Evidence map›Paper›PMID 30198887›Full record

ArticleActa crystallographica. Section F, Structural biology communications2018

MBP-binding DARPins facilitate the crystallization of an MBP fusion protein.

Rajesh Gumpena, George T Lountos, David S Waugh

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 48% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. A study of flavonoid inhibitors against Monkeypox H1 phosphatase.Journal of enzyme inhibition and medicinal chemistry · 2025
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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

3 authors at 2 institutions in 1 country.

Rajesh GumpenaMacromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, MD 21702, USA.
George T LountosMacromolecular Crystallography Laboratory, Basic Science Program, Leidos Biomedical Research Inc., Frederick National Laboratory for Cancer Research Sponsored by the National Cancer Institute, Frederick, MD 21702, USA.
David S WaughMacromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, MD 21702, USA.
National Cancer Institute · USFrederick National Laboratory for Cancer Research · US

Funding

Protein Engineering CoreZICBC011868 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI WAUGH, DAVID S · 2019 to 2021
$2.5M
CCR NIH HHS HHSN261200800001CNCI NIH HHS HHSN261200800001ENIH HHS HHSN261200800001EU.S. Department of Energy, Office of Science W-31-109-Eng-38
6 · The paper itself

Abstract

The production of high-quality crystals is the main bottleneck in determining the structures of proteins using X-ray crystallography. In addition to being recognized as a very effective solubility-enhancing fusion partner, Escherichia coli maltose-binding protein (MBP) has also been successfully employed as a `fixed-arm' crystallization chaperone in more than 100 cases. Here, it is reported that designed ankyrin-repeat proteins (DARPins) that bind with high affinity to MBP can promote the crystallization of an MBP fusion protein when the fusion protein alone fails to produce diffraction-quality crystals. As a proof of principle, three different co-crystal structures of MBP fused to the catalytic domain of human dual-specificity phosphatase 1 in complex with DARPins are reported.

Indexed as

Amino Acid SequenceBinding SitesCloning, MolecularCrystallizationCrystallography, X-RayDual Specificity Phosphatase 1Escherichia coliGene ExpressionGenetic VectorsHumansMaltose-Binding ProteinsModels, MolecularMolecular ChaperonesProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandDual Specificity Phosphatase 1DUSP1 protein, humanMaltose-Binding ProteinsMolecular ChaperonesRecombinant Fusion Proteinscrystallization chaperonesdesigned ankyrin-repeat proteinsdual-specificity phosphatase 1maltose-binding proteinsurface-entropy-reduction mutagenesis

Identifiers

PMID30198887
PMCPMC6130421
OpenAlexW2889100016

What OpenQuestion holds

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LicenceCC BY
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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.