Evidence map›Paper›PMID 26821641›Full record

ReviewProtein science : a publication of the Protein Society2016

Why reinvent the wheel? Building new proteins based on ready-made parts.

Olga Khersonsky, Sarel J Fleishman

Abstract 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 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Review
  2. Context-dependent design of induced-fit enzymes using deep learning generates well-expressed, thermally stable and active enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Review
  4. Review
  5. Review
  6. Protein-protein interaction prediction with deep learning: A comprehensive review.Computational and structural biotechnology journal · 2022
    Review
  7. Review
  8. Review
  9. Article
  10. Tight and specific lanthanide binding in a de novo TIM barrel with a large internal cavity designed by symmetric domain fusion.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Harnessing Conformational Plasticity to Generate Designer Enzymes.Journal of the American Chemical Society · 2020
    Review
  12. A general-purpose protein design framework based on mining sequence-structure relationships in known protein structures.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Principles for computational design of binding antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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

2 authors.

Olga KhersonskyDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, 76100, Israel.
Sarel J FleishmanDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, 76100, Israel.

Funding

European Research Council 335439
6 · The paper itself

Abstract

We protein engineers are ambivalent about evolution: on the one hand, evolution inspires us with myriad examples of biomolecular binders, sensors, and catalysts; on the other hand, these examples are seldom well-adapted to the engineering tasks we have in mind. Protein engineers have therefore modified natural proteins by point substitutions and fragment exchanges in an effort to generate new functions. A counterpoint to such design efforts, which is being pursued now with greater success, is to completely eschew the starting materials provided by nature and to design new protein functions from scratch by using de novo molecular modeling and design. While important progress has been made in both directions, some areas of protein design are still beyond reach. To this end, we advocate a synthesis of these two strategies: by using design calculations to both recombine and optimize fragments from natural proteins, we can build stable and as of yet un-sampled structures, thereby granting access to an expanded repertoire of conformations and desired functions. We propose that future methods that combine phylogenetic analysis, structure and sequence bioinformatics, and atomistic modeling may well succeed where any one of these approaches has failed on its own.

Indexed as

Catalytic DomainComputational BiologyEvolution, MolecularModels, MolecularPhylogenyProtein ConformationProtein EngineeringProteinsProteinsantibodybioinformaticsevolutionprotein designRosettaβ-propellerβ/α barrel

Identifiers

PMID26821641
PMCPMC4918424

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.