Evidence map›Paper›PMID 19489109›Full record

ArticleJournal of Zhejiang University. Science. B2009

MoFLP1, encoding a novel fungal fasciclin-like protein, is involved in conidiation and pathogenicity in Magnaporthe oryzae.

Tong-bao Liu, Guo-qing Chen, Hang Min, Fu-cheng Lin

Open access · bronzeAbstract read
In one paragraph

Article in Journal of Zhejiang University. Science. B, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

27 citing papers in PubMed, 62 citations in OpenAlex.

  1. Pyricularia oryzae: Lab star and field scourge.Molecular plant pathology · 2024
    Review
  2. Article
  3. Transcriptome analysis ofFrontiers in microbiology · 2024
    Article
  4. Article
  5. The Devastating Rice Blast Airborne PathogenPathogens (Basel, Switzerland) · 2023
    Review
  6. Unveiling the Secretome of the Fungal Plant PathogenJournal of fungi (Basel, Switzerland) · 2022
    Article
  7. Adhesion as a Focus in Trichoderma-Root Interactions.Journal of fungi (Basel, Switzerland) · 2022
    Review
  8. Article
  9. Article
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  14. Review
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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

4 authors at 2 institutions in 1 country.

Tong-bao LiuState Key Laboratory for Rice Biology, Biotechnology Institute, Zhejiang University, Hangzhou 310029, China.
Guo-qing Chen
Hang Min
Fu-cheng Lin
Zhejiang University · CNChina National Rice Research Institute · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fasciclin family proteins have been identified as cell adhesion molecules in various organisms. In this study, a novel Magnaporthe oryzae fasciclin-like protein encoding gene, named MoFLP1, was isolated from a subtractive suppressive cDNA library and functionally analyzed. Sequence analysis showed that the MoFLP1 gene contains an open reading frame (ORF) of 1050 nucleotides encoding 349 amino acids with a calculated molecular weight of 35.85 kDa and a pI of 7.76. The deduced MoFLP1 protein contains a 17-amino acid secretion signal sequence and an 18-amino acid sequence with the characteristics of a glycosylphosphotidylinositol (GPI) anchor additional signal at its N- and C-terminuses, respectively. Potential N-glycosylation sites and domains involving cell adhesion were also identified in MoFLP1. Sequence analysis and subcellular localization by the expression of MoFLP1-GFP fusion construct in M. oryzae indicated that the MoFLP1 protein is probably localized on the vacuole membrane. Two MoFLP1 null mutants generated by targeted gene disruption exhibited marked reduction of conidiation, conidial adhesion, appressorium turgor, and pathogenicity. Our results indicate that fasciclin proteins play important roles in fungal development and pathogenicity in M. oryzae.

Indexed as

Cell Adhesion MoleculesFungal ProteinsMagnaportheSpores, FungalCell Adhesion MoleculesFungal Proteins

Identifiers

PMID19489109
PMCPMC2689556
OpenAlexW2058712650

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.