Evidence map›Paper›PMID 22540023›Full record

ReviewNucleus (Austin, Tex.)

Integrated regulation of PIKK-mediated stress responses by AAA+ proteins RUVBL1 and RUVBL2.

Natsuko Izumi, Akio Yamashita, Shigeo Ohno

Open access · goldAbstract readReview
In one paragraph

Review in Nucleus (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  15. Mechanism, factors, and physiological role of nonsense-mediated mRNA decay.Cellular and molecular life sciences : CMLS · 2015
    Review
  16. Article
  17. Review
  18. Article
  19. Hsp90 picks PIKKs via R2TP and Tel2.Structure (London, England : 1993) · 2014
    Article
  20. Review
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

3 authors at 1 institution in 2 countries.

Natsuko IzumiDepartment of Molecular Biology, Yokohama City University School of Medicine, Yokohama, Japan.
Akio Yamashita
Shigeo Ohno
Yokohama City University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family are activated by various cellular stresses, including DNA damage, premature termination codon and nutritional status, and induce appropriate cellular responses. The importance of PIKK functions in the maintenance of genome integrity, accurate gene expression and the proper control of cell growth/proliferation is established. Recently, ATPase associated diverse cellular activities (AAA+) proteins RUVBL1 and RUVBL2 (RUVBL1/2) have been shown to be common regulators of PIKKs. The RUVBL1/2 complex regulates PIKK-mediated stress responses through physical interactions with PIKKs and by controlling PIKK mRNA levels. In this review, the functions of PIKKs in stress responses are outlined and the physiological significance of the integrated regulation of PIKKs by the RUVBL1/2 complex is presented. We also discuss a putative "PIKK regulatory chaperone complex" including other PIKK regulators, Hsp90 and the Tel2 complex.

Indexed as

Stress, PhysiologicalAdenosine TriphosphatasesAnimalsDNA HelicasesHumansMolecular ChaperonesPhosphatidylinositol 3-KinasesProtein KinasesAdenosine TriphosphatasesDNA HelicasesMolecular ChaperonesPhosphatidylinositol 3-KinasesProtein KinasesAAA+ATMATRDNA damage responseDNA-PKcsmTORPIKKRUVBLSMG-1TRRAP

Identifiers

PMID22540023
PMCPMC3337166
OpenAlexW2071401245

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.