Evidence map›Paper›PMID 31209034›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Molecular basis for enantioselective herbicide degradation imparted by aryloxyalkanoate dioxygenases in transgenic plants.

Jonathan R Chekan, Chayanid Ongpipattanakul, Terry R Wright, Bo Zhang, J Martin Bollinger, Lauren J Rajakovich, Carsten Krebs, Robert M Cicchillo, Satish K Nair

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

12 citing papers in PubMed, 26 citations in OpenAlex.

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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

9 authors at 3 institutions in 1 country.

Jonathan R ChekanDepartment of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801.
Chayanid OngpipattanakulDepartment of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801.
Terry R WrightCorteva Agriscience, Agriculture Division of DowDuPont, Indianapolis, IN 46268.ORCID 0000-0002-3969-2812
Bo ZhangDepartment of Chemistry, The Pennsylvania State University, University Park, PA 16802.
J Martin BollingerDepartment of Chemistry, The Pennsylvania State University, University Park, PA 16802.
Lauren J RajakovichDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802.ORCID 0000-0001-5412-1981
Carsten KrebsDepartment of Chemistry, The Pennsylvania State University, University Park, PA 16802.ORCID 0000-0002-3302-7053
Robert M CicchilloCorteva Agriscience, Agriculture Division of DowDuPont, Indianapolis, IN 46268.
Satish K NairDepartment of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801; snair@illinois.edu.
Pennsylvania State University · USUniversity of Illinois Urbana-Champaign · USCorteva (United States) · US

Funding

Mechanisms of Mononuclear non-Heme-Iron EnzymesR35GM127079 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI CARSTEN KREBS · 2018 to 2026
$3.8M
Mechanism of Taurine: Alpha-Ketoglutarate DioxygenaseR01GM069657 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI BOLLINGER, JOSEPH M, KREBS, CARSTEN · 2004 to 2016
$2.7M
NIGMS NIH HHS R01 GM069657NIGMS NIH HHS R35 GM127079
6 · The paper itself

Abstract

The synthetic auxin 2,4-dichlorophenoxyacetic acid (2,4-D) is an active ingredient of thousands of commercial herbicides. Multiple species of bacteria degrade 2,4-D via a pathway initiated by the Fe(II) and α-ketoglutarate (Fe/αKG)-dependent aryloxyalkanoate dioxygenases (AADs). Recently, genes encoding 2 AADs have been deployed commercially in herbicide-tolerant crops. Some AADs can also inactivate chiral phenoxypropionate and aryloxyphenoxypropionate (AOPP) herbicides, albeit with varying substrate enantioselectivities. Certain AAD enzymes, such as AAD-1, have expanded utility in weed control systems by enabling the use of diverse modes of action with a single trait. Here, we report 1) the use of a genomic context-based approach to identify 59 additional members of the AAD class, 2) the biochemical characterization of AAD-2 from

Indexed as

Herbicide Resistance2,4-Dichlorophenoxyacetic AcidDioxygenasesGlycine maxHerbicidesIndoleacetic AcidsPlant ProteinsPlants, Genetically ModifiedProtein Structure, TertiaryStereoisomerismStructure-Activity RelationshipZea mays2,4-Dichlorophenoxyacetic AcidDioxygenasesHerbicidesIndoleacetic AcidsPlant Proteinsauxinenzymeherbicidemechanismresistance

Identifiers

PMID31209034
PMCPMC6613135
OpenAlexW2952856810

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.