SH3 domain-containing genes and the subcellular localization of their respective products in <i>F. graminearum.</i>

SH3 domain-containing genes and the subcellular localization of their respective products in <i>F. graminearum.</i>

<p>SH3 domain-containing genes and the subcellular localization of their respective products in <i>F. graminearum.</i></p>

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Bibliographische Detailangaben
1. Verfasser:	Yakubu Saddeeq Abubakar (5558399) (author)
Weitere Verfasser:	Shiqi Ji (20476509) (author), Qiaoli Chen (538344) (author), Huawei Zheng (713784) (author), Zonghua Wang (133934) (author), Wenhui Zheng (133904) (author), Yi Lou (381696) (author)
Veröffentlicht:	2025
Schlagworte:	Biophysics Biochemistry Medicine Microbiology Cell Biology Genetics Developmental Biology Infectious Diseases Plant Biology div >< p conserved molecular scaffolds irregular colony edges form protein condensates dynamic protein assembly remaining 20 proteins plant fungal pathogen idrs largely altered proteins exhibited features fusarium graminearum </ graminearum </ fusarium </ protein interaction plant infection mediate protein irregular septation fungal pathogenesis containing proteins wide characterization varied functions systematically identified src homology septal pore previously characterized potential targets plasma membrane nuclear fragmentation nuclear distribution negative regulators mutant strains multifaceted functions hyphal tip head blight functional diversity completely abolished apical collar
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<i>In silico</i> analysis of intrinsically disordered sequences (IDRs) in the SH3 domain-containing proteins in <i>F. graminearum.</i>
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The file compiles all original, uncropped, and unprocessed data collected in the experiments, including colony diameter, conidia production, conidia size, septa of conidia, DON production, the disease indexes, relative gene expression level.
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qRT-PCR showing the expression of sexual reproduction-responsive genes in Δ<i>Fghof1</i> and Δ<i>Fgrax2</i> mutants.
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Defects of Δ<i>Fgcyk3</i> mutant in nuclear division.
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Effects of <i>FgHOF1</i> deletion on cytoskeletal and nuclear distribution.
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Δ<i>Fghof1</i> mutant could be compromised in cell division.
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