Waterlogging stress leads to a reduction in the oxygen level around the root system (hypoxia). It can be caused by poor air exchange in flooded or compacted soil or in a non-aerated medium.
Anna Kołton +6 more
doaj +1 more source
Cell cycle regulation of a Xenopus Wee1-like kinase [PDF]
Using a polymerase chain reaction-based strategy, we have isolated a gene encoding a Wee1-like kinase from Xenopus eggs. The recombinant Xenopus Wee1 protein efficiently phosphorylates Cdc2 exclusively on Tyr- 15 in a cyclin-dependent manner.
Coleman, Thomas R. +2 more
core
A foszfoprotein foszfatáz (PPP) enzimcsalád funkciójának vizsgálata Arabidopsis thalianaban = Functional study of the PPP family of phosphoprotein phosphatases in Arabidopsis thaliana [PDF]
A szerin/treonin-specifikus foszfoprotein foszfatázok (PPP-k) minden eukariótában megtalálhatók, szabályozó szerepük azonban növényekben alig ismert. Az Arabidopsis genom 26 PPP katalitikus alegységet kódol, PP1- és PP2A-típusú, újtípusú és ismétlődő ...
Csóka, Balázs +4 more
core
Protein phosphatase 2A (PP2A) is one of the most abundant serine/threonine phosphatases and plays critical roles in regulating cell fate and function.
Kaixiang Zhu +9 more
doaj +1 more source
PP2A activation targets MYCN in neuroblastoma. [PDF]
Nazam N +12 more
europepmc +1 more source
Phosphatase PP2A promotes RTA dephosphorylation to impair KSHV lytic replication. [PDF]
Bai L +12 more
europepmc +1 more source
On the history, synthesis, and medicinal use of cantharidin, LB-100, and their analogs. [PDF]
Scott KA +3 more
europepmc +1 more source
Phosphatase specificity influences phosphorylation timing of CDK substrates during the cell cycle. [PDF]
Zeisner TU +3 more
europepmc +1 more source
Protein phosphatase 2A (PP2A) function in male germ cells and its importance for male fertility. [PDF]
Simon V.
europepmc +1 more source
PP2A Promotes Epithelial-Mesenchymal Transition in Chronic Rhinosinusitis with Nasal Polyps via Wnt/β-Catenin Pathway: A Novel Insight. [PDF]
Chen W +6 more
europepmc +1 more source

