ReviewTrends in biochemical sciences2014
Marching to the beat of the ring: polypeptide translocation by AAA+ proteases.
Review in Trends in biochemical sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 45 citations in OpenAlex.
- Dual targeting of the UPS and autophagy as a novel therapy for neurodegenerative proteinopathies.Frontiers in cellular neuroscience · 2026Review
- Maintaining the Integral Membrane Proteome: Revisiting the Functional Repertoire of Integral Membrane Proteases.Chembiochem : a European journal of chemical biology · 2025Review
- Cryo-EM structure of AAA + ATPase thorase reveals novel helical filament formation.Computational and structural biotechnology journal · 2025Article
- Temperature Matters: Bacterial Response to Temperature Change.Journal of microbiology (Seoul, Korea) · 2023Review
- Article
- AAA+ ATPases: structural insertions under the magnifying glass.Current opinion in structural biology · 2021Review
- Stairway to translocation: AAA+ motor structures reveal the mechanisms of ATP-dependent substrate translocation.Protein science : a publication of the Protein Society · 2020Review
- Structure of spastin bound to a glutamate-rich peptide implies a hand-over-hand mechanism of substrate translocation.The Journal of biological chemistry · 2020Article
- The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn.Nature communications · 2019Article
- Article
- Functional degradation: A mechanism of NLRP1 inflammasome activation by diverse pathogen enzymes.Science (New York, N.Y.) · 2019Article
- Structure and mechanism of the ESCRT pathway AAA+ ATPase Vps4.Biochemical Society transactions · 2019Review
- Expanded Coverage of the 26S Proteasome Conformational Landscape Reveals Mechanisms of Peptidase Gating.Cell reports · 2018Article
- Structure and Function of the 26S Proteasome.Annual review of biochemistry · 2018Review
- Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing.Science (New York, N.Y.) · 2017Article
- Structural insights into the functional cycle of the ATPase module of the 26S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- An atomic structure of the human 26S proteasome.Nature structural & molecular biology · 2016Article
- Structure of the human 26S proteasome at a resolution of 3.9 Å.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Gates, Channels, and Switches: Elements of the Proteasome Machine.Trends in biochemical sciences · 2016Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
ATP-dependent proteases exist in all cells and are crucial regulators of the proteome. These machines consist of a hexameric, ring-shaped motor responsible for engaging, unfolding, and translocating protein substrates into an associated peptidase for degradation. Here, we discuss recent work that has established how the six motor subunits coordinate their ATP-hydrolysis and translocation activities. The closed topology of the ring and the rigidity of subunit/subunit interfaces cause conformational changes within a single subunit to drive motions in other subunits of the hexamer. This structural effect generates allostery between the ATP-binding sites, leading to a preferred order of binding and hydrolysis events among the motor subunits as well as a unique biphasic mechanism of translocation.
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.