Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–8 of 8 results
Advanced filters: Author: Martin Haslbeck Clear advanced filters
  • Oligomers of human αA-crystallin are characterized structurally via a hybrid approach, combining cryo-EM, cross-linking/mass spectrometry, NMR and modeling, providing insight into their dynamic behavior and heterogeneity and revealing that oxidized oligomers can also act as chaperones.

    • Christoph J. O. Kaiser
    • Carsten Peters
    • Sevil Weinkauf
    Research
    Nature Structural & Molecular Biology
    Volume: 26, P: 1141-1150
  • Small heat shock proteins (sHsps) form large spherical assemblies and their regulation is not well understood. Here, the authors provide insights into the mechanism of Hsp26 activation by characterising phospho-mimetic mutants of yeast Hsp26. They present cryo-EM structures of the wild-type Hsp26 40mer and its phospho-mimetic mutants that reveal the location of the thermosensor in the oligomer, and the authors also show that the thermosensor domain is targeted by phosphorylation, which relieves the intrinsic inhibition of chaperone activity.

    • Moritz Mühlhofer
    • Carsten Peters
    • Johannes Buchner
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-14
  • Biochemical and biophysical analyses of eye lenses from mouse strains that develop cataract due to mutations in α-, β-, or γ-crystallin proteins reveal that the mutant protein levels are largely reduced, but other crystallin proteins, including α-crystallins, precipitate.

    • Philipp W. N. Schmid
    • Nicole C. H. Lim
    • Johannes Buchner
    Research
    Nature Structural & Molecular Biology
    Volume: 28, P: 143-151
  • A systematic analysis of the proteostasis network of secreted proteins in Caenorhabditis elegans identifies numerous regulators of protein homeostasis outside the cell, and highlights the contribution of extracellular proteostasis to host defence.

    • Ivan Gallotta
    • Aneet Sandhu
    • Della C. David
    Research
    Nature
    Volume: 584, P: 410-414
  • It is unclear how unassembled secretory pathway proteins are discriminated from misfolded ones. Here the authors combine biophysical and cellular experiments to study the folding of heterodimeric interleukin 23 and describe how ER chaperones recognize unassembled proteins and aid their assembly into protein complexes while preventing the premature degradation of unassembled units.

    • Susanne Meier
    • Sina Bohnacker
    • Matthias J. Feige
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-12