Evidence map›Paper›PMID 16511257›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2006

Purification, crystallization and X-ray diffraction analysis of dihydropyrimidinase from Dictyostelium discoideum.

Bernhard Lohkamp, Birgit Andersen, Jure Piskur, Doreen Dobritzsch

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 60% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

4 authors at 1 institution in 1 country.

Bernhard LohkampDepartment of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Birgit Andersen
Jure Piskur
Doreen Dobritzsch
Karolinska Institutet · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dihydropyrimidinase (EC 3.5.2.2) is the second enzyme in the reductive pyrimidine-degradation pathway and catalyses the hydrolysis of 5,6-dihydrouracil and 5,6-dihydrothymine to the corresponding N-carbamylated beta-amino acids. The recombinant enzyme from the slime mould Dictyostelium discoideum was overexpressed, purified and crystallized by the vapour-diffusion method. One crystal diffracted to better than 1.8 A resolution on a synchrotron source and was shown to belong to space group I222, with unit-cell parameters a = 84.6, b = 89.6, c = 134.9 A and one molecule in the asymmetric unit.

Indexed as

AmidohydrolasesAmino Acid SequenceAnimalsCrystallizationCrystallography, X-RayDictyosteliumMolecular Sequence DataProtozoan ProteinsRecombinant ProteinsAmidohydrolasesdihydropyrimidinaseProtozoan ProteinsRecombinant Proteins

Identifiers

PMID16511257
PMCPMC2150923
OpenAlexW2057774921

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.