Related references
Note: Only part of the references are listed.Comprehensive structural characterization of the human AAA plus disaggregase CLPB in the apo- and substrate-bound states reveals a unique mode of action driven by oligomerization
Damu Wu et al.
PLOS BIOLOGY (2023)
Chaperones directly and efficiently disperse stress-triggered biomolecular condensates
Haneul Yoo et al.
MOLECULAR CELL (2022)
Human mitochondrial AAA plus ATPase SKD3/CLPB assembles into nucleotide-stabilized dodecamers
Zachary Spaulding et al.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2022)
Unique structural features govern the activity of a human mitochondrial AAA plus disaggregase, Skd3
Ryan R. Cupo et al.
CELL REPORTS (2022)
DeepEMhancer: a deep learning solution for cryo-EM volume post-processing
Ruben Sanchez-Garcia et al.
COMMUNICATIONS BIOLOGY (2021)
Neutropenia and intellectual disability are hallmarks of biallelic and de novo CLPB deficiency
Saskia B. Wortmann et al.
GENETICS IN MEDICINE (2021)
Highly accurate protein structure prediction with AlphaFold
John Jumper et al.
NATURE (2021)
J-domain proteins promote client relay from Hsp70 during tail-anchored membrane protein targeting
Hyunju Cho et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2021)
Stairway to translocation: AAA plus motor structures reveal the mechanisms of ATP-dependent substrate translocation
Stephanie N. Gates et al.
PROTEIN SCIENCE (2020)
The biogenesis of mitochondrial intermembrane space proteins
Ruairidh Edwards et al.
BIOLOGICAL CHEMISTRY (2020)
Amino and PEG-amino graphene oxide grids enrich and protect samples for high-resolution single particle cryo-electron microscopy
Feng Wang et al.
JOURNAL OF STRUCTURAL BIOLOGY (2020)
Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein
Rahmi Imamoglu et al.
NATURE COMMUNICATIONS (2020)
CLPB (caseinolytic peptidase B homolog), the first mitochondrial protein refoldase associated with human disease
Dagmara Mroz et al.
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS (2020)
Skd3 (human ClpB) is a potent mitochondrial protein disaggregase that is inactivated by 3-methylglutaconic aciduria-linked mutations
Ryan R. Cupo et al.
ELIFE (2020)
Human CLPB forms ATP-dependent complexes in the mitochondrial intermembrane space
Indhujah Thevarajan et al.
INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY (2020)
Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase
James Shorter et al.
COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY (2019)
The Chaperonin TRiC/CCT Associates with Prefoldin through a Conserved Electrostatic Interface Essential for Cellular Proteostasis
Daniel Gestaut et al.
CELL (2019)
The Hsp70 chaperone network
Rina Rosenzweig et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2019)
Structural basis for substrate gripping and translocation by the ClpB AAA plus disaggregase
Alexandrea N. Rizo et al.
NATURE COMMUNICATIONS (2019)
Structural Basis of Mitochondrial Scaffolds by Prohibitin Complexes: Insight into a Role of the Coiled-Coil Region
Takahiro Yoshinaka et al.
ISCIENCE (2019)
Quantitative mass imaging of single biological macromolecules
Gavin Young et al.
SCIENCE (2018)
Cryo-EM structures of the TMEM16A calcium-activated chloride channel
Shangyu Dang et al.
NATURE (2017)
Ratchet-like polypeptide translocation mechanism of the AAA plus disaggregase Hsp104
Stephanie N. Gates et al.
SCIENCE (2017)
Novel CLPB mutation in a patient with 3-methylglutaconic aciduria causing severe neurological involvement and congenital neutropenia
Ayca Kiykim et al.
CLINICAL IMMUNOLOGY (2016)
Molecular mechanisms of protein aggregation from global fitting of kinetic models
Georg Meisl et al.
NATURE PROTOCOLS (2016)
ConSurf 2016: an improved methodology to estimate and visualize evolutionary conservation in macromolecules
Haim Ashkenazy et al.
