Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase
Published 2019 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase
Authors
Keywords
-
Journal
Nature Communications
Volume 10, Issue 1, Pages -
Publisher
Springer Science and Business Media LLC
Online
2019-06-03
DOI
10.1038/s41467-019-10150-y
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation
- (2019) Sukyeong Lee et al. Cell Reports
- Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase
- (2019) James Shorter et al. Cold Spring Harbor Perspectives in Biology
- More than Just a Phase: Prions at the Crossroads of Epigenetic Inheritance and Evolutionary Change
- (2018) Anupam K. Chakravarty et al. JOURNAL OF MOLECULAR BIOLOGY
- Malaria parasite translocon structure and mechanism of effector export
- (2018) Chi-Min Ho et al. NATURE
- ATP hydrolysis-coupled peptide translocation mechanism of Mycobacterium tuberculosis ClpB
- (2018) Hongjun Yu et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Structure of Calcarisporiella thermophila Hsp104 Disaggregase that Antagonizes Diverse Proteotoxic Misfolding Events
- (2018) Karolina Michalska et al. STRUCTURE
- FUS inclusions disrupt RNA localization by sequestering kinesin-1 and inhibiting microtubule detyrosination
- (2017) Kyota Yasuda et al. JOURNAL OF CELL BIOLOGY
- MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
- (2017) Shawn Q Zheng et al. NATURE METHODS
- cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
- (2017) Ali Punjani et al. NATURE METHODS
- Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104
- (2017) Stephanie N. Gates et al. SCIENCE
- Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing
- (2017) Cristina Puchades et al. SCIENCE
- The AAA ATPase Vps4 binds ESCRT-III substrates through a repeating array of dipeptide-binding pockets
- (2017) Han Han et al. eLife
- Structure of a AAA+ unfoldase in the process of unfolding substrate
- (2017) Zev A Ripstein et al. eLife
- Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase
- (2017) Célia Deville et al. Science Advances
- Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104
- (2016) Elizabeth A. Sweeny et al. JOURNAL OF MOLECULAR BIOLOGY
- Gctf: Real-time CTF determination and correction
- (2016) Kai Zhang JOURNAL OF STRUCTURAL BIOLOGY
- Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation
- (2016) Adam L Yokom et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation
- (2016) Adam L Yokom et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Structural basis for the disaggregase activity and regulation of Hsp104
- (2016) Alexander Heuck et al. eLife
- Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2
- (2016) Dari Kimanius et al. eLife
- Disparate Mutations Confer Therapeutic Gain of Hsp104 Function
- (2015) Meredith E. Jackrel et al. ACS Chemical Biology
- Escherichia coliClpB is a non-processive polypeptide translocase
- (2015) Tao Li et al. BIOCHEMICAL JOURNAL
- Atomic-accuracy models from 4.5-Å cryo-electron microscopy data with density-guided iterative local refinement
- (2015) Frank DiMaio et al. NATURE METHODS
- Sequence composition of disordered regions fine-tunes protein half-life
- (2015) Susan Fishbain et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- ClpB N-terminal domain plays a regulatory role in protein disaggregation
- (2015) Rina Rosenzweig et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Sequence composition of disordered regions fine-tunes protein half-life
- (2015) Susan Fishbain et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Stochastic but Highly Coordinated Protein Unfolding and Translocation by the ClpXP Proteolytic Machine
- (2014) Juan Carlos Cordova et al. CELL
- Potentiated Hsp104 Variants Antagonize Diverse Proteotoxic Misfolding Events
- (2014) Meredith E. Jackrel et al. CELL
- Reversing deleterious protein aggregation with re-engineered protein disaggregases
- (2014) Meredith E Jackrel et al. CELL CYCLE
- Potentiated Hsp104 variants suppress toxicity of diverse neurodegenerative disease-linked proteins
- (2014) M. E. Jackrel et al. Disease Models & Mechanisms
- ClpB chaperone passively threads soluble denatured proteins through its central pore
- (2014) Yosuke Nakazaki et al. GENES TO CELLS
- Robust and accurate prediction of residue–residue interactions across protein interfaces using evolutionary information
- (2014) Sergey Ovchinnikov et al. eLife
- Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation
- (2014) Marta Carroni et al. eLife
- Quantifying the local resolution of cryo-EM density maps
- (2013) Alp Kucukelbir et al. NATURE METHODS
- Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency
- (2013) Ting Zhang et al. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
- Unraveling the Mechanism of Protein Disaggregation Through a ClpB-DnaK Interaction
- (2013) R. Rosenzweig et al. SCIENCE
- High-Resolution Comparative Modeling with RosettaCM
- (2013) Yifan Song et al. STRUCTURE
- Operational Plasticity Enables Hsp104 to Disaggregate Diverse Amyloid and Nonamyloid Clients
- (2012) Morgan E. DeSantis et al. CELL
- DnaK Chaperone-dependent Disaggregation by Caseinolytic Peptidase B (ClpB) Mutants Reveals Functional Overlap in the N-terminal Domain and Nucleotide-binding Domain-1 Pore Tyrosine
- (2012) Shannon M. Doyle et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- RELION: Implementation of a Bayesian approach to cryo-EM structure determination
- (2012) Sjors H.W. Scheres JOURNAL OF STRUCTURAL BIOLOGY
- A tightly regulated molecular toggle controls AAA+ disaggregase
- (2012) Yuki Oguchi et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Structure and function of the AAA+ nucleotide binding pocket
- (2011) Petra Wendler et al. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
- Allosteric Communication between the Nucleotide Binding Domains of Caseinolytic Peptidase B
- (2011) José Ángel Fernández-Higuero et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Features and development ofCoot
- (2010) P. Emsley et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- PHENIX: a comprehensive Python-based system for macromolecular structure solution
- (2010) Paul D. Adams et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Synergistic Cooperation between Two ClpB Isoforms in Aggregate Reactivation
- (2009) Maria Nagy et al. JOURNAL OF MOLECULAR BIOLOGY
- Gly-Ala Repeats Induce Position- and Substrate-specific Regulation of 26 S Proteasome-dependent Partial Processing
- (2008) Chrysoula Daskalogianni et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Diverse Pore Loops of the AAA+ ClpX Machine Mediate Unassisted and Adaptor-Dependent Recognition of ssrA-Tagged Substrates
- (2008) Andreas Martin 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
- Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding
- (2008) Andreas Martin et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
Add your recorded webinar
Do you already have a recorded webinar? Grow your audience and get more views by easily listing your recording on Peeref.
Upload NowAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started