Evidence map›Paper›PMID 36289347›Full record

ArticleNature2022

Cryo-EM structure of the SEA complex.

Lucas Tafur, Kerstin Hinterndorfer, Caroline Gabus, Chiara Lamanna, Ariane Bergmann, Yashar Sadian, Farzad Hamdi, Fotis L Kyrilis, Panagiotis L Kastritis, Robbie Loewith

Open access · hybridAbstract read
In one paragraph

Article in Nature, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Architecture of the human KICSTOR and GATOR1-KICSTOR complexes.Nature structural & molecular biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Rag-Ragulator is the central organizer of the physical architecture of the mTORC1 nutrient-sensing pathway.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  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

10 authors at 2 institutions in 2 countries.

Lucas TafurDepartment of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland.ORCID http://orcid.org/0000-0002-6618-9649
Kerstin HinterndorferDepartment of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland.
Caroline GabusDepartment of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland.
Chiara LamannaDepartment of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland.
Ariane BergmannDepartment of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland.
Yashar SadianCryoGEnic facility (DCI Geneva), University of Geneva, Geneva, Switzerland.
Farzad HamdiInterdisciplinary Research Center HALOmem & Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Halle, Germany.ORCID http://orcid.org/0000-0002-2155-5000
Fotis L KyrilisInterdisciplinary Research Center HALOmem & Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Halle, Germany.ORCID http://orcid.org/0000-0002-4040-6289
Panagiotis L KastritisInterdisciplinary Research Center HALOmem & Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Halle, Germany.ORCID http://orcid.org/0000-0002-1463-8422
Robbie LoewithDepartment of Molecular and Cellular Biology, University of Geneva, Geneva, Switzerland. Robbie.Loewith@unige.ch.ORCID http://orcid.org/0000-0002-2482-603X
University of Geneva · CHMartin Luther University Halle-Wittenberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The SEA complex (SEAC) is a growth regulator that acts as a GTPase-activating protein (GAP) towards Gtr1, a Rag GTPase that relays nutrient status to the Target of Rapamycin Complex 1 (TORC1) in yeast

Indexed as

Cryoelectron MicroscopyGTPase-Activating ProteinsMultienzyme ComplexesAmino AcidsAnimalsCOP-Coated VesiclesGlucoseGTP PhosphohydrolasesMammalsMechanistic Target of Rapamycin Complex 1Monomeric GTP-Binding ProteinsProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAmino AcidsGlucoseGTPase-Activating ProteinsGTP PhosphohydrolasesGtr1 protein, S cerevisiaeMechanistic Target of Rapamycin Complex 1Monomeric GTP-Binding ProteinsMultienzyme ComplexesProtein SubunitsSaccharomyces cerevisiae Proteins

Identifiers

PMID36289347
PMCPMC9646525
OpenAlexW4307659347

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.