ArticleProceedings of the National Academy of Sciences of the United States of America2015
Unique double-ring structure of the peroxisomal Pex1/Pex6 ATPase complex revealed by cryo-electron microscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 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
49 citing papers in PubMed, 79 citations in OpenAlex.
- Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026Review
- Visualisation of peroxisomes: a journey through seven decades.Histochemistry and cell biology · 2026Review
- Cryo-EM Structure of Human ATAD2B Reveals a Hexameric Organization Contributes to ATPase Activity and Substrate Coordination.bioRxiv : the preprint server for biology · 2026Article
- Structural basis of receptor retro-translocation in peroxisomal protein import.bioRxiv : the preprint server for biology · 2026Article
- Mapping Hsp104 interactions using cross-linking mass spectrometry.FEBS open bio · 2025Article
- Towards solving the mystery of peroxisomal matrix protein import.Trends in cell biology · 2024Review
- The peroxisome: an update on mysteries 3.0.Histochemistry and cell biology · 2024Review
- PEX1 is essential for glycosome biogenesis and trypanosomatid parasite survival.Frontiers in cellular and infection microbiology · 2024Article
- 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
- Protein import into peroxisomes occurs through a nuclear pore-like phase.Science (New York, N.Y.) · 2022Article
- AAA+ protease-adaptor structures reveal altered conformations and ring specialization.Nature structural & molecular biology · 2022Article
- PEX5 translocation into and out of peroxisomes drives matrix protein import.Molecular cell · 2022Article
- Article
- Insights into the Structure and Function of the Pex1/Pex6 AAA-ATPase in Peroxisome Homeostasis.Cells · 2022Review
- Peroxisomal Stress Response and Inter-Organelle Communication in Cellular Homeostasis and Aging.Antioxidants (Basel, Switzerland) · 2022Review
- Balancing the Opposing Principles That Govern Peroxisome Homeostasis.Trends in biochemical sciences · 2021Review
- Comparative Genomics of Peroxisome Biogenesis Proteins: Making Sense of the PEX Proteins.Frontiers in cell and developmental biology · 2021Article
- The molecular principles governing the activity and functional diversity of AAA+ proteins.Nature reviews. Molecular cell biology · 2020Review
- Expanding the clinical and genetic spectrum of Heimler syndrome.Orphanet journal of rare diseases · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
Members of the AAA family of ATPases assemble into hexameric double rings and perform vital functions, yet their molecular mechanisms remain poorly understood. Here, we report structures of the Pex1/Pex6 complex; mutations in these proteins frequently cause peroxisomal diseases. The structures were determined in the presence of different nucleotides by cryo-electron microscopy. Models were generated using a computational approach that combines Monte Carlo placement of structurally homologous domains into density maps with energy minimization and refinement protocols. Pex1 and Pex6 alternate in an unprecedented hexameric double ring. Each protein has two N-terminal domains, N1 and N2, structurally related to the single N domains in p97 and N-ethylmaleimide sensitive factor (NSF); N1 of Pex1 is mobile, but the others are packed against the double ring. The N-terminal ATPase domains are inactive, forming a symmetric D1 ring, whereas the C-terminal domains are active, likely in different nucleotide states, and form an asymmetric D2 ring. These results suggest how subunit activity is coordinated and indicate striking similarities between Pex1/Pex6 and p97, supporting the hypothesis that the Pex1/Pex6 complex has a role in peroxisomal protein import analogous to p97 in ER-associated protein degradation.
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.