Evidence map›Paper›PMID 23722843›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013

Crystallization and X-ray diffraction analysis of an antifungal laticifer protein.

Frederico Bruno-Moreno, Raquel Sombra Basílio de Oliveira, Renato de Azevedo Moreira, Marina Duarte Pinto Lobo, Cléverson Diniz Teixeira de Freitas, Márcio Viana Ramos, Thalles Barbosa Grangeiro, Ana Cristina Oliveira Monteiro-Moreira

Open access · bronzeAbstract 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
0.2field-weighted citation impact, top 41% 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, 5 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

8 authors at 2 institutions in 1 country.

Frederico Bruno-MorenoCentro de Ciências da Saúde, Universidade de Fortaleza, Avenida Washington Soares 1321, Bairro Edson Queiroz, 60811-905 Fortaleza-CE, Brazil.
Raquel Sombra Basílio de Oliveira
Renato de Azevedo Moreira
Marina Duarte Pinto Lobo
Cléverson Diniz Teixeira de Freitas
Márcio Viana Ramos
Thalles Barbosa Grangeiro
Ana Cristina Oliveira Monteiro-Moreira
Universidade Federal do Ceará · BRUniversidade de Fortaleza · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An osmotin (CpOsm) from the latex of Calotropis procera has been crystallized in both tetragonal and trigonal forms suitable for structure determination. Crystallographic studies of CpOsm are of great interest because limited information is available concerning the structure of latex proteins and CpOsm has previously been shown to interact with the spore membranes of some plant pathogenic fungi, thus impairing spore germination and hyphal growth. CpOsm crystals were grown using 0.1 M HEPES buffer pH 7.5, 26% PEG 4000, 0.2 M ammonium sulfate (space group P4(3)) or using 0.1 M HEPES buffer pH 7.5, 35% MPD, 0.7 M ammonium sulfate (space group P3(1)12). X-ray diffraction data were collected to 2.17 Å (P4(3)) and 1.80 Å (P3(1)12) resolution and molecular-replacement analyses produced initial phases for both crystal forms.

Indexed as

CalotropisAntifungal AgentsCrystallizationLatexPlant ExtractsPlant ProteinsSpectrometry, Mass, Electrospray IonizationX-Ray DiffractionAntifungal AgentsLatexPlant ExtractsPlant ProteinsCalotropis proceralatex proteinsosmotinsPR-5thaumatin-like proteins

Identifiers

PMID23722843
PMCPMC3668584
OpenAlexW2036556836

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.