Evidence map›Paper›PMID 18626786›Full record

ReviewPhotosynthesis research

Directing the evolution of Rubisco and Rubisco activase: first impressions of a new tool for photosynthesis research.

Oliver Mueller-Cajar, Spencer M Whitney

Open access · hybridAbstract readReview
In one paragraph

Review in Photosynthesis research. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

34 citing papers in PubMed, 89 citations in OpenAlex.

  1. Review
  2. Review
  3. Enzymatic Conversion of COChemical reviews · 2023
    Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
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  12. An improvedThe Journal of biological chemistry · 2018
    Article
  13. Article
  14. Review
  15. Article
  16. Towards engineering carboxysomes into C3 plants.The Plant journal : for cell and molecular biology · 2016
    Article
  17. Article
  18. Article
  19. Improving recombinant Rubisco biogenesis, plant photosynthesis and growth by coexpressing its ancillary RAF1 chaperone.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  20. Biocatalysis for the application of CO2 as a chemical feedstock.Beilstein journal of organic chemistry · 2015
    Review
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 at 2 institutions in 2 countries.

Oliver Mueller-CajarMolecular Plant Physiology, Research School of Biological Sciences, Australian National University, Canberra, Australian Capital Territory 2601, Australia.
Spencer M Whitney
Australian National University · AUMax Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During the last decade the practice of laboratory-directed protein evolution has become firmly established as a versatile tool in biochemical research by enabling molecular evolution toward desirable phenotypes or detection of novel structure-function interactions. Applications of this technique in the field of photosynthesis research are still in their infancy, but recently first steps have been reported in the directed evolution of the CO(2)-fixing enzyme Rubisco and its helper protein Rubisco activase. Here we summarize directed protein evolution strategies and review the progressive advances that have been made to develop and apply suitable selection systems for screening mutant forms of these enzymes that improve the fitness of the host organism. The goal of increasing photosynthetic efficiency of plants by improving the kinetics of Rubisco has been a long-term goal scoring modest successes. We discuss how directed evolution methodologies may one day be able to circumvent the problems encountered during this venture.

Indexed as

Directed Molecular EvolutionEvolution, MolecularPhotosynthesisPlant ProteinsRibulose-Bisphosphate CarboxylaseSelection, GeneticPlant Proteinsrca protein, plantRibulose-Bisphosphate Carboxylase

Identifiers

PMID18626786
PMCPMC2758363
OpenAlexW2059030608

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.