ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structural basis for intersubunit signaling in a protein disaggregating machine.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
28 citing papers in PubMed.
- Deciphering the mechanism and function of Hsp100 unfoldases from protein structure.Biochemical Society transactions · 2022Article
- Structural and mechanistic insights into Hsp104 function revealed by synchrotron X-ray footprinting.The Journal of biological chemistry · 2020Article
- Insights into the mechanism and regulation of the CbbQO-type Rubisco activase, a MoxR AAA+ ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A History of Molecular Chaperone Structures in the Protein Data Bank.International journal of molecular sciences · 2019Review
- Mitochondrial AAA proteases: A stairway to degradation.Mitochondrion · 2019Review
- Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104.Science (New York, N.Y.) · 2017Article
- Covalently linked HslU hexamers support a probabilistic mechanism that links ATP hydrolysis to protein unfolding and translocation.The Journal of biological chemistry · 2017Article
- Assessing heterogeneity in oligomeric AAA+ machines.Cellular and molecular life sciences : CMLS · 2017Review
- Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions.Frontiers in molecular biosciences · 2017Review
- Structural Elements Regulating AAA+ Protein Quality Control Machines.Frontiers in molecular biosciences · 2017Review
- Article
- Article
- The Symbiotic Performance of Chickpea Rhizobia Can Be Improved by Additional Copies of the clpB Chaperone Gene.PloS one · 2016Article
- ClpB N-terminal domain plays a regulatory role in protein disaggregation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Analysis of the cooperative ATPase cycle of the AAA+ chaperone ClpB from Thermus thermophilus by using ordered heterohexamers with an alternating subunit arrangement.The Journal of biological chemistry · 2015Article
- Molecular chaperones: guardians of the proteome in normal and disease states.F1000Research · 2015Review
- The mechanism of Torsin ATPase activation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Crowding activates ClpB and enhances its association with DnaK for efficient protein aggregate reactivation.Biophysical journal · 2014Article
- Elements in nucleotide sensing and hydrolysis of the AAA+ disaggregation machine ClpB: a structure-based mechanistic dissection of a molecular motor.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Structural mechanisms of chaperone mediated protein disaggregation.Frontiers in molecular biosciences · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
ClpB is a ring-forming, ATP-dependent protein disaggregase that cooperates with the cognate Hsp70 system to recover functional protein from aggregates. How ClpB harnesses the energy of ATP binding and hydrolysis to facilitate the mechanical unfolding of previously aggregated, stress-damaged proteins remains unclear. Here, we present crystal structures of the ClpB D2 domain in the nucleotide-bound and -free states, and the fitted cryoEM structure of the D2 hexamer ring, which provide a structural understanding of the ATP power stroke that drives protein translocation through the ClpB hexamer. We demonstrate that the conformation of the substrate-translocating pore loop is coupled to the nucleotide state of the cis subunit, which is transmitted to the neighboring subunit via a conserved but structurally distinct intersubunit-signaling pathway common to diverse AAA+ machines. Furthermore, we found that an engineered, disulfide cross-linked ClpB hexamer is fully functional biochemically, suggesting that ClpB deoligomerization is not required for protein disaggregation.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.