hsp70. J Biol Chem (2016) Nature 539:448-451. doi: 10.1038/nature20137.

Hentze, N., Le Breton, L., Wiesner, J., Kempf, G., Mayer, M.P. Molecular mechanism of thermosensory function of human heat shock transcription factor Hsf1. (2016) Elife 5:e11576. pii: e11576. doi: 10.7554/eLife.11576.

Kityk R, Vogel M, Schlecht R, Bukau B, Mayer MP. Pathways of allosteric regulation in Hsp70 chaperones. Nat Commun (2015) 6:8308. doi: 10.1038/ncomms9308.

Gao X, Carroni M, Nussbaum-Krammer C, Mogk A, Nillegoda NB, Szlachcic A, Guilbride DL, Saibil HR, Mayer MP, Bukau B. Mol Cell (2015) 59:781-793.

Nillegoda NB, Kirstein J, Szlachcic A, Berynskyy M, Stank A, Stengel F, Arnsburg K, Gao X, Scior A, Aebersold R, Guilbride DL, Wade RC, Morimoto RI, Mayer MP, Bukau B. Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation. Nature (2015) 524:247-251.

Dunn DM, Woodford MR, Truman AW, Jensen SM, Schulman J, Caza T, Remillard TC, Loiselle D, Wolfgeher D, Blagg BS, Franco L, Haystead TA, Daturpalli S, Mayer MP, Trepel JB, Morgan RM, Prodromou C, Kron SJ, Panaretou B, Stetler-Stevenson WG, Landas SK, Neckers L, Bratslavsky G, Bourboulia D, Mollapour M. c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells. Cell Rep (2015) 12:1006-1018.

Zeitler M, Steringer JP, Müller HM, Mayer MP, Nickel W. HIV-Tat Forms Phosphoinositide Dependent Membrane Pores Implicated in Unconventional Protein Secretion. J Biol Cell (2015) 290:21976-21984.

Mayer MP, Le Breton, L. Hsp90: Breaking the Symmetry. Mol Cell (2015) 58:8-20.

Hassan AQ, Kirby CA, Zhou W, Schuhmann T, Kityk R, Kipp DR, Baird J, Chen J, Chen Y, Chung F, Hoepfner D, Movva NR, Pagliarini R, Petersen F, Quinn C, Quinn D, Riedl R, Schmitt EK, Schitter A, Stams T, Studer C, Fortin PD, Mayer MP, Sadlish H. The novolactone natural product disrupts the allosteric regulation of hsp70. Chem Biol (2015) 22:87-97.

Parisotto D, Pfau M, Scheutzow A, Wild K, Mayer MP, Malsam J, Sinning I, Sollner TH. An extended helical conformation in domain 3a of the SM protein Munc18-1 provides a template for SNARE (soluble N-ethylmaleimide sensitive factor attachment protein receptor) complex assembly. J Biol Chem (2014) 289:9639-9650.

Hentze N, Mayer MP. Analyzing protein dynamics using hydrogen exchange mass spectrometry. J Vis Exp (2013) 81: e50839.

Mashaghi A, Kramer G, Lamb DC, Mayer MP, Tans SJ. Chaperone Action at the Single-Molecule Level. Chem Rev (2013) 114:660-676.

Lee CT, Malzahn E, Brunner M, Mayer MP. Light-Induced Differences in Conformational Dynamics of the Circadian Clock Regulator VIVID. J Mol Biol (2013) 426:601-610.

Schlecht R, Scholz SR, Dahmen H, Wegener A, Sirrenberg C, Musil D, Bomke J, Eggenweiler HM, Mayer MP, Bukau B. Functional analysis of hsp70 inhibitors. PLoS One (2013) 8: e78444. -> Correction

Mayer, MP. Hsp70 chaperone dynamics and molecular mechanism. Trends Biochem Sci (2013) 38, 507-514.

Sandikci A, Gloge F, Martinez M, Mayer MP, Wade R, Bukau B, Kramer G. Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding. Nat Struct Mol Biol (2013) 20, 843-850.

Kityk R, Kopp J, Sinning I, Mayer MP. Structure and Dynamics of the ATP-Bound Open Conformation of Hsp70 Chaperones. Mol Cell (2012) 48:863-874. pii: S1097-2765(12)00823-4.

Ratzke C, Nguyen MN, Mayer MP, Hugel T. From a Ratchet Mechanism to Random Fluctuations Evolution of Hsp90's Mechanochemical Cycle. J Mol Biol (2012) 423:462-471.

Zuiderweg ER, Bertelsen EB, Rousaki A, Mayer MP, Gestwicki JE, Ahmad A. Allostery in the Hsp70 Chaperone Proteins. Top Curr Chem (2012) 328, 99-153.

Mayer, MP. The unfolding story of a redox chaperone. Cell (2012) 148, 843-844.

Lee, CT, Graf, C, Mayer, FJ, Richter SM, Mayer, MP. Dynamics of the regulation of Hsp90 by the co-chaperone Sti1. EMBO J. (2012) 31, 1518-1528.

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.