Results 51 to 60 of about 35,429 (234)

Activation of the Tumor Suppressor PP2A Emerges as a Potