Evidence map›Paper›PMID 15643068›Full record

ArticleEukaryotic cell2005

Role for RNA-binding proteins implicated in pathogenic development of Ustilago maydis.

Philip Becht, Evelyn Vollmeister, Michael Feldbrügge

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2005. 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
4.6field-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. Deciphering the RNA-binding protein network during endosomal mRNA transport.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. The serine-arginine (SR) protein UmRrm75 from Ustilago maydis is a functional ortholog of yeast ScHrb1.International microbiology : the official journal of the Spanish Society for Microbiology · 2024
    Article
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  4. Kinesin Motors in the Filamentous Basidiomycetes in Light of theJournal of fungi (Basel, Switzerland) · 2022
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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

3 authors at 2 institutions in 1 country.

Philip BechtDepartment of Organismic Interactions, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.
Evelyn Vollmeister
Michael Feldbrügge
Max Planck Institute for Terrestrial Microbiology · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ustilago maydis causes smut disease on corn. Successful infection depends on a number of morphological transitions, such as pheromone-dependent formation of conjugation tubes and the switch to filamentous dikaryotic growth, as well as different types of mycelial structures during growth within the host plant. In order to address the involvement of RNA-binding proteins during this developmental program, we identified 27 open reading frames from the genome sequence encoding potential RNA-binding proteins. They exhibit similarities to RNA-binding proteins with Pumilio homology domains (PUM), the K homology domain (KHD), the double-stranded RNA binding motif (DSRM), and the RNA recognition motif (RRM). For 18 of these genes, we generated replacement mutants in compatible haploid strains. Through analysis of growth behavior, morphology, cyclic AMP response, mating, and pathogenicity, we identified three candidates with aberrant phenotypes. Loss of Khd1, a K homology protein containing three KHDs, resulted in a cold-sensitive growth phenotype. Deletion of khd4 encoding a protein with five KHDs led to abnormal cell morphology, reduced mating, and virulence. rrm4Delta strains were affected in filamentous growth and pathogenicity. Rrm4 is an RRM protein with a so far unique domain organization consisting of three N-terminal RRMs as well as a domain found in the C terminus of poly(A)-binding proteins. These results indicate a role for RNA-binding proteins in regulation of morphology as well as in pathogenic development in U. maydis.

Indexed as

Alternative SplicingAmino Acid MotifsAnimalsComputational BiologyCyclic AMPGene DeletionModels, GeneticMutationOpen Reading FramesPhenotypePhylogenyProtein BindingProtein Structure, TertiaryRNARNA-Binding ProteinsRNA, MessengerCyclic AMPRNARNA-Binding ProteinsRNA, Messenger

Identifiers

PMID15643068
PMCPMC544158
OpenAlexW2096168662

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.