Evidence map›Paper›PMID 24390158›Full record

ArticlePlant signaling & behavior2013

Silencing ribulose-1,5-bisphosphate carboxylase/oxygenase expression does not disrupt nitrogen allocation to defense after simulated herbivory in Nicotiana attenuata.

Mariana A Stanton, Lynn Ullmann-Zeunert, Natalie Wielsch, Stefan Bartram, Aleš Svatoš, Ian T Baldwin, Karin Groten

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Article in Plant signaling & behavior, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.3field-weighted citation impact, top 39% 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

5 citing papers in PubMed, 9 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

7 authors at 1 institution in 2 countries.

Mariana A StantonDepartment of Molecular Ecology; Max Planck Institute for Chemical Ecology; Jena, Germany.
Lynn Ullmann-ZeunertDepartment of Molecular Ecology; Max Planck Institute for Chemical Ecology; Jena, Germany; Qiagen; Hilden, Germany.
Natalie WielschMS Group; Max Planck Institute for Chemical Ecology; Jena, Germany.
Stefan BartramDepartment of Bioorganic Chemistry; Max Planck Institute for Chemical Ecology; Jena, Germany.
Aleš SvatošMS Group; Max Planck Institute for Chemical Ecology; Jena, Germany.
Ian T BaldwinDepartment of Molecular Ecology; Max Planck Institute for Chemical Ecology; Jena, Germany.
Karin GrotenDepartment of Molecular Ecology; Max Planck Institute for Chemical Ecology; Jena, Germany.
Max Planck Institute for Chemical Ecology · DE

Funding

European Research Council 293926
6 · The paper itself

Abstract

Ribulose-1,5-bisphosphate carboxylase/ oxygenase (RuBisCO) is the most abundant protein on the planet and in addition to its central role in photosynthesis it is thought to function as a nitrogen (N)-storage protein and a potential source of N for defense biosynthesis in plants. In a recent study in the wild tobacco Nicotiana attenuata, we showed that the decrease in absolute N invested in soluble proteins and RuBisCO elicited by simulated herbivory was much larger than the N-requirements of nicotine and phenolamide biosynthesis; (15)N flux studies revealed that N for defensive phenolamide synthesis originates from recently assimilated N rather than from RuBisCO turnover. Here we show that a transgenic line of N. attenuata silenced in the expression of RuBisCO (asRUB) invests similar or even larger amounts of N into phenolamide biosynthesis compared with wild type plants, consistent with our previous conclusion that recently assimilated N is channeled into phenolamide synthesis after elicitation. We suggest that the decrease in leaf proteins after simulated herbivory is a tolerance mechanism, rather than a consequence of N-demand for defense biosynthesis.

Indexed as

Gene SilencingAnimalsHerbivoryManducaModels, BiologicalNicotianaNicotineNitrogenNitrogen IsotopesProtein SubunitsPutrescineRibulose-Bisphosphate CarboxylaseSpermidineNicotineNitrogenNitrogen IsotopesProtein SubunitsPutrescineRibulose-Bisphosphate CarboxylaseSpermidinecaffeoyl-putrescinedicaffeoyl-spermidinegrowth-defense trade-offribulose-1,5-bisphosphate carboxylase/ oxygenasetotal soluble protein

Identifiers

PMID24390158
PMCPMC4091567
OpenAlexW1982698875

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.