M
Matthias P. Mayer
Researcher at Heidelberg University
Publications - 167
Citations - 15809
Matthias P. Mayer is an academic researcher from Heidelberg University. The author has contributed to research in topics: Chaperone (protein) & Protein folding. The author has an hindex of 62, co-authored 166 publications receiving 13680 citations. Previous affiliations of Matthias P. Mayer include University of Freiburg & German Cancer Research Center.
Papers
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Journal ArticleDOI
Hsp70 chaperones: cellular functions and molecular mechanism.
Matthias P. Mayer,Bernd Bukau +1 more
TL;DR: This work has shown that for specific tasks the Hsp70 cycle is coupled to the action of other chaperones, such as Hsp90 and Hsp100, and this ATPase cycle is controlled by co-chaperones of the family of J-domain proteins, which target H Sp70s to their substrates, and by nucleotide exchange factors, which determine the lifetime of the HSp70-substrate complex.
Journal ArticleDOI
The Hsp70 chaperone network
TL;DR: Recent advances that have increased the understanding of the molecular mechanisms and working principles of the Hsp70 network are described, and new opportunities for the development of chemical compounds that modulate disease-related HSp70 activities are offered.
Journal ArticleDOI
Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones
Thomas Laufen,Matthias P. Mayer,Christian Beisel,Dagmar Klostermeier,Axel Mogk,Jochen Reinstein,Bernd Bukau +6 more
TL;DR: This paper showed that DnaJ stimulates ATP hydrolysis by Escherichia coli Hsp70, DnaK, very efficiently to > 1000-fold, but only if present at high (micromolar) concentration.
Journal ArticleDOI
Hsp70 chaperone dynamics and molecular mechanism.
TL;DR: Recent insights into the structure and mechanism of Hsp70s are discussed, shedding light on the molecular mechanism by which Hsp80s assist protein folding and suggesting that Hsp 70s exist in at least two conformational states.
Journal ArticleDOI
Multistep mechanism of substrate binding determines chaperone activity of Hsp70
TL;DR: In this article, the authors analyzed mutants of DnaK, an Hsp70 homolog, altered in key residues of its substrate binding domain and found that the conformational changes in the alpha-helical lid and the beta-domain caused the opening of the substrate binding cavity.