Evidence map›Paper›PMID 29718000›Full record

ArticleActa crystallographica. Section F, Structural biology communications2018

Structure of the tandem PX-PH domains of Bem3 from Saccharomyces cerevisiae.

Imtiaz Ali, Sungmin Eu, Daniel Koch, Nathalie Bleimling, Roger S Goody, Matthias P Müller

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–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

2 citing papers in PubMed.

  1. HJournal of fungi (Basel, Switzerland) · 2021
    Article
  2. 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

6 authors.

Imtiaz AliDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
Sungmin EuDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
Daniel KochDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.ORCID 0000-0002-4893-1774
Nathalie BleimlingDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
Roger S GoodyDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.ORCID 0000-0002-0772-0444
Matthias P MüllerDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.ORCID 0000-0002-1529-8933

Funding

Deutsche Forschungsgemeinschaft GO 284/8-1Deutsche Forschungsgemeinschaft SFB 642
6 · The paper itself

Abstract

The structure of the tandem lipid-binding PX and pleckstrin-homology (PH) domains of the Cdc42 GTPase-activating protein Bem3 from Saccharomyces cerevisiae (strain S288c) has been determined to a resolution of 2.2 Å (R

Indexed as

Amino Acid SequenceCrystallizationGTPase-Activating ProteinsProtein Interaction Domains and MotifsProtein Structure, SecondaryProtein Structure, TertiarySaccharomyces cerevisiae ProteinsBEM3 protein, S cerevisiaeGTPase-Activating ProteinsSaccharomyces cerevisiae ProteinsBem3PH domainphosphatidylinositol phosphatesphoxPIPpleckstrin homologyPX domainSaccharomyces cerevisiae

Identifiers

PMID29718000
PMCPMC5931145

What OpenQuestion holds

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Registered trials

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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.