Evidence map›Paper›PMID 28841019›Full record

ReviewChemical reviews2017

Structural and Chemical Biology of Terpenoid Cyclases.

David W Christianson

Erratum issuedAbstract readReview
In one paragraph

Review in Chemical reviews, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 481 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
481citing papers in PubMed, 1 pooled it
31.2field-weighted citation impact, top 1% 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

481 citing papers in PubMed, 1 synthesis or guideline pooled it, 1,143 citations in OpenAlex.

  1. Molecules (Basel, Switzerland) · 2024
    Pooled it
  2. Diverse oxidosqualene cyclases for triterpenoid biosynthesis.Synthetic and systems biotechnology · 2027
    Review
  3. Article
  4. Article
  5. Review
  6. Metal dependent regulation of sesquiterpene biosynthesis and redox signalling in Santalum album.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Construction of a globally modular recombinantSynthetic and systems biotechnology · 2026
    Article
  15. Article
  16. Article
  17. The Catalytic Asymmetric Alkylation of Olefins with Alcohol Derivatives.Journal of the American Chemical Society · 2026
    Article
  18. Article
  19. Article
  20. Investigations of the Evolved Molecular Basis for Terpenoid Biosynthesis in Marine Sponges.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

David W ChristiansonRoy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania , 231 South 34th Street, Philadelphia, Pennsylvania 19104-6323, United States.ORCID http://orcid.org/0000-0002-0194-5212
University of Pennsylvania · US

Funding

STRUCTURE/FUNCTION OF BIOSYNTHETIC ENZYMESR01GM056838 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI CHRISTIANSON, DAVID W · 1998 to 2025
$8.0M
NIGMS NIH HHS R01 GM056838
6 · The paper itself

Abstract

The year 2017 marks the twentieth anniversary of terpenoid cyclase structural biology: a trio of terpenoid cyclase structures reported together in 1997 were the first to set the foundation for understanding the enzymes largely responsible for the exquisite chemodiversity of more than 80000 terpenoid natural products. Terpenoid cyclases catalyze the most complex chemical reactions in biology, in that more than half of the substrate carbon atoms undergo changes in bonding and hybridization during a single enzyme-catalyzed cyclization reaction. The past two decades have witnessed structural, functional, and computational studies illuminating the modes of substrate activation that initiate the cyclization cascade, the management and manipulation of high-energy carbocation intermediates that propagate the cyclization cascade, and the chemical strategies that terminate the cyclization cascade. The role of the terpenoid cyclase as a template for catalysis is paramount to its function, and protein engineering can be used to reprogram the cyclization cascade to generate alternative and commercially important products. Here, I review key advances in terpenoid cyclase structural and chemical biology, focusing mainly on terpenoid cyclases and related prenyltransferases for which X-ray crystal structures have informed and advanced our understanding of enzyme structure and function.

Indexed as

Alkyl and Aryl TransferasesCarbon-Carbon LyasesCrystallography, X-RayDimethylallyltranstransferaseIntramolecular LyasesProtein Structure, TertiaryTerpenesAlkyl and Aryl TransferasesCarbon-Carbon LyasesDimethylallyltranstransferaseIntramolecular Lyasespinene cyclase Iterpene carbocyclaseTerpenestrichodiene synthetase

Identifiers

PMID28841019
PMCPMC5599884
OpenAlexW2750432728

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.