Evidence map›Paper›PMID 35670759›Full record

ArticleThe Plant cell2022

Proteomic and metabolic disturbances in lignin-modified Brachypodium distachyon.

Jaime Barros, Him K Shrestha, Juan C Serrani-Yarce, Nancy L Engle, Paul E Abraham, Timothy J Tschaplinski, Robert L Hettich, Richard A Dixon

Open access · hybridAbstract read
In one paragraph

Article in The Plant cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

20 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
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  7. Review
  8. Article
  9. Plant stress and proteomics in medicinal plants.Frontiers in plant science · 2025
    Review
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  11. Article
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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 2 institutions in 1 country.

Jaime BarrosBioDiscovery Institute and Department of Biological Sciences, University of North Texas, Denton, Texas 76201, USA.ORCID 0000-0002-9545-312X
Him K ShresthaBiosciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37830, USA.ORCID 0000-0001-9686-357X
Juan C Serrani-YarceBioDiscovery Institute and Department of Biological Sciences, University of North Texas, Denton, Texas 76201, USA.ORCID 0000-0002-0550-9450
Nancy L EngleBioDiscovery Institute and Department of Biological Sciences, University of North Texas, Denton, Texas 76201, USA.ORCID 0000-0003-0290-7987
Paul E AbrahamCenter for Bioenergy Innovation (CBI), Oak Ridge National Laboratory, Oak Ridge, Tennessee 37830, USA.ORCID 0000-0003-2685-9123
Timothy J TschaplinskiCenter for Bioenergy Innovation (CBI), Oak Ridge National Laboratory, Oak Ridge, Tennessee 37830, USA.ORCID 0000-0002-9540-6622
Robert L HettichCenter for Bioenergy Innovation (CBI), Oak Ridge National Laboratory, Oak Ridge, Tennessee 37830, USA.ORCID 0000-0001-7708-786X
Richard A DixonBioDiscovery Institute and Department of Biological Sciences, University of North Texas, Denton, Texas 76201, USA.ORCID 0000-0001-8393-9408
Oak Ridge National Laboratory · USUniversity of North Texas · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lignin biosynthesis begins with the deamination of phenylalanine and tyrosine (Tyr) as a key branch point between primary and secondary metabolism in land plants. Here, we used a systems biology approach to investigate the global metabolic responses to lignin pathway perturbations in the model grass Brachypodium distachyon. We identified the lignin biosynthetic protein families and found that ammonia-lyases (ALs) are among the most abundant proteins in lignifying tissues in grasses. Integrated metabolomic and proteomic data support a link between lignin biosynthesis and primary metabolism mediated by the ammonia released from ALs that is recycled for the synthesis of amino acids via glutamine. RNA interference knockdown of lignin genes confirmed that the route of the canonical pathway using shikimate ester intermediates is not essential for lignin formation in Brachypodium, and there is an alternative pathway from Tyr via sinapic acid for the synthesis of syringyl lignin involving yet uncharacterized enzymatic steps. Our findings support a model in which plant ALs play a central role in coordinating the allocation of carbon for lignin synthesis and the nitrogen available for plant growth. Collectively, these data also emphasize the value of integrative multiomic analyses to advance our understanding of plant metabolism.

Indexed as

BrachypodiumLigninPlant ProteinsProteomicsLigninPlant Proteins

Identifiers

PMID35670759
PMCPMC9421481
OpenAlexW4281779189

What OpenQuestion holds

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LicenceCC BY
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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.