Evidence map›Paper›PMID 28659384›Full record

ReviewOpen biology2017

Cell signalling pathway regulation by RanBPM: molecular insights and disease implications.

Louisa M Salemi, Matthew E R Maitland, Christina J McTavish, Caroline Schild-Poulter

Open access · goldAbstract readReview
In one paragraph

Review in Open biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

28 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. RANBP9 and RANBP10 cooperate in regulating non-small cell lung cancer proliferation.Journal of experimental & clinical cancer research : CR · 2025
    Article
  4. THE GID COMPLEX REGULATES DNA END PROCESSING DURING DNA DOUBLE-STRAND BREAK REPAIR BY NONHOMOLOGOUS END JOINING.Transactions of the American Clinical and Climatological Association · 2025
    Article
  5. The hGIDLife science alliance · 2024
    Article
  6. Article
  7. Article
  8. Structural and Functional Insights into GID/CTLH E3 Ligase Complexes.International journal of molecular sciences · 2022
    Review
  9. Article
  10. Article
  11. Proteomic analysis of ubiquitination substrates reveals a CTLH E3 ligase complex-dependent regulation of glycolysis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. RANBP9 as potential therapeutic target in non-small cell lung cancer.Journal of cancer metastasis and treatment · 2020
    Article
  18. Article
  19. Article
  20. The plant pathology journal · 2019
    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 3 countries.

Louisa M SalemiRobarts Research Institute, Department of Biochemistry, Schulich School of Medicine and Dentistry, The University of Western Ontario, 1151 Richmond Street North, London, Ontario, Canada N6A 5B7.
Matthew E R MaitlandRobarts Research Institute, Department of Biochemistry, Schulich School of Medicine and Dentistry, The University of Western Ontario, 1151 Richmond Street North, London, Ontario, Canada N6A 5B7.
Christina J McTavishRobarts Research Institute, Department of Biochemistry, Schulich School of Medicine and Dentistry, The University of Western Ontario, 1151 Richmond Street North, London, Ontario, Canada N6A 5B7.
Caroline Schild-PoulterRobarts Research Institute, Department of Biochemistry, Schulich School of Medicine and Dentistry, The University of Western Ontario, 1151 Richmond Street North, London, Ontario, Canada N6A 5B7 cschild-poulter@robarts.ca.ORCID 0000-0001-9943-9942
Western University · CA

Funding

CIHR MOP-142414
6 · The paper itself

Abstract

RanBPM (Ran-binding protein M, also called RanBP9) is an evolutionarily conserved, ubiquitous protein which localizes to both nucleus and cytoplasm. RanBPM has been implicated in the regulation of a number of signalling pathways to regulate several cellular processes such as apoptosis, cell adhesion, migration as well as transcription, and plays a critical role during development. In addition, RanBPM has been shown to regulate pathways implicated in cancer and Alzheimer's disease, implying that RanBPM has important functions in both normal and pathological development. While its functions in these processes are still poorly understood, RanBPM has been identified as a component of a large complex, termed the CTLH (C-terminal to LisH) complex. The yeast homologue of this complex functions as an E3 ubiquitin ligase that targets enzymes of the gluconeogenesis pathway. While the CTLH complex E3 ubiquitin ligase activity and substrates still remain to be characterized, the high level of conservation between the complexes in yeast and mammals infers that the CTLH complex could also serve to promote the degradation of specific substrates through ubiquitination, therefore suggesting the possibility that RanBPM's various functions may be mediated through the activity of the CTLH complex.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCell MovementConserved SequenceCytoskeletal ProteinsModels, MolecularMutationNuclear ProteinsSignal TransductionUbiquitinationAdaptor Proteins, Signal TransducingCytoskeletal ProteinsNuclear ProteinsRan binding protein 9Alzheimer diseasecancerCTLH complexGidRanBPM

Identifiers

PMID28659384
PMCPMC5493780
OpenAlexW2724321370

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.