Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding

Widespread Proteome Remodeling and Aggregation in Aging C. elegans

(2015) Dirk M. Walther et al.   CELL

Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition

(2015) S. B. Miller et al.   EMBO JOURNAL

Spatially Organized Aggregation of Misfolded Proteins as Cellular Stress Defense Strategy

(2015) Stephanie B.M. Miller et al.   JOURNAL OF MOLECULAR BIOLOGY

A First Line of Stress Defense: Small Heat Shock Proteins and Their Function in Protein Homeostasis

(2015) Martin Haslbeck et al.   JOURNAL OF MOLECULAR BIOLOGY

Protein aggregates are associated with replicative aging without compromising protein quality control

(2015) Juha Saarikangas et al.   eLife

Small heat-shock proteins: important players in regulating cellular proteostasis

(2014) Teresa M. Treweek et al.   CELLULAR AND MOLECULAR LIFE SCIENCES

Proteostasis impairment in protein-misfolding and -aggregation diseases

(2014) Mark S. Hipp et al.   TRENDS IN CELL BIOLOGY

Small Heat Shock Protein IbpB Acts as a Robust Chaperone in Living Cells by Hierarchically Activating Its Multi-type Substrate-binding Residues

(2013) Xinmiao Fu et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

An Unusual Dimeric Small Heat Shock Protein Provides Insight into the Mechanism of This Class of Chaperones

(2013) Eman Basha et al.   JOURNAL OF MOLECULAR BIOLOGY

Reshaping of the conformational search of a protein by the chaperone trigger factor

(2013) Alireza Mashaghi et al.   NATURE

Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress

(2013) Stéphanie Escusa-Toret et al.   NATURE CELL BIOLOGY

Lysine-specific chemical cross-linking of protein complexes and identification of cross-linking sites using LC-MS/MS and the xQuest/xProphet software pipeline

(2013) Alexander Leitner et al.   Nature Protocols

Dissecting Heterogeneous Molecular Chaperone Complexes Using a Mass Spectrum Deconvolution Approach

(2012) Florian Stengel et al.   CHEMISTRY & BIOLOGY

False discovery rate estimation for cross-linked peptides identified by mass spectrometry

(2012) Thomas Walzthoeni et al.   NATURE METHODS

Alternative bacterial two-component small heat shock protein systems

(2012) A. Bepperling et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT

(2012) Alexander Leitner et al.   STRUCTURE

Hsp42 is required for sequestration of protein aggregates into deposition sites inSaccharomyces cerevisiae

(2011) Sebastian Specht et al.   JOURNAL OF CELL BIOLOGY

Independent evolution of the core domain and its flanking sequences in small heat shock proteins

(2010) Thomas Kriehuber et al.   FASEB JOURNAL

Cellular strategies for controlling protein aggregation

(2010) Jens Tyedmers et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

Quaternary dynamics and plasticity underlie small heat shock protein chaperone function

(2010) F. Stengel et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Widespread Protein Aggregation as an Inherent Part of Aging in C. elegans

(2010) Della C. David et al.   PLOS BIOLOGY

Structure and Mechanism of Protein Stability Sensors: Chaperone Activity of Small Heat Shock Proteins

(2009) Hassane S. Mchaourab et al.   BIOCHEMISTRY

Substrate binding site flexibility of the small heat shock protein molecular chaperones

(2009) N. Jaya et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Insights into Small Heat Shock Protein and Substrate Structure during Chaperone Action Derived from Hydrogen/Deuterium Exchange and Mass Spectrometry

(2008) Guilong Cheng et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Distinct Activities of Escherichia coli Small Heat Shock Proteins IbpA and IbpB Promote Efficient Protein Disaggregation

(2008) Elżbieta Ratajczak et al.   JOURNAL OF MOLECULAR BIOLOGY

Activation of the Chaperone Hsp26 Is Controlled by the Rearrangement of Its Thermosensor Domain

(2008) Titus M. Franzmann et al.   MOLECULAR CELL

Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation

(2008) Peter Tessarz et al.   MOLECULAR MICROBIOLOGY

Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity

(2008) C. Andreasson et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Chaperone-dependent amyloid assembly protects cells from prion toxicity

(2008) P. M. Douglas et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA