Evidence map›Paper›PMID 23295489›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013

Crystallization and preliminary X-ray diffraction studies of Drosophila melanogaster Gαo-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036.

Svetlana Tishchenko, Azat Gabdulkhakov, Uliana Tin, Olga Kostareva, Chen Lin, Vladimir L Katanaev

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. 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
0.1field-weighted citation impact, top 48% 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, 3 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 2 institutions in 2 countries.

Svetlana TishchenkoInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russian Federation. sveta@vega.protres.ru
Azat Gabdulkhakov
Uliana Tin
Olga Kostareva
Chen Lin
Vladimir L Katanaev
Institute of Protein Research · RUUniversity of Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Regulator of G-protein signalling (RGS) proteins negatively regulate heterotrimeric G-protein signalling through their conserved RGS domains. RGS domains act as GTPase-activating proteins, accelerating the GTP hydrolysis rate of the activated form of Gα-subunits. Although omnipresent in eukaryotes, RGS proteins have not been adequately analysed in non-mammalian organisms. The Drosophila melanogaster Gαo-subunit and the RGS domain of its interacting partner CG5036 have been overproduced and purified; the crystallization of the complex of the two proteins using PEG 4000 as a crystallizing agent and preliminary X-ray crystallographic analysis are reported. Diffraction data were collected to 2.0 Å resolution using a synchrotron-radiation source.

Indexed as

AnimalsBase SequenceCloning, MolecularCrystallizationCrystallography, X-RayDrosophila ProteinsGTP-Binding Protein alpha Subunits, Gi-GoMolecular Sequence DataPolyethylene GlycolsProtein Structure, TertiaryRGS Proteinsdhit protein, DrosophilaDrosophila ProteinsGTP-Binding Protein alpha Subunits, Gi-GoPolyethylene GlycolsRGS Proteins

Identifiers

PMID23295489
PMCPMC3539706
OpenAlexW2020138204

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.