Evidence map›Paper›PMID 19632140›Full record

ReviewCurrent opinion in chemical biology2009

Mechanistic advances in plant natural product enzymes.

Aimee R Usera, Sarah E O'Connor

Open access · greenAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Current opinion in chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

1 citing paper in PubMed, 10 citations in OpenAlex.

  1. Natural products as chemical probes.ACS chemical biology · 2010
    Review
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 at 1 institution in 1 country.

Aimee R UseraMassachusetts Institute of Technology, Department of Chemistry, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
Sarah E O'Connor
Massachusetts Institute of Technology · US

Funding

Early Steps in Alkaloid BiosynthesisR01GM074820 · NIGMS · UNIVERSITY OF EAST ANGLIA · PI O'CONNOR, SARAH E · 2007 to 2011
$1.5M
Fluorescence Sensing of NO: Development of Reversible Sensors Using Fe(III)F32GM085930 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI PLUTH, MICHAEL · 2008 to 2009
$76k
NIGMS NIH HHS F32 GM085930NIGMS NIH HHS GM 074820NIGMS NIH HHS GM 085930NIGMS NIH HHS R01 GM074820
6 · The paper itself

Abstract

The biosynthetic pathways of plant natural products offer an abundance of knowledge to scientists in many fields. Synthetic chemists can be inspired by the synthetic strategies that nature uses to construct these compounds. Chemical and biological engineers are working to reprogram these biosynthetic pathways to more efficiently produce valuable products. Finally, biochemists and enzymologists are interested in the detailed mechanisms of the complex transformations involved in the construction of these natural products. Study of biosynthetic enzymes and pathways therefore has a wide-ranging impact. In recent years, many plant biosynthetic pathways have been characterized, particularly the pathways that are responsible for alkaloid biosynthesis. Here we highlight recently studied alkaloid biosynthetic enzymes that catalyze production of numerous complex medicinal compounds, as well as the specifier proteins in glucosinosolate biosynthesis, whose structure and mechanism of action are just beginning to be unraveled.

Indexed as

AlkaloidsBiological ProductsGlucosinolatesPlantsAlkaloidsBiological ProductsGlucosinolates

Identifiers

PMID19632140
PMCPMC2749912
OpenAlexW1969173934

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.