Evidence map›Paper›PMID 22505404›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012

Structures of the pleckstrin homology domain of Saccharomyces cerevisiae Avo1 and its human orthologue Sin1, an essential subunit of TOR complex 2.

Dongqing Pan, Yoshiyuki Matsuura

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. microPublication biology · 2023
    Article
  4. Article
  5. RAS interaction with Sin1 is dispensable for mTORC2 assembly and activity.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Article
  7. Article
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  11. PI3K signaling in cancer: beyond AKT.Current opinion in cell biology · 2017
    Review
  12. Article
  13. Article
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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 1 institution in 1 country.

Dongqing PanDivision of Biological Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan.
Yoshiyuki Matsuura
Nagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In eukaryotes, multiprotein complexes termed TOR complex 1 (TORC1) and TOR complex 2 (TORC2) function as major regulators of cell growth, metabolism and ageing. The C-terminal domain of the Saccharomyces cerevisiae TORC2 component Avo1 is required for plasma-membrane localization of TORC2 and is essential for yeast viability. X-ray crystal structures of the C-terminal domain of Avo1 and of its human orthologue Sin1 have been determined. The structures show that the C-termini of Avo1 and Sin1 both have the pleckstrin homology (PH) domain fold. Comparison with known PH-domain structures suggests a putative binding site for phosphoinositides.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceCarrier ProteinsHumansModels, MolecularMolecular Sequence DataProtein Structure, QuaternaryProtein Structure, TertiaryProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentStructural Homology, ProteinTranscription FactorsAdaptor Proteins, Signal TransducingAvo1 protein, S cerevisiaeCarrier ProteinsCRTC2 protein, humanMAPKAP1 protein, humanProtein SubunitsSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID22505404
PMCPMC3325804
OpenAlexW2021557955

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.