Evidence map›Paper›PMID 31512989›Full record

ReviewSmall GTPases2021

Small GTPases of the Ras superfamily and glycogen phosphorylase regulation in T cells.

Francisco Llavero, Alazne Arrazola Sastre, Miriam Luque Montoro, Miguel A Martín, Joaquín Arenas, Alejandro Lucia, José L Zugaza

Open access · bronzeAbstract readReview
In one paragraph

Review in Small GTPases, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

11 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. The Role of the Guanosine Nucleotide-Binding Protein in the Corpus Luteum.Animals : an open access journal from MDPI · 2021
    Review
  10. Review
  11. McArdle Disease: New Insights into Its Underlying Molecular Mechanisms.International journal of molecular sciences · 2019
    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

7 authors at 4 institutions in 1 country.

Francisco LlaveroAchucarro Basque Center for Neuroscience, Science Park of the UPV/EHU , Leioa, Spain.
Alazne Arrazola SastreAchucarro Basque Center for Neuroscience, Science Park of the UPV/EHU , Leioa, Spain.
Miriam Luque MontoroAchucarro Basque Center for Neuroscience, Science Park of the UPV/EHU , Leioa, Spain.
Miguel A MartínEnfermedades Raras, Mitocondriales y Neuromusculares., Instituto de Investigación Hospital 12 de Octubre (i+12) , Madrid, Spain.
Joaquín ArenasEnfermedades Raras, Mitocondriales y Neuromusculares., Instituto de Investigación Hospital 12 de Octubre (i+12) , Madrid, Spain.
Alejandro LuciaFaculty of Sport Sciences, Universidad Europea de Madrid , Madrid, Spain.
José L ZugazaAchucarro Basque Center for Neuroscience, Science Park of the UPV/EHU , Leioa, Spain.ORCID 0000-0002-9000-6398
Instituto de Salud Carlos III · ESAchucarro Basque Center for Neuroscience · ESIkerbasque · ESUniversity of the Basque Country · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small GTPases, together with their regulatory and effector molecules, are key intermediaries in the complex signalling pathways that control almost all cellular processes, working as molecular switches to transduce extracellular cues into cellular responses that drive vital functions, such as intracellular transport, biomolecule synthesis, gene activation and cell survival. How all of these networks are linked to metabolic pathways is a subject of intensive study. Because any response to cellular action requires some form of energy input, elucidating how cells coordinate the signals that lead to a tangible response involving metabolism is central to understand cellular activities. In this review, we summarize recent advances in our understanding of the molecular basis of the crosstalk between small GTPases of the Ras superfamily, specifically Rac1 and Ras/Rap1, and glycogen phosphorylase in T lymphocytes.

Indexed as

Glycogen PhosphorylaseT-LymphocytesAnimalsHumansMonomeric GTP-Binding ProteinsProto-Oncogene Masras ProteinsSignal TransductionGlycogen PhosphorylaseMAS1 protein, humanMonomeric GTP-Binding ProteinsProto-Oncogene Masras ProteinsEGFRglycogen phosphorylaseIL-2Rsmall GTPasesT lymphocytes

Identifiers

PMID31512989
PMCPMC7849735
OpenAlexW2972536087

What Socratic 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 Socratic graph.