NUCLEIC ACIDS RESEARCH (2016)
The GroEL-GroES Chaperonin Machine: A Nano-Cage for Protein Folding
Manajit Hayer-Hartl et al.
TRENDS IN BIOCHEMICAL SCIENCES (2016)
Small heat shock proteins sequester misfolding proteins in near-native conformation for cellular protection and efficient refolding
Sophia Ungelenk et al.
NATURE COMMUNICATIONS (2016)
CLPB Mutations Cause 3-Methylglutaconic Aciduria, Progressive Brain Atrophy, Intellectual Disability, Congenital Neutropenia, Cataracts, Movement Disorder
Saskia B. Wortmann et al.
AMERICAN JOURNAL OF HUMAN GENETICS (2015)
Bi-allelic CLPB mutations cause cataract, renal cysts, nephrocalcinosis and 3-methylglutaconic aciduria, a novel disorder of mitochondrial protein disaggregation
Marta Kanabus et al.
JOURNAL OF INHERITED METABOLIC DISEASE (2015)
Disruption of CLPB is associated with congenital microcephaly, severe encephalopathy and 3-methylglutaconic aciduria
Jose-Mario Capo-Chichi et al.
JOURNAL OF MEDICAL GENETICS (2015)
Metabolic and Chaperone Gene Loss Marks the Origin of Animals: Evidence for Hsp104 and Hsp78 Chaperones Sharing Mitochondrial Enzymes as Clients
Albert J. Erives et al.
PLOS ONE (2015)
Potentiated Hsp104 Variants Antagonize Diverse Proteotoxic Misfolding Events
Meredith E. Jackrel et al.
CELL (2014)
Molecular Chaperone Functions in Protein Folding and Proteostasis
Yujin E. Kim et al.
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 82 (2013)
Structure and Allostery of the Chaperonin GroEL
Helen R. Saibil et al.
JOURNAL OF MOLECULAR BIOLOGY (2013)
Unraveling the Mechanism of Protein Disaggregation Through a ClpB-DnaK Interaction
Rina Rosenzweig et al.
SCIENCE (2013)
Operational Plasticity Enables Hsp104 to Disaggregate Diverse Amyloid and Nonamyloid Clients
Morgan E. DeSantis et al.
CELL (2012)
Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA plus disaggregase at aggregate surfaces
Fabian Seyffer et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2012)
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Paul D. Adams et al.
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2010)
Oxidation and Reduction of Cysteines in the Intermembrane Space of Mitochondria: Multiple Facets of Redox Control
Johannes M. Herrmann et al.
ANTIOXIDANTS & REDOX SIGNALING (2010)
Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation
Tobias Haslberger et al.
BIOCHEMISTRY AND CELL BIOLOGY (2010)
The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase
Sandeep K. Sharma et al.
NATURE CHEMICAL BIOLOGY (2010)
`The HSP70 chaperone machinery: J proteins as drivers of functional specificity
Harm H. Kampinga et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2010)
CryoEM structure of Hsp104 and its mechanistic implication for protein disaggregation
Sukyeong Lee et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2010)
A facile method for expression and purification of the Alzheimer's disease-associated amyloid beta-peptide
Dominic M. Walsh et al.
FEBS JOURNAL (2009)
Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions
James Shorter et al.
EMBO JOURNAL (2008)
Protein disaggregation by the AAA plus chaperone ClpB involves partial threading of looped polypeptide segments
Tobias Haslberger et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2008)
Consensus design of repeat proteins
P Forrer et al.
CHEMBIOCHEM (2004)
Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides
C Schlieker et al.
FEBS LETTERS (2004)
Substrate recognition by the AAA plus chaperone ClpB
C Schlieker et al.
NATURE STRUCTURAL & MOLECULAR BIOLOGY (2004)
Coot:: model-building tools for molecular graphics
P Emsley et al.
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2004)
Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB
J Weibezahn et al.
CELL (2004)
Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
PB Rosenthal et al.
JOURNAL OF MOLECULAR BIOLOGY (2003)
Share Paper
