Evidence map›Paper›PMID 18487352›Full record

ArticleThe Plant cell2008

Mutation of a rice gene encoding a phenylalanine biosynthetic enzyme results in accumulation of phenylalanine and tryptophan.

Tetsuya Yamada, Fumio Matsuda, Koji Kasai, Shuichi Fukuoka, Keisuke Kitamura, Yuzuru Tozawa, Hisashi Miyagawa, Kyo Wakasa

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed, 1 pooled it
3.0field-weighted citation impact, top 8% 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

36 citing papers in PubMed, 1 synthesis or guideline pooled it, 114 citations in OpenAlex.

  1. Pooled it
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  17. Metabolite Analysis of Jerusalem Artichoke (International journal of molecular sciences · 2021
    Article
  18. 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 4 institutions in 1 country.

Tetsuya YamadaCREST, Japan Science and Technology Agency, Tokyo 103-0027, Japan.
Fumio Matsuda
Koji Kasai
Shuichi Fukuoka
Keisuke Kitamura
Yuzuru Tozawa
Hisashi Miyagawa
Kyo Wakasa
Japan Science and Technology Agency · JPHokkaido University · JPInstitute of Agrobiological Sciences · JPTokyo University of Agriculture · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two distinct biosynthetic pathways for Phe in plants have been proposed: conversion of prephenate to Phe via phenylpyruvate or arogenate. The reactions catalyzed by prephenate dehydratase (PDT) and arogenate dehydratase (ADT) contribute to these respective pathways. The Mtr1 mutant of rice (Oryza sativa) manifests accumulation of Phe, Trp, and several phenylpropanoids, suggesting a link between the synthesis of Phe and Trp. Here, we show that the Mtr1 mutant gene (mtr1-D) encodes a form of rice PDT with a point mutation in the putative allosteric regulatory region of the protein. Transformed callus lines expressing mtr1-D exhibited all the characteristics of Mtr1 callus tissue. Biochemical analysis revealed that rice PDT possesses both PDT and ADT activities, with a preference for arogenate as substrate, suggesting that it functions primarily as an ADT. The wild-type enzyme is feedback regulated by Phe, whereas the mutant enzyme showed a reduced feedback sensitivity, resulting in Phe accumulation. In addition, these observations indicate that rice PDT is critical for regulating the size of the Phe pool in plant cells. Feeding external Phe to wild-type callus tissue and seedlings resulted in Trp accumulation, demonstrating a connection between Phe accumulation and Trp pool size.

Indexed as

MutationAmino Acid SequenceChromatography, LiquidHydro-LyasesModels, BiologicalMolecular Sequence DataMolecular StructurePhenylalaninePlant ProteinsPoint MutationPrephenate DehydrataseSequence Analysis, DNASequence Homology, Amino AcidTandem Mass SpectrometryTryptophanHydro-LyasesPhenylalaninePlant ProteinsPrephenate Dehydratasepretyrosine dehydrataseTryptophan

Identifiers

PMID18487352
PMCPMC2438470
OpenAlexW2145486451

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.