ArticleProceedings of the National Academy of Sciences of the United States of America2020
Insights into the mechanism and regulation of the CbbQO-type Rubisco activase, a MoxR AAA+ ATPase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 43 citations in OpenAlex.
- NorQD AAA+ complex drives metal insertion by a twisting mechanism.Nature communications · 2026Article
- A Cyanobacterial Screening Platform for Rubisco Mutant Variants.ACS synthetic biology · 2025Article
- MoxR effects as an ATPase on anti-stress and pathogenicity of Riemerella anatipestifer.Veterinary research · 2025Article
- Structural modeling and biochemical characterization of MSMEG_0748, a MoxR ATPase fromComputational and structural biotechnology journal · 2025Article
- Translation Fidelity and Respiration Deficits in CLPP-Deficient Tissues: Mechanistic Insights from Mitochondrial Complexome Profiling.International journal of molecular sciences · 2023Article
- The RavA-ViaA chaperone complex modulates bacterial persistence through its association with the fumarate reductase enzyme.The Journal of biological chemistry · 2023Article
- Article
- Red Rubiscos and opportunities for engineering green plants.Journal of experimental botany · 2023Review
- Molecular mechanism of Rubisco activase: Dynamic assembly and Rubisco remodeling.Frontiers in molecular biosciences · 2023Review
- The AAA+ ATPase RavA and its binding partner ViaA modulate E. coli aminoglycoside sensitivity through interaction with the inner membrane.Nature communications · 2022Article
- Decoding the Absolute Stoichiometric Composition and Structural Plasticity of α-Carboxysomes.mBio · 2022Article
- Article
- The MIDAS domain of AAA mechanoenzyme Mdn1 forms catch bonds with two different substrates.eLife · 2022Article
- Incorporation of Functional Rubisco Activases into Engineered Carboxysomes to Enhance Carbon Fixation.ACS synthetic biology · 2022Article
- New discoveries expand possibilities for carboxysome engineering.Current opinion in microbiology · 2021Review
- AAA+ ATPases: structural insertions under the magnifying glass.Current opinion in structural biology · 2021Review
- The Novel Halovirus Hardycor1, and the Presence of Active (Induced) Proviruses in Four Haloarchaea.Genes · 2021Article
- Rubisco activase requires residues in the large subunit N terminus to remodel inhibited plant Rubisco.The Journal of biological chemistry · 2020Article
- Long-range intramolecular allostery and regulation in the dynein-like AAA protein Mdn1.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Catalytic Role of RuBisCO forFrontiers in bioengineering and biotechnology · 2020Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The vast majority of biological carbon dioxide fixation relies on the function of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco). In most cases the enzyme exhibits a tendency to become inhibited by its substrate RuBP and other sugar phosphates. The inhibition is counteracted by diverse molecular chaperones known as Rubisco activases (Rcas). In some chemoautotrophic bacteria, the CbbQO-type Rca Q2O2 repairs inhibited active sites of hexameric form II Rubisco. The 2.2-Å crystal structure of the MoxR AAA+ protein CbbQ2 from
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