Evidence map›Paper›PMID 20823545›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010

Mammalian cell expression, purification, crystallization and microcrystal data collection of autotaxin/ENPP2, a secreted mammalian glycoprotein.

Jens Hausmann, Evangelos Christodoulou, Mobien Kasiem, Valeria De Marco, Laurens A van Meeteren, Wouter H Moolenaar, Danny Axford, Robin L Owen, Gwyndaf Evans, Anastassis Perrakis

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

13 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Structure-Based Discovery of Novel Chemical Classes of Autotaxin Inhibitors.International journal of molecular sciences · 2020
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Crystallization and preliminary X-ray crystallographic analysis of human autotaxin.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011
    Article
  10. The design of macromolecular crystallography diffraction experiments.Acta crystallographica. Section D, Biological crystallography · 2011
    Article
  11. Article
  12. Article
  13. Crystallization and preliminary X-ray diffraction analysis of rat autotaxin.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    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

10 authors at 2 institutions in 2 countries.

Jens HausmannDivision of Biochemistry B8, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.
Evangelos Christodoulou
Mobien Kasiem
Valeria De Marco
Laurens A van Meeteren
Wouter H Moolenaar
Danny Axford
Robin L Owen
Gwyndaf Evans
Anastassis Perrakis
The Netherlands Cancer Institute · NLDiamond Light Source · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autotaxin (ATX or ENPP2) is a secreted glycosylated mammalian enzyme that exhibits lysophospholipase D activity, hydrolyzing lysophosphatidylcholine to the signalling lipid lysophosphatidic acid. ATX is an approximately 100 kDa multi-domain protein encompassing two N-terminal somatomedin B-like domains, a central catalytic phosphodiesterase domain and a C-terminal nuclease-like domain. Protocols for the efficient expression of ATX from stably transfected mammalian HEK293 cells in amounts sufficient for crystallographic studies are reported. Purification resulted in protein that crystallized readily, but various attempts to grow crystals suitable in size for routine crystallographic structure determination were not successful. However, the available micrometre-thick plates diffracted X-rays beyond 2.0 A resolution and allowed the collection of complete diffraction data to about 2.6 A resolution. The problems encountered and the current advantages and limitations of diffraction data collection from thin crystal plates are discussed.

Indexed as

AnimalsCrystallizationCrystallography, X-RayGene ExpressionGlycoproteinsHEK293 CellsHumansLysophospholipase DPhosphoric Diester HydrolasesPyrophosphatasesRatsGlycoproteinsLysophospholipase DPhosphoric Diester HydrolasesPyrophosphatases

Identifiers

PMID20823545
PMCPMC2935246
OpenAlexW2133193758

What OpenQuestion holds

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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.