ArticleNature communications2015
Molecular snapshots of the Pex1/6 AAA+ complex in action.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 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
39 citing papers in PubMed, 79 citations in OpenAlex.
- Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026Review
- Ribosome biogenesis in plants requires the nuclear envelope and mitochondria localized OPENER complex.Nature communications · 2025Article
- Towards solving the mystery of peroxisomal matrix protein import.Trends in cell biology · 2024Review
- Structure of the peroxisomal Pex1/Pex6 ATPase complex bound to a substrate.Nature communications · 2023Article
- Purification of a Recombinant Human PEX1/PEX6 AAA+ ATPase Complex from HEK293TT Cells.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Genetics behind Cerebral Disease with Ocular Comorbidity: Finding Parallels between the Brain and Eye Molecular Pathology.International journal of molecular sciences · 2022Review
- Insights into the Structure and Function of the Pex1/Pex6 AAA-ATPase in Peroxisome Homeostasis.Cells · 2022Review
- The essential role of fungal peroxisomes in plant infection.Molecular plant pathology · 2022Review
- An orthologous gene coevolution network provides insight into eukaryotic cellular and genomic structure and function.Science advances · 2022Article
- Article
- Peroxisomal Stress Response and Inter-Organelle Communication in Cellular Homeostasis and Aging.Antioxidants (Basel, Switzerland) · 2022Review
- Image-Based Analysis Revealing the Molecular Mechanism of Peroxisome Dynamics in Plants.Frontiers in cell and developmental biology · 2022Review
- Expanding the clinical and genetic spectrum of Heimler syndrome.Orphanet journal of rare diseases · 2019Article
- A Mechanistic Perspective on PEX1 and PEX6, Two AAA+ Proteins of the Peroxisomal Protein Import Machinery.International journal of molecular sciences · 2019Review
- Structural Mapping of Missense Mutations in the Pex1/Pex6 Complex.International journal of molecular sciences · 2019Review
- Current Advances in Protein Import into Peroxisomes.The protein journal · 2019Review
- The peroxisome: an update on mysteries 2.0.Histochemistry and cell biology · 2018Review
- Chemically monoubiquitinated PEX5 binds to the components of the peroxisomal docking and export machinery.Scientific reports · 2018Article
- Receptor recognition by the peroxisomal AAA complex depends on the presence of the ubiquitin moiety and is mediated by Pex1p.The Journal of biological chemistry · 2018Article
- Peroxisomal monoubiquitinated PEX5 interacts with the AAA ATPases PEX1 and PEX6 and is unfolded during its dislocation into the cytosol.The Journal of biological chemistry · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The peroxisomal proteins Pex1 and Pex6 form a heterohexameric type II AAA+ ATPase complex, which fuels essential protein transport across peroxisomal membranes. Mutations in either ATPase in humans can lead to severe peroxisomal disorders and early death. We present an extensive structural and biochemical analysis of the yeast Pex1/6 complex. The heterohexamer forms a trimer of Pex1/6 dimers with a triangular geometry that is atypical for AAA+ complexes. While the C-terminal nucleotide-binding domains (D2) of Pex6 constitute the main ATPase activity of the complex, both D2 harbour essential substrate-binding motifs. ATP hydrolysis results in a pumping motion of the complex, suggesting that Pex1/6 function involves substrate translocation through its central channel. Mutation of the Walker B motif in one D2 domain leads to ATP hydrolysis in the neighbouring domain, giving structural insights into inter-domain communication of these unique heterohexameric AAA+ assemblies.
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.