Evidence map›Paper›PMID 34254507›Full record

ReviewAccounts of chemical research2021

Assembly-Line Catalysis in Bifunctional Terpene Synthases.

Jacque L Faylo, Trey A Ronnebaum, David W Christianson

Open access · greenAbstract readReview
In one paragraph

Review in Accounts of chemical research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.8field-weighted citation impact, top 5% 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

32 citing papers in PubMed, 65 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Crystal structure and catalytic mechanism of drimenol synthase, an unusual bifunctional terpene cyclase-phosphatase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Article
  12. Engineering substrate channeling in a bifunctional terpene synthase.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Engineering Substrate Channeling in Assembly-Line Terpene Biosynthesis.bioRxiv : the preprint server for biology · 2024
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Jacque L FayloRoy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6323, United States.
Trey A RonnebaumRoy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6323, United States.
David W ChristiansonRoy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6323, United States.ORCID 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
STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008275 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2018
$6.0M
Understanding Oligomer Assembly of Isoprenoid and Terpene SynthasesF32GM137461 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI RONNEBAUM, TREY ADAM · 2021 to 2022
$77k
NIGMS NIH HHS F32 GM137461NIGMS NIH HHS R01 GM056838NIGMS NIH HHS T32 GM008275
6 · The paper itself

Abstract

The magnificent chemodiversity of more than 95 000 terpenoid natural products identified to date largely originates from catalysis by two types of terpene synthases, prenyltransferases and cyclases. Prenyltransferases utilize 5-carbon building blocks in processive chain elongation reactions to generate linear C

Indexed as

Alkyl and Aryl TransferasesBiocatalysisHumansModels, MolecularAlkyl and Aryl Transferasesterpene synthase

Identifiers

PMID34254507
PMCPMC8530900
OpenAlexW3179452580

What OpenQuestion holds

Textmetadata
LicenceTDM
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.