Matthias P. Mayer

[Molecular mechanism of Hsp70 chaperones].

Structure-function analysis of HscC, the Escherichia coli member of a novel subfamily of specialized Hsp70 chaperones.

Mechanisms of protein folding: molecular chaperones and their application in biotechnology.

Major differences in antigen-processing correlate with a single Arg71<-->Lys substitution in HLA-DR molecules predisposing to rheumatoid arthritis and with their selective interactions with 70-kDa heat shock protein chaperones.

Aha, another regulator for hsp90 chaperones.

Revisiting vimentin expression in early chick development.

Posttranscriptional control of quorum-sensing-dependent virulence genes by DksA in Pseudomonas aeruginosa.

Mapping temperature-induced conformational changes in the Escherichia coli heat shock transcription factor sigma 32 by amide hydrogen exchange.

Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity.

Timing the catch.

Influence of GrpE on DnaK-substrate interactions.

Analysis of subsecond protein dynamics by amide hydrogen exchange and mass spectrometry using a quenched-flow setup.

Rapid desalting of protein samples for on-line microflow electrospray ionization mass spectrometry.

Human and yeast Hsp110 chaperones exhibit functional differences.

Allosteric regulation of Hsp70 chaperones by a proline switch.

Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation.

Modeling Hsp70-mediated protein folding.

Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.

A multimeric membrane protein reveals 14-3-3 isoform specificity in forward transport in yeast.

Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker.

Human heat shock protein 70 enhances tumor antigen presentation through complex formation and intracellular antigen delivery without innate immune signaling.

Functional characterization of the atypical Hsp70 subunit of yeast ribosome-associated complex.

Dynamics of trigger factor interaction with translating ribosomes.

Hsp110 is a nucleotide-activated exchange factor for Hsp70.

Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones.

Impaired interdomain communication in mitochondrial Hsp70 results in the loss of inward-directed translocation force.

The Hsp90 mosaic: a picture emerges.

Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine.

An intrinsic quality-control mechanism ensures unconventional secretion of fibroblast growth factor 2 in a folded conformation.

Hsp90 charged-linker truncation reverses the functional consequences of weakened hydrophobic contacts in the N domain.

Insights into the conformational dynamics of the E3 ubiquitin ligase CHIP in complex with chaperones and E2 enzymes.

Phosphotyrosine confers client specificity to Hsp90.

Asna1/TRC40-mediated membrane insertion of tail-anchored proteins.

Deuteration distribution estimation with improved sequence coverage for HX/MS experiments.

CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates.

Gymnastics of molecular chaperones.

The chaperone network connected to human ribosome-associated complex.

Mechanics of Hsp70 chaperones enables differential interaction with client proteins.

Lipids trigger a conformational switch that regulates signal recognition particle (SRP)-mediated protein targeting.

Nucleotide exchange factors for Hsp70 chaperones.

Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity.

Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity.

Dynamics of the regulation of Hsp90 by the co-chaperone Sti1.

The unfolding story of a redox chaperone.

Allostery in the Hsp70 chaperone proteins.

From a ratchet mechanism to random fluctuations evolution of Hsp90's mechanochemical cycle.

Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones.

Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding.

Chaperone Action at the Single-Molecule Level.

Hsp70 chaperone dynamics and molecular mechanism.

Light-Induced Differences in Conformational Dynamics of the Circadian Clock Regulator VIVID.

Functional analysis of hsp70 inhibitors.