Evidence map›Paper›PMID 35003157›Full record

ArticleFrontiers in plant science2021

Proteogenic Dipeptides Are Characterized by Diel Fluctuations and Target of Rapamycin Complex-Signaling Dependency in the Model Plant

Maria Juliana Calderan-Rodrigues, Marcin Luzarowski, Carolina Cassano Monte-Bello, Romina I Minen, Boris M Zühlke, Zoran Nikoloski, Aleksandra Skirycz, Camila Caldana

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

8 citing papers in PubMed, 13 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

8 authors at 3 institutions in 2 countries.

Maria Juliana Calderan-RodriguesMax Planck Institute of Molecular Plant Physiology, Potsdam, Germany.
Marcin LuzarowskiMax Planck Institute of Molecular Plant Physiology, Potsdam, Germany.
Carolina Cassano Monte-BelloMax Planck Institute of Molecular Plant Physiology, Potsdam, Germany.
Romina I MinenBoyce Thompson Institute, Ithaca, NY, United States.
Boris M ZühlkeMax Planck Institute of Molecular Plant Physiology, Potsdam, Germany.
Zoran NikoloskiMax Planck Institute of Molecular Plant Physiology, Potsdam, Germany.
Aleksandra SkiryczMax Planck Institute of Molecular Plant Physiology, Potsdam, Germany.
Camila CaldanaMax Planck Institute of Molecular Plant Physiology, Potsdam, Germany.
Max Planck Institute of Molecular Plant Physiology · DEIthaca College · USUniversity of Potsdam · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As autotrophic organisms, plants capture light energy to convert carbon dioxide into ATP, nicotinamide adenine dinucleotide phosphate (NADPH), and sugars, which are essential for the biosynthesis of building blocks, storage, and growth. At night, metabolism and growth can be sustained by mobilizing carbon (C) reserves. In response to changing environmental conditions, such as light-dark cycles, the small-molecule regulation of enzymatic activities is critical for reprogramming cellular metabolism. We have recently demonstrated that proteogenic dipeptides, protein degradation products, act as metabolic switches at the interface of proteostasis and central metabolism in both plants and yeast. Dipeptides accumulate in response to the environmental changes and act

Indexed as

amino acidcarbon limitationdiel cycledipeptidemetabolismprotein-metabolite interactionsTOR signaling

Identifiers

PMID35003157
PMCPMC8727597
OpenAlexW4200509303

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.