Evidence map›Paper›PMID 24393003›Full record

ArticleThe Biochemical journal2014

The ability of TRIM3 to induce growth arrest depends on RING-dependent E3 ligase activity.

Radhika Raheja, Yuhui Liu, Ellen Hukkelhoven, Nancy Yeh, Andrew Koff

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2014. 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
1.6field-weighted citation impact, top 17% 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
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Expression and Role of TRIM2 in Human Diseases.BioMed research international · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. How to Inactivate Human Ubiquitin E3 Ligases by Mutation.Frontiers in cell and developmental biology · 2020
    Review
  14. Exosomal TRIM3 is a novel marker and therapy target for gastric cancer.Journal of experimental & clinical cancer research : CR · 2018
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

5 authors at 1 institution in 1 country.

Radhika Raheja
Yuhui Liu*Program in Molecular Biology, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, U.S.A.
Ellen Hukkelhoven*Program in Molecular Biology, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, U.S.A.
Nancy Yeh*Program in Molecular Biology, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY 10021, U.S.A.
Andrew Koff
Memorial Sloan Kettering Cancer Center · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
P27KIP1 EXPRESSION, A PROGNOSTIC INDICATOR==BUT WHY?R01CA089563 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI KOFF, ANDREW · 2001 to 2011
$4.2M
NCI NIH HHS CA89563NCI NIH HHS P30 CA008748NCI NIH HHS P30CA08748NCI NIH HHS R01 CA089563
6 · The paper itself

Abstract

Mutation of the TRIM (tripartite motif)-NHL family members brat and mei-P26 perturb the differentiation of transit-amplifying progenitor cells resulting in tumour-like phenotypes. The NHL (named after the NCL1, HT2A and LIN41 repeat) domain is essential for their growth suppressive activity, and they can induce cell-cycle exit in a RING-independent manner. TRIM3 is the only bona fide tumour suppressor in the mammalian TRIM-NHL subfamily and similar to the other members of this family, its ability to inhibit cell proliferation depends on the NHL domain. However, whether the RING domain was required for TRIM3-dependent cell-cycle exit had not been investigated. In the present study, we establish that the RING domain is required for TRIM3-induced growth suppression. Furthermore, we show that this domain is necessary to promote ubiquitination of p21 in a reconstituted in vitro system where UbcH5a is the preferred E2. Thus the ability of TRIM3 to suppress growth is associated with its ability to ubiquitinate proteins.

Indexed as

AnimalsCarrier ProteinsCell Line, TumorCell ProliferationCyclin-Dependent Kinase Inhibitor p21HumansMiceMutationProtein Structure, TertiaryUbiquitinationUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesCarrier ProteinsCyclin-Dependent Kinase Inhibitor p21TRIM3 protein, mouseUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligases

Identifiers

PMID24393003
PMCPMC4404499
OpenAlexW2321624895

What OpenQuestion holds

Textmetadata
LicenceTDM
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.