Evidence map›Paper›PMID 26682969›Full record

ReviewProtein science : a publication of the Protein Society2016

Crystal structures of MBP fusion proteins.

David S Waugh

Open access · bronzeAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

28 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
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  4. X-ray crystal structure of a designed rigidified imaging scaffold in the ligand-free conformation.Acta crystallographica. Section F, Structural biology communications · 2024
    Article
  5. Expression and kinetic characterization of PYCR3.Archives of biochemistry and biophysics · 2023
    Article
  6. Article
  7. Cryo-EM structure determination of small proteins by nanobody-binding scaffolds (Legobodies).Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Innovation versus practice in biological crystallization.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  15. Structure of the RECK CC domain, an evolutionary anomaly.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. 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

1 author at 1 institution in 1 country.

David S WaughProtein Engineering Section, Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, P.O. Box B, Frederick, Maryland, 21702-1201.
Center for Cancer Research · US

Funding

Structural studies of molecular targets for drug developmentZIABC011551 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WAUGH, DAVID S · 2014 to 2018
$4.5M
Protein Expression and Purification in the Fast LaneZIABC010341 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WAUGH, DAVID S · 2009 to 2018
$4.3M
6 · The paper itself

Abstract

Although chaperone-assisted protein crystallization remains a comparatively rare undertaking, the number of crystal structures of polypeptides fused to maltose-binding protein (MBP) that have been deposited in the Protein Data Bank (PDB) has grown dramatically during the past decade. Altogether, 102 fusion protein structures were detected by Basic Local Alignment Search Tool (BLAST) analysis. Collectively, these structures comprise a range of sizes, space groups, and resolutions that are typical of the PDB as a whole. While most of these MBP fusion proteins were equipped with short inter-domain linkers to increase their rigidity, fusion proteins with long linkers have also been crystallized. In some cases, surface entropy reduction mutations in MBP appear to have facilitated the formation of crystals. A comparison of the structures of fused and unfused proteins, where both are available, reveals that MBP-mediated structural distortions are very rare.

Indexed as

Amino Acid SequenceAnimalsCloning, MolecularCrystallizationCrystallographyEntropyHumansMaltose-Binding ProteinsModels, MolecularMolecular ChaperonesMutationPeptidesProtein ConformationRecombinant Fusion ProteinsMaltose-Binding ProteinsMolecular ChaperonesPeptidesRecombinant Fusion Proteinschaperone-assisted crystallizationcrystallization chaperonecrystallization tagmaltose-binding proteinMBP fusion proteinsurface entropy reduction mutagenesis

Identifiers

PMID26682969
PMCPMC4815407
OpenAlexW2219158342

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.