Evidence map›Paper›PMID 22907771›Full record

ReviewNatural product reports2012

Terpenoid synthase structures: a so far incomplete view of complex catalysis.

Yang Gao, Richard B Honzatko, Reuben J Peters

Abstract readReview
In one paragraph

Review in Natural product reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 164 papers.

0numbers the graph read from it
0cells of the map it votes in
164citing papers in PubMed
8.7field-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

164 citing papers in PubMed, 354 citations in OpenAlex.

  1. Terpenoids fromPlants (Basel, Switzerland) · 2026
    Review
  2. Article
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  17. Review
  18. Characteristics and Functions ofInternational journal of molecular sciences · 2025
    Article
  19. Article
  20. Engineering substrate channeling in a bifunctional terpene synthase.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article

104 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

3 authors at 1 institution in 1 country.

Yang GaoDepartment of Biochemistry, Biophysics, & Molecular Biology, Iowa State University, Ames, IA 50011, USA.
Richard B Honzatko
Reuben J Peters
Iowa State University · US

Funding

REGULATORY ENZYMES OF GLYCOLYSIS AND GLUCONEOGENESISR01NS010546 · NINDS · IOWA STATE UNIVERSITY · PI HONZATKO, RICHARD B · 1985 to 2011
$3.6M
Enzymatic formation of the hydrocarbon skeletons underlying diterpenoid diversityR01GM076324 · NIGMS · IOWA STATE UNIVERSITY · PI PETERS, REUBEN JOHN · 2006 to 2019
$3.4M
Regulatory Enzymes of Glycolysis and GluconeogenesisR56NS010546 · NINDS · IOWA STATE UNIVERSITY · PI FROMM, HERBERT JEROME · 2007 to 2007
$358k
TARGETING OF PROTEINS TO THE NEUROMUSCULAR JUNCTIONF32NS010546 · NINDS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI KAMMESHEIDT, ANJA · 1997 to 1999
–
NIGMS NIH HHS GM076324NIGMS NIH HHS R01 GM076324NINDS NIH HHS F32 NS010546NINDS NIH HHS NS010546NINDS NIH HHS R01 NS010546NINDS NIH HHS R56 NS010546
6 · The paper itself

Abstract

The complexity of terpenoid natural products has drawn significant interest, particularly since their common (poly)isoprenyl origins were discovered. Notably, much of this complexity is derived from the highly variable cyclized and/or rearranged nature of the observed hydrocarbon skeletal structures. Indeed, at least in some cases it is difficult to immediately recognize their derivation from poly-isoprenyl precursors. Nevertheless, these diverse structures are formed by sequential elongation to acyclic precursors, most often with subsequent cyclization and/or rearrangement. Strikingly, the reactions used to assemble and diversify terpenoid backbones share a common carbocationic driven mechanism, although the means by which the initial carbocation is generated does vary. High-resolution crystal structures have been obtained for at least representative examples from each of the various types of enzymes involved in producing terpenoid hydrocarbon backbones. However, while this has certainly led to some insights into the enzymatic structure-function relationships underlying the elongation and simpler cyclization reactions, our understanding of the more complex cyclization and/or rearrangement reactions remains limited. Accordingly, selected examples are discussed here to demonstrate our current understanding, its limits, and potential ways forward.

Indexed as

Alkyl and Aryl TransferasesCatalysisMolecular StructureProtein ConformationStructure-Activity RelationshipTerpenesAlkyl and Aryl TransferasesTerpenesterpene synthase

Identifiers

PMID22907771
PMCPMC3448952
OpenAlexW2014796703

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.