M P Mayer
Affiliation: University of Heidelberg
- Hsp90: breaking the symmetryMatthias P Mayer
Zentrum für Molekulare Biologie der Universität Heidelberg ZMBH, DKFZ ZMBH Alliance, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany Electronic address
Mol Cell 58:8-20. 2015....
- Functional analysis of Hsp70 inhibitorsRainer Schlecht
Zentrum für Molekulare Biologie der Universität Heidelberg ZMBH, DKFZ ZMBH Alliance, Heidelberg, Germany
PLoS ONE 8:e78443. 2013..Compound PES interacts with the SBD of Hsp70 in an unspecific, detergent-like fashion, under the conditions tested. None of the two inhibitors investigated was isoform-specific. ..
- Hsp70 chaperone dynamics and molecular mechanismMatthias P Mayer
Zentrum für Molekulare Biologie der Universität Heidelberg ZMBH, DKFZ ZMBH Alliance, Heidelberg, Germany Electronic address
Trends Biochem Sci 38:507-14. 2013..In this review recent insights into the structure and mechanism of Hsp70s are discussed. ..
- The unfolding story of a redox chaperoneMatthias P Mayer
Zentrum fur Molekulare Biologie der Universitat Heidelberg, Heidelberg, Germany
Cell 148:843-4. 2012..In this issue, Reichmann et al. demonstrate how a destabilized linker region of the bacterial chaperone Hsp33 prevents aggregation of a denatured protein by stabilizing structural elements...
- Gymnastics of molecular chaperonesMatthias P Mayer
Zentrum für Molekulare Biologie der Universität Heidelberg ZMBH, DKFZ ZMBH Allianz, Heidelberg, Germany
Mol Cell 39:321-31. 2010..In order to do so, they progress through complex conformational cycles themselves. In this review, I discuss the diverse conformational dynamics of the ATP-dependent chaperones of the Hsp60, Hsp70, Hsp90, and Hsp100 families...
- Phosphotyrosine confers client specificity to Hsp90Matthias P Mayer
Zentrum fur Molekulare Biologie der Universitat Heidelberg, DKFZ ZMBH Alliance, Heidelberg 69120, Germany
Mol Cell 37:295-6. 2010..In this issue of Molecular Cell, Mollapour et al. (2010) report a new tyrosine phosphorylation site in Hsp90, which is essential for Hsp90's interaction with a subset of its client proteins, notably protein kinases...
- Recruitment of Hsp70 chaperones: a crucial part of viral survival strategiesM P Mayer
Zentrum fur Molekulare Biologie, Universitat Heidelberg, Im Neuenheimer Feld 282, 69120, Heidelberg, Germany
Rev Physiol Biochem Pharmacol 153:1-46. 2005..This review focuses on the function of Hsp70 chaperones at the different stages of the viral life cycle emphasizing mechanistic aspects...
- Hsp70 chaperones: cellular functions and molecular mechanismM P Mayer
Zentrum für Molekulare Biologie ZMBH, Universitat Heidelberg, Im Neuenheimer Feld 282, 69120, Heidelberg, Germany
Cell Mol Life Sci 62:670-84. 2005..Additional co-chaperones fine-tune this chaperone cycle. For specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100...
- Mechanism of substrate recognition by Hsp70 chaperonesA Erbse
Zentrum für Molekulare Biologie Heidelberg, Universitat Heidelberg, Im Neuenheimer Feld 282, D 69120 Heidelberg, Germany
Biochem Soc Trans 32:617-21. 2004..In the present study, we review the molecular details of the mechanism behind substrate recognition by Hsp70 proteins...
- Upregulation of the cochaperone Mdg1 in endothelial cells is induced by stress and during in vitro angiogenesisF Prols
Institute of Anatomy II, Albert Ludwigs University, Freiburg, 79104, Germany
Exp Cell Res 269:42-53. 2001..These data suggest that Mdg1 is involved in the control of cell cycle arrest taking place during terminal cell differentiation and under stress conditions...
- Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactorC S Gassler
, , 79104 Freiburg, Germany
J Biol Chem 276:32538-44. 2001..Bag-1M accelerated ATP-triggered substrate release by Hsc70/Hsp70. We propose that Bag-1M acts as substrate discharging factor for Hsc70 and Hsp70...
- Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchangeD Brehmer
Institut fur Biochemie und Molekularbiologie, Albert Ludwigs Universitat Freiburg, Hermann Herder Str 7, D 79104 Freiburg, Germany
Nat Struct Biol 8:427-32. 2001..These subfamilies show strong differences in nucleotide dissociation and interaction with the exchange factors GrpE and Bag-1...
- Pseudo-T-even bacteriophage RB49 encodes CocO, a cochaperonin for GroEL, which can substitute for Escherichia coli's GroES and bacteriophage T4's Gp31D Ang
Departement de Biochimie Medicale, Centre Medical Universitaire, 1 rue Michel Servet, CH 1211 Geneve 4, Switzerland
J Biol Chem 276:8720-6. 2001..Both the CocO wild type and epsilon22 proteins have been purified and shown in vitro to assist GroEL in the refolding of denatured citrate synthase...
- Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic archS Rudiger
Institut fur Biochemie und Molekularbiologie, Hermann Herder Str 7, Universitat Freiburg, D 79104, Germany
J Mol Biol 304:245-51. 2000..This finding is of particular interest, since of all the residues of the substrate-binding cavity that contact bound substrate, only the arch-forming residues show significant variation within the Hsp70 family...
- Modulation of the Escherichia coli sigmaE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteinsD Missiakas
Centre National de Recherche Scientifique, LIDSM, Marseille, France
Mol Microbiol 24:355-71. 1997..In contrast, RseC is an inner membrane protein that positively modulates sigma(E) activity. Most of these protein-protein interactions were verified in vivo using the yeast two-hybrid system...