Evidence map›Paper›PMID 28659378›Full record

ArticleThe EMBO journal2017

The AAA+ ATPase TRIP13 remodels HORMA domains through N-terminal engagement and unfolding.

Qiaozhen Ye, Dong Hyun Kim, Ihsan Dereli, Scott C Rosenberg, Goetz Hagemann, Franz Herzog, Attila Tóth, Don W Cleveland, Kevin D Corbett

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.9field-weighted citation impact, top 5% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

54 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
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  8. Article
  9. Role of TRIP13 in human cancer development.Molecular biology reports · 2024
    Review
  10. Article
  11. Article
  12. Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin.bioRxiv : the preprint server for biology · 2024
    Article
  13. Article
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  15. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 2 countries.

Qiaozhen YeLudwig Institute for Cancer Research, San Diego Branch, La Jolla, CA, USA.
Dong Hyun KimLudwig Institute for Cancer Research, San Diego Branch, La Jolla, CA, USA.
Ihsan DereliInstitute of Physiological Chemistry, Faculty of Medicine at the TU Dresden, Dresden, Germany.
Scott C RosenbergLudwig Institute for Cancer Research, San Diego Branch, La Jolla, CA, USA.
Goetz HagemannGene Center Munich and Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
Franz HerzogGene Center Munich and Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany.
Attila TóthInstitute of Physiological Chemistry, Faculty of Medicine at the TU Dresden, Dresden, Germany.
Don W ClevelandLudwig Institute for Cancer Research, San Diego Branch, La Jolla, CA, USA.
Kevin D CorbettLudwig Institute for Cancer Research, San Diego Branch, La Jolla, CA, USA kcorbett@ucsd.edu.ORCID 0000-0001-5854-2388
University of California San Diego · USLudwig Cancer Research · USLudwig-Maximilians-Universität München · DETechnische Universität Dresden · DE

Funding

Mechanisms of chromosome segregation, aneuploidy, and tumorigenesisR35GM122476 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Don W Cleveland · 2017 to 2026
$9.0M
MICROTUBULE REGULATIONR01GM029513 · NIGMS · LUDWIG INSTITUTE FOR CANCER RES LTD · PI CLEVELAND, DON W · 1985 to 2016
$8.2M
Molecular mechanisms of chromosome organization and recombination control by the meiotic chromosome axis.R01GM104141 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CORBETT, KEVIN DANIEL · 2013 to 2021
$3.1M
NIGMS NIH HHS R01 GM029513NIGMS NIH HHS R01 GM104141
6 · The paper itself

Abstract

Proteins of the conserved HORMA domain family, including the spindle assembly checkpoint protein MAD2 and the meiotic HORMADs, assemble into signaling complexes by binding short peptides termed "closure motifs". The AAA+ ATPase TRIP13 regulates both MAD2 and meiotic HORMADs by disassembling these HORMA domain-closure motif complexes, but its mechanisms of substrate recognition and remodeling are unknown. Here, we combine X-ray crystallography and crosslinking mass spectrometry to outline how TRIP13 recognizes MAD2 with the help of the adapter protein p31

Indexed as

Protein UnfoldingAdaptor Proteins, Signal TransducingAdenosine TriphosphateATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsCell Cycle ProteinsCrystallography, X-RayHumansMad2 ProteinsMass SpectrometryModels, MolecularNuclear ProteinsProtein ConformationAdaptor Proteins, Signal TransducingAdenosine TriphosphateATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsCell Cycle ProteinsMAD2L1BP protein, humanMAD2L1 protein, humanMad2 ProteinsNohma protein, mouseNuclear ProteinsTRIP13 protein, humanAAA+ ATPaseHORMA domainmeiotic chromosome structurespindle assembly checkpoint

Identifiers

PMID28659378
PMCPMC5556265
OpenAlexW2726002411

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.