Evidence map›Paper›PMID 26850170›Full record

ArticleJournal of structural biology2016

Easy mammalian expression and crystallography of maltose-binding protein-fused human proteins.

Marcel Bokhove, Hamed Sadat Al Hosseini, Takako Saito, Elisa Dioguardi, Katharina Gegenschatz-Schmid, Kaoru Nishimura, Isha Raj, Daniele de Sanctis, Ling Han, Luca Jovine

Open access · hybridAbstract read
In one paragraph

Article in Journal of structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. The N-terminal region of malaria vaccine candidatebioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Structure of the RECK CC domain, an evolutionary anomaly.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Article
  18. Article
  19. Article
  20. 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.

Marcel BokhoveKarolinska Institutet, Department of Biosciences and Nutrition & Center for Innovative Medicine, Huddinge, Sweden.
Hamed Sadat Al HosseiniKarolinska Institutet, Department of Biosciences and Nutrition & Center for Innovative Medicine, Huddinge, Sweden.
Takako SaitoKarolinska Institutet, Department of Biosciences and Nutrition & Center for Innovative Medicine, Huddinge, Sweden.
Elisa DioguardiKarolinska Institutet, Department of Biosciences and Nutrition & Center for Innovative Medicine, Huddinge, Sweden.
Katharina Gegenschatz-SchmidKarolinska Institutet, Department of Biosciences and Nutrition & Center for Innovative Medicine, Huddinge, Sweden.
Kaoru NishimuraKarolinska Institutet, Department of Biosciences and Nutrition & Center for Innovative Medicine, Huddinge, Sweden.
Isha RajKarolinska Institutet, Department of Biosciences and Nutrition & Center for Innovative Medicine, Huddinge, Sweden.
Daniele de SanctisESRF - The European Synchrotron, Grenoble 38000, France.
Ling HanKarolinska Institutet, Department of Biosciences and Nutrition & Center for Innovative Medicine, Huddinge, Sweden.
Luca JovineKarolinska Institutet, Department of Biosciences and Nutrition & Center for Innovative Medicine, Huddinge, Sweden. Electronic address: luca.jovine@ki.se.
Karolinska Institutet · SEEuropean Synchrotron Radiation Facility · FR

Funding

European Research Council 260759
6 · The paper itself

Abstract

We present a strategy to obtain milligrams of highly post-translationally modified eukaryotic proteins, transiently expressed in mammalian cells as rigid or cleavable fusions with a mammalianized version of bacterial maltose-binding protein (mMBP). This variant was engineered to combine mutations that enhance MBP solubility and affinity purification, as well as provide crystal-packing interactions for increased crystallizability. Using this cell type-independent approach, we could increase the expression of secreted and intracellular human proteins up to 200-fold. By molecular replacement with MBP, we readily determined five novel high-resolution structures of rigid fusions of targets that otherwise defied crystallization.

Indexed as

Protein ConformationAmino Acid SequenceAnimalsBacterial ProteinsBase SequenceCHO CellsCricetinaeCricetulusCrystallography, X-RayGene ExpressionHEK293 CellsHumansMaltose-Binding ProteinsModels, MolecularMutationRecombinant Fusion ProteinsBacterial ProteinsMaltose-Binding ProteinsRecombinant Fusion ProteinsCrystallizationGlycoproteinsMaltose-binding protein fusionMammalian cell expressionMolecular replacementX-ray crystallography

Identifiers

PMID26850170
PMCPMC4771870
OpenAlexW2288386302

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.