Evidence map›Paper›PMID 28722511›Full record

ReviewCell cycle (Georgetown, Tex.)2017

GRWD1, a new player among oncogenesis-related ribosomal/nucleolar proteins.

Takuya Takafuji, Kota Kayama, Nozomi Sugimoto, Masatoshi Fujita

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell cycle (Georgetown, Tex.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

20 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. GRWD1 Drives Melanoma Growth Through NF-κB Signaling Pathway.Dermatology practical & conceptual · 2025
    Article
  4. Article
  5. A specific negatively charged sequence confers intramolecular regulation on Munc13-1 function in synaptic exocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Inactivation ofInternational journal of biological sciences · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. The nucleolus, an ally, and an enemy of cancer cells.Histochemistry and cell biology · 2018
    Review
  20. Article
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

4 authors at 1 institution in 1 country.

Takuya Takafujia Department of Cellular Biochemistry, Graduate School of Pharmaceutical Sciences , Kyushu University , Higashi-ku, Fukuoka , Japan.
Kota Kayamaa Department of Cellular Biochemistry, Graduate School of Pharmaceutical Sciences , Kyushu University , Higashi-ku, Fukuoka , Japan.
Nozomi Sugimotoa Department of Cellular Biochemistry, Graduate School of Pharmaceutical Sciences , Kyushu University , Higashi-ku, Fukuoka , Japan.
Masatoshi Fujitaa Department of Cellular Biochemistry, Graduate School of Pharmaceutical Sciences , Kyushu University , Higashi-ku, Fukuoka , Japan.ORCID http://orcid.org/0000-0001-6617-2452
Kyushu University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Increasing attention has been paid to certain ribosomal or ribosome biosynthesis-related proteins involved in oncogenesis. Members of one group are classified as "tumor suppressive factors" represented by RPL5 and RPL11; loss of their functions leads to cancer predisposition. RPL5 and RPL11 prevent tumorigenesis by binding to and inhibiting the MDM2 ubiquitin ligase and thereby up-regulating p53. Many other candidate tumor suppressive ribosomal/nucleolar proteins have been suggested. However, it remains to be experimentally clarified whether many of these factors can actually prevent tumorigenesis and if so, how they do so. Conversely, some ribosomal/nucleolar proteins promote tumorigenesis. For example, PICT1 binds to and anchors RPL11 in nucleoli, down-regulating p53 and promoting tumorigenesis. GRWD1 was recently identified as another such factor. When overexpressed, GRWD1 suppresses p53 and transforms normal human cells, probably by binding to RPL11 and sequestrating it from MDM2. However, other pathways may also be involved.

Indexed as

AnimalsCarrier ProteinsCell NucleolusHumansNuclear ProteinsProto-Oncogene Proteins c-mdm2RibosomesTumor Suppressor Protein p53Carrier ProteinsGRWD1 protein, humanNuclear ProteinsProto-Oncogene Proteins c-mdm2Tumor Suppressor Protein p53GRWD1nucleolar stress responseoncogenep53PICT1RPL11tumor suppressor

Identifiers

PMID28722511
PMCPMC5553401
OpenAlexW2737295160

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.