Evidence map›Paper›PMID 25849510›Full record

ArticleActa crystallographica. Section F, Structural biology communications2015

Crystallization and preliminary X-ray analysis of four cysteine proteases from Ficus carica latex.

Sarah Haesaerts, John Alexander Rodriguez Buitrago, Remy Loris, Danielle Baeyens-Volant, Mohamed Azarkan

Open access · greenAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.0field-weighted citation impact, top 16% 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

7 citing papers in PubMed, 21 citations in OpenAlex.

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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

5 authors at 3 institutions in 1 country.

Sarah HaesaertsStructural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussels, Belgium.
John Alexander Rodriguez BuitragoLaboratoire de Bactériologie Moléculaire, Faculté de Médecine, Université Libre De Bruxelles, Route de Lennik 808, B-1070 Brussels, Belgium.
Remy LorisStructural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussels, Belgium.
Danielle Baeyens-VolantProtein Chemistry Unit, Faculté de Médecine, Université Libre De Bruxelles, Route de Lennik 808, B-1070 Brussels, Belgium.
Mohamed AzarkanProtein Chemistry Unit, Faculté de Médecine, Université Libre De Bruxelles, Route de Lennik 808, B-1070 Brussels, Belgium.
Université Libre de Bruxelles · BEVIB-VUB Center for Structural Biology · BEVrije Universiteit Brussel · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The latex of the common fig (Ficus carica) contains a mixture of at least five cysteine proteases commonly known as ficins (EC 3.4.22.3). Four of these proteases were purified to homogeneity and crystals were obtained in a variety of conditions. The four ficin (iso)forms appear in ten different crystal forms. All diffracted to better than 2.10 Å resolution and for each form at least one crystal form diffracted to 1.60 Å resolution or higher. Ficin (iso)forms B and C share a common crystal form, suggesting close sequence and structural similarity. The latter diffracted to a resolution of 1.20 Å and belonged to space group P3₁21 or P3₂21, with unit-cell parameters a = b = 88.9, c = 55.9 Å.

Indexed as

CrystallizationCrystallography, X-RayCysteine ProteasesFicusLatexPlant ProteinsCysteine ProteasesLatexPlant Proteinscysteine proteaseficinFicus caricapapain

Identifiers

PMID25849510
PMCPMC4388184
OpenAlexW1989693372

What OpenQuestion holds

Textmetadata
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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.