Evidence map›Paper›PMID 26284673›Full record

ReviewNature chemical biology2015

The structural biology of biosynthetic megaenzymes.

Kira J Weissman

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.

0numbers the graph read from it
0cells of the map it votes in
103citing 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

103 citing papers in PubMed.

  1. Review
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  10. Review
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  16. Biosynthetic mechanism of the yellow pigments in the marine bacteriumApplied and environmental microbiology · 2024
    Article
  17. Article
  18. Review
  19. Review
  20. Review

43 more citing papers are in PubMed but not listed here.

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.

Kira J WeissmanUMR 7365, Ingénierie Moléculaire et Physiopathologie Articulaire (IMoPA), CNRS-Université de Lorraine, Biopôle de l'Université de Lorraine, Campus Biologie Santé, Vandœuvre-lès-Nancy, France.ORCID 0000000230122960

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The modular polyketide synthases (PKSs) and nonribosomal peptide synthetases (NRPSs) are among the largest and most complicated enzymes in nature. In these biosynthetic systems, independently folding protein domains, which are organized into units called 'modules', operate in assembly-line fashion to construct polymeric chains and tailor their functionalities. Products of PKSs and NRPSs include a number of blockbuster medicines, and this has motivated researchers to understand how they operate so that they can be modified by genetic engineering. Beginning in the 1990s, structural biology has provided a number of key insights. The emerging picture is one of remarkable dynamics and conformational programming in which the chemical states of individual catalytic domains are communicated to the others, configuring the modules for the next stage in the biosynthesis. This unexpected level of complexity most likely accounts for the low success rate of empirical genetic engineering experiments and suggests ways forward for productive megaenzyme synthetic biology.

Indexed as

Bacterial ProteinsCatalytic DomainGene ExpressionGenetic EngineeringKineticsModels, MolecularMultienzyme ComplexesPeptide SynthasesPolyketide SynthasesProtein BiosynthesisProtein FoldingProtein Structure, SecondaryStreptomycesSubstrate SpecificitySynthetic BiologyBacterial ProteinsMultienzyme Complexesnon-ribosomal peptide synthasePeptide SynthasesPolyketide Synthases

Identifiers

PMID26284673

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.