Back to search

Article

iTRAQ-based proteomic and phosphoproteomic analyses of STRIPAK mutants from the fungus <i>Sordaria macrospora</i> identifies a conserved serine phosphorylation site in PAK kinase CLA4 to be important for sexual development and polarized growth

2019-11-04

Abstract excerpt

<h4>Summary</h4> The highly conserved striatin-interacting phosphatases and kinases (STRIPAK) complex regulates phosphorylation of developmental proteins in eukaryotic microorganisms, animals, and humans. To first identify potential targets of STRIPAK, we performed extensive isobaric tags for relative and absolute quantification (iTRAQ)-based proteomic and phosphoproteomic analyses in the filamentous fungus Sord...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work
7484f2f2-60b8-5ba4-abcd-945f226649c1
DOI
10.1101/828111
Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest
Interactive article relationship graphSelect a related publication card to move it into the centre and load its closest explainable connections. Solid lines are source-backed structured connections. Dashed lines are semantic discovery signals and are not scientific evidence.
iTRAQ-based proteomic and phosphoproteomic analyses of STRIPAK mutants from the fungus <i>Sordaria macrospora</i> identifies a conserved serine phosphorylation site in PAK kinase CLA4 to be important for sexual development and polarized growthDOI 10.1101/828111
Select a neighboring publication to make it the new centre.