Evidence map›Paper›PMID 15849305›Full record

ArticlePlant physiology2005

A novel short-root gene encodes a glucosamine-6-phosphate acetyltransferase required for maintaining normal root cell shape in rice.

Huawu Jiang, Shaomin Wang, Lei Dang, Shoufeng Wang, Hanmin Chen, Yunrong Wu, Xinhang Jiang, Ping Wu

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

25 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Frontiers in plant science · 2022
    Article
  6. Interference of ArabidopsisFrontiers in plant science · 2022
    Article
  7. Article
  8. Review
  9. UDP-Frontiers in plant science · 2021
    Article
  10. Article
  11. International journal of molecular sciences · 2020
    Article
  12. The Temperature-Dependent Retention of Introns inInternational journal of molecular sciences · 2019
    Article
  13. Article
  14. Review
  15. Frontiers in plant science · 2018
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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.

Huawu JiangState Key Laboratory of Plant Physiology and Biochemistry, College of Life Sciences, Zhejiang University, Hangzhou 310029, People's Republic of China.
Shaomin Wang
Lei Dang
Shoufeng Wang
Hanmin Chen
Yunrong Wu
Xinhang Jiang
Ping Wu
State Key Laboratory of Plant Physiology and BiochemistryZhejiang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosylation is a posttranslational modification occurring in many secreted and membrane-associated proteins in eukaryotes. It plays important roles in both physiological and pathological processes. Most of these protein modifications depend on UDP-N-acetylglucosamine. In this study, a T-DNA insertional rice (Oryza sativa) mutant exhibiting a temperature-sensitive defect in root elongation was isolated. Genetic and molecular analysis indicated that the mutated phenotype was caused by loss of function of a gene encoding a glucosamine-6-P acetyltransferase (designated OsGNA1), which is involved in de novo UDP-N-acetylglucosamine biosynthesis. The aberrant root morphology of the gna1 mutant includes shortening of roots, disruption of microtubules, and shrinkage of cells in the root elongation zone. Our observations support the idea that protein glycosylation plays a key role in cell metabolism, microtubule stabilization, and cell shape in rice roots.

Indexed as

AcetyltransferasesAmino Acid SequenceCell ShapeCloning, MolecularConsensus SequenceGlucosamine 6-Phosphate N-AcetyltransferaseKineticsMolecular Sequence DataOryzaPhenotypePlant RootsRestriction MappingSequence AlignmentSequence Homology, Amino AcidAcetyltransferasesGlucosamine 6-Phosphate N-Acetyltransferase

Identifiers

PMID15849305
PMCPMC1104178
OpenAlexW2095732134

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.