ArticleeLife2015
TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 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
104 citing papers in PubMed, 180 citations in OpenAlex.
- NPP-21/TPR is required for developmental control of spindle checkpoint strength inbioRxiv : the preprint server for biology · 2026Article
- TRIP13 promotes the expansion and immunosuppression of CD4Cell death & disease · 2026Article
- Real-time capture of σNature communications · 2025Article
- Linear ubiquitination of p31Cell & bioscience · 2025Article
- Advancing the development of TRIP13 inhibitors: A high-throughput screening approach.SLAS discovery : advancing life sciences R & D · 2025Article
- p31International journal of molecular sciences · 2025Article
- Repeated ionizing radiation exposure induces TRIP13 expression, conferring radioresistance in lung cancer cells.Scientific reports · 2025Article
- Mosaic variegated aneuploidy in development, ageing and cancer.Nature reviews. Genetics · 2024Review
- Non-autonomous insulin signaling delays mitotic progression in C. elegans germline stem and progenitor cells.PLoS genetics · 2024Article
- U6 snRNA m6A modification is required for accurate and efficient splicing of C. elegans and human pre-mRNAs.Nucleic acids research · 2024Article
- Analysis of meiotic recombination in Drosophila simulans shows no evidence of an interchromosomal effect.Genetics · 2024Article
- Ribosomal protein S3 mediates drug resistance of proteasome inhibitor: potential therapeutic application in multiple myeloma.Haematologica · 2024Article
- Role of spindle assembly checkpoint proteins in gametogenesis and embryogenesis.Frontiers in cell and developmental biology · 2024Review
- Exportin-mediated nucleocytoplasmic transport maintains Pch2 homeostasis during meiosis.PLoS genetics · 2023Article
- Targeting TRIP13 for overcoming anticancer drug resistance (Review).Oncology reports · 2023Article
- Oncogenic Targets Regulated by Tumor-SuppressiveCancers · 2023Article
- Principles and dynamics of spindle assembly checkpoint signalling.Nature reviews. Molecular cell biology · 2023Review
- Revolving hexameric ATPases as asymmetric motors to translocate double-stranded DNA genome along one strand.iScience · 2023Review
- Structure, substrate binding and activity of a unique AAA+ protein: the BrxL phage restriction factor.Nucleic acids research · 2023Article
- Shieldin complex assembly kinetics and DNA binding by SHLD3.Communications biology · 2023Article
44 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The AAA+ family ATPase TRIP13 is a key regulator of meiotic recombination and the spindle assembly checkpoint, acting on signaling proteins of the conserved HORMA domain family. Here we present the structure of the Caenorhabditis elegans TRIP13 ortholog PCH-2, revealing a new family of AAA+ ATPase protein remodelers. PCH-2 possesses a substrate-recognition domain related to those of the protein remodelers NSF and p97, while its overall hexameric architecture and likely structural mechanism bear close similarities to the bacterial protein unfoldase ClpX. We find that TRIP13, aided by the adapter protein p31(comet), converts the HORMA-family spindle checkpoint protein MAD2 from a signaling-active 'closed' conformer to an inactive 'open' conformer. We propose that TRIP13 and p31(comet) collaborate to inactivate the spindle assembly checkpoint through MAD2 conformational conversion and disassembly of mitotic checkpoint complexes. A parallel HORMA protein disassembly activity likely underlies TRIP13's critical regulatory functions in meiotic chromosome structure and recombination.
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.