Evidence map›Paper›PMID 18212112›Full record

ArticleAntimicrobial agents and chemotherapy2008

Structure-function correlations of two highly conserved motifs in Saccharomyces cerevisiae squalene epoxidase.

Christoph Ruckenstuhl, Andrea Poschenel, Reinhard Possert, Pravas Kumar Baral, Karl Gruber, Friederike Turnowsky

Open access · greenAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.6field-weighted citation impact, top 32% 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

1 citing paper in PubMed, 9 citations in OpenAlex.

  1. 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 at 1 institution in 1 country.

Christoph RuckenstuhlInstitute of Molecular Biosciences, Karl-Franzens-Universität Graz, Humboldtstrasse 50, A-8010 Graz, Austria.
Andrea Poschenel
Reinhard Possert
Pravas Kumar Baral
Karl Gruber
Friederike Turnowsky
University of Graz · AT

Funding

Austrian Science Fund FWF W 901
6 · The paper itself

Abstract

Saccharomyces cerevisiae squalene epoxidase contains two highly conserved motifs, 1 and 2, of unknown function. Amino acid substitutions in both regions reduce enzyme activity and/or alter allylamine sensitivity. In the homology model, these motifs flank the flavin adenine dinucleotide cofactor and form part of the interface between cofactor and substrate binding domains.

Indexed as

AllylamineAmino Acid MotifsAmino Acid SequenceConserved SequenceModels, MolecularSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSqualene MonooxygenaseStructure-Activity RelationshipAllylamineSaccharomyces cerevisiae ProteinsSqualene Monooxygenase

Identifiers

PMID18212112
PMCPMC2292544
OpenAlexW2149684335

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.