Evidence map›Paper›PMID 28788436›Full record

ReviewBiomolecules2017

The Architecture of the Rag GTPase Signaling Network.

Raffaele Nicastro, Alessandro Sardu, Nicolas Panchaud, Claudio De Virgilio

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed, 1 pooled it
3.8field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 1 synthesis or guideline pooled it, 74 citations in OpenAlex.

  1. Guideline
  2. Article
  3. Review
  4. Article
  5. NovelKidney international reports · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. A novel variation inFrontiers in genetics · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Plasma membrane HiScience · 2022
    Article
  18. Article
  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

4 authors at 2 institutions in 1 country.

Raffaele NicastroDepartment of Biology, University of Fribourg, Chemin du Musée 10, CH-1700 Fribourg, Switzerland. raffaele.nicastro2@unifr.ch.
Alessandro SarduDepartment of Biology, University of Fribourg, Chemin du Musée 10, CH-1700 Fribourg, Switzerland. alessandro.sardu@unifr.ch.
Nicolas PanchaudNovartis Institutes for Biomedical Research, NIBR, Novartis Pharma AG, 4002 Basel, Switzerland. nicolas_panchaud@hotmail.com.
Claudio De VirgilioDepartment of Biology, University of Fribourg, Chemin du Musée 10, CH-1700 Fribourg, Switzerland. claudio.devirgilio@unifr.ch.
University of Fribourg · CHNovartis (Switzerland) · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The evolutionarily conserved target of rapamycin complex 1 (TORC1) couples an array of intra- and extracellular stimuli to cell growth, proliferation and metabolism, and its deregulation is associated with various human pathologies such as immunodeficiency, epilepsy, and cancer. Among the diverse stimuli impinging on TORC1, amino acids represent essential input signals, but how they control TORC1 has long remained a mystery. The recent discovery of the Rag GTPases, which assemble as heterodimeric complexes on vacuolar/lysosomal membranes, as central elements of an amino acid signaling network upstream of TORC1 in yeast, flies, and mammalian cells represented a breakthrough in this field. Here, we review the architecture of the Rag GTPase signaling network with a special focus on structural aspects of the Rag GTPases and their regulators in yeast and highlight both the evolutionary conservation and divergence of the mechanisms that control Rag GTPases.

Indexed as

Signal TransductionAmino AcidsAmino Acid SequenceAnimalsConserved SequenceFungal ProteinsGene Expression RegulationGTP PhosphohydrolasesHumansMechanistic Target of Rapamycin Complex 1Models, MolecularYeastsAmino AcidsFungal ProteinsGTP PhosphohydrolasesMechanistic Target of Rapamycin Complex 1amino acid signalingbudding yeastEGO complexLst4–Lst7Rag GTPasesSEACATSEACITtarget of rapamycin complex 1 (TORC1)

Identifiers

PMID28788436
PMCPMC5618229
OpenAlexW2726091387

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.