Evidence map›Paper›PMID 29311130›Full record

ReviewCold Spring Harbor perspectives in medicine2018

MRAS: A Close but Understudied Member of the RAS Family.

Lucy C Young, Pablo Rodriguez-Viciana

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in medicine, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

32 citing papers in PubMed, 1 synthesis or guideline pooled it, 59 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. M-Ras distinct activation scenarios: A mechanistic outlook and targeting.Computational and structural biotechnology journal · 2025
    Article
  10. Article
  11. Crystal structure of the GDP-bound human M-RAS protein in two crystal forms.Acta crystallographica. Section F, Structural biology communications · 2024
    Article
  12. Article
  13. Review
  14. The ancestral type of the R-RAS protein has oncogenic potential.Cellular & molecular biology letters · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. 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

2 authors at 2 institutions in 2 countries.

Lucy C YoungUCSF Helen Diller Family Comprehensive Cancer Center, San Francisco, California 94158.
Pablo Rodriguez-VicianaUCL Cancer Institute, Paul O'Gorman Building, University College London, London WC1E 6BT, United Kingdom.
UCSF Helen Diller Family Comprehensive Cancer Center · USUniversity College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MRAS is the closest relative to the classical RAS oncoproteins and shares most regulatory and effector interactions. However, it also has unique functions, including its ability to function as a phosphatase regulatory subunit when in complex with SHOC2 and protein phosphatase 1 (PP1). This phosphatase complex regulates a crucial step in the activation cycle of RAF kinases and provides a key coordinate input required for efficient ERK pathway activation and transformation by RAS. MRAS mutations rarely occur in cancer but deregulated expression may play a role in tumorigenesis in some settings. Activating mutations in MRAS (as well as SHOC2 and PP1) do occur in the RASopathy Noonan syndrome, underscoring a key role for MRAS within the RAS-ERK pathway. MRAS also has unique roles in cell migration and differentiation and has properties consistent with a key role in the regulation of cell polarity. Further investigations should shed light on what remains a relatively understudied RAS family member.

Indexed as

CarcinogenesisCell DifferentiationCell MovementCell PolarityGene Expression RegulationHumansIntracellular Signaling Peptides and ProteinsMAP Kinase Signaling SystemNoonan SyndromeProtein Phosphatase 1ras ProteinsSignal TransductionIntracellular Signaling Peptides and ProteinsMRAS protein, humanProtein Phosphatase 1ras ProteinsSHOC2 protein, human

Identifiers

PMID29311130
PMCPMC6280710
OpenAlexW2784165555

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.