ReviewFrontiers in molecular biosciences2017
Structural Elements Regulating AAA+ Protein Quality Control Machines.
Review in Frontiers in molecular biosciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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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.
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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.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Cryo-EM structure of the AAA+ SPATA5 complex and its role in human cytoplasmic pre-60S maturation.Nature communications · 2025Article
- MoxR effects as an ATPase on anti-stress and pathogenicity of Riemerella anatipestifer.Veterinary research · 2025Article
- An empirical energy landscape reveals mechanism of proteasome in polypeptide translocation.eLife · 2022Article
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Structural basis for distinct operational modes and protease activation in AAA+ protease Lon.Science advances · 2020Article
- Stairway to translocation: AAA+ motor structures reveal the mechanisms of ATP-dependent substrate translocation.Protein science : a publication of the Protein Society · 2020Review
- 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
- Mitochondrial AAA proteases: A stairway to degradation.Mitochondrion · 2019Review
- Article
- Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing.Science (New York, N.Y.) · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Members of the ATPases Associated with various cellular Activities (AAA+) superfamily participate in essential and diverse cellular pathways in all kingdoms of life by harnessing the energy of ATP binding and hydrolysis to drive their biological functions. Although most AAA+ proteins share a ring-shaped architecture, AAA+ proteins have evolved distinct structural elements that are fine-tuned to their specific functions. A central question in the field is how ATP binding and hydrolysis are coupled to substrate translocation through the central channel of ring-forming AAA+ proteins. In this mini-review, we will discuss structural elements present in AAA+ proteins involved in protein quality control, drawing similarities to their known role in substrate interaction by AAA+ proteins involved in DNA translocation. Elements to be discussed include the pore loop-1, the Inter-Subunit Signaling (ISS) motif, and the Pre-Sensor I insert (PS-I) motif. Lastly, we will summarize our current understanding on the inter-relationship of those structural elements and propose a model how ATP binding and hydrolysis might be coupled to polypeptide translocation in protein quality control machines.
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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.