Evidence map›Paper›PMID 29849027›Full record

ReviewNature communications2018

The role of dynamic enzyme assemblies and substrate channelling in metabolic regulation.

Lee J Sweetlove, Alisdair R Fernie

Abstract readReview
In one paragraph

Review in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 179 papers.

0numbers the graph read from it
0cells of the map it votes in
179citing 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

179 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Molecular architecture of the human citrate synthase-malate dehydrogenase 2 metabolon.Acta crystallographica. Section D, Structural biology · 2026
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Lessons, connections, hypotheses and predictions from protein film electrochemistry.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Review

119 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

2 authors.

Lee J SweetloveDepartment of Plant Sciences, University of Oxford, South Parks Road, Oxford, OX1 3RB, UK. lee.sweetlove@plants.ox.ac.uk.
Alisdair R FernieMax-Planck-Institut für Molekulare Pflanzenphysiologie, Potsdam-Golm, 14476, Germany. fernie@mpimp-golm.mpg.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transient physical association between enzymes appears to be a cardinal feature of metabolic systems, yet the purpose of this metabolic organisation remains enigmatic. It is generally assumed that substrate channelling occurs in these complexes. However, there is a lack of information concerning the mechanisms and extent of substrate channelling and confusion regarding the consequences of substrate channelling. In this review, we outline recent advances in the structural characterisation of enzyme assemblies and integrate this with new insights from reaction-diffusion modelling and synthetic biology to clarify the mechanistic and functional significance of the phenomenon.

Indexed as

Allosteric RegulationEnergy MetabolismModels, BiologicalAnimalsBacteriaBiocatalysisEnzymesHumansMetabolic Networks and PathwaysSubstrate SpecificityEnzymes

Identifiers

PMID29849027
PMCPMC5976638

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.