Evidence map›Paper›PMID 24557139›Full record

ArticleNature chemistry2014

A protein engineered to bind uranyl selectively and with femtomolar affinity.

Lu Zhou, Mike Bosscher, Changsheng Zhang, Salih Ozçubukçu, Liang Zhang, Wen Zhang, Charles J Li, Jianzhao Liu, Mark P Jensen, Luhua Lai and 1 more

Abstract read
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Article in Nature chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
–field-weighted citation impact
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

50 citing papers in PubMed.

  1. Article
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  3. Review
  4. Conditional Protein Structure Generation with Protpardelle-1c.bioRxiv : the preprint server for biology · 2025
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  11. Characterization of Uranyl (UOACS chemical neuroscience · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Protein-protein interaction prediction with deep learning: A comprehensive review.Computational and structural biotechnology journal · 2022
    Review
  20. De novo metalloprotein design.Nature reviews. Chemistry · 2022
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors.

Lu Zhou1] Department of Chemistry and Institute for Biophysical Dynamics, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA [2].
Mike Bosscher1] Department of Chemistry and Institute for Biophysical Dynamics, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA [2].
Changsheng Zhang1] BNLMS, State Key Laboratory for Structural Chemistry of Unstable and Stable Species, College of Chemistry and Molecular Engineering and Center for Quantitative Biology, Peking University, Beijing 100871, China [2] Center for Life Sciences, Peking University, Beijing 100871, China [3].
Salih OzçubukçuDepartment of Chemistry and Institute for Biophysical Dynamics, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
Liang ZhangDepartment of Chemistry and Institute for Biophysical Dynamics, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
Wen ZhangDepartment of Chemistry and Institute for Biophysical Dynamics, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
Charles J LiDepartment of Chemistry and Institute for Biophysical Dynamics, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
Jianzhao LiuDepartment of Chemistry and Institute for Biophysical Dynamics, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
Mark P JensenChemical Sciences and Engineering Division, Argonne National Laboratory, Argonne, Illinois 60439, USA.
Luhua Lai1] BNLMS, State Key Laboratory for Structural Chemistry of Unstable and Stable Species, College of Chemistry and Molecular Engineering and Center for Quantitative Biology, Peking University, Beijing 100871, China [2] Center for Life Sciences, Peking University, Beijing 100871, China.
Chuan HeDepartment of Chemistry and Institute for Biophysical Dynamics, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Uranyl (UO2(2+)), the predominant aerobic form of uranium, is present in the ocean at a concentration of ~3.2 parts per 10(9) (13.7 nM); however, the successful enrichment of uranyl from this vast resource has been limited by the high concentrations of metal ions of similar size and charge, which makes it difficult to design a binding motif that is selective for uranyl. Here we report the design and rational development of a uranyl-binding protein using a computational screening process in the initial search for potential uranyl-binding sites. The engineered protein is thermally stable and offers very high affinity and selectivity for uranyl with a Kd of 7.4 femtomolar (fM) and >10,000-fold selectivity over other metal ions. We also demonstrated that the uranyl-binding protein can repeatedly sequester 30-60% of the uranyl in synthetic sea water. The chemical strategy employed here may be applied to engineer other selective metal-binding proteins for biotechnology and remediation applications.

Indexed as

Binding SitesMetal NanoparticlesModels, MolecularProtein EngineeringProteinsUraniumProteinsUranium

Identifiers

PMID24557139

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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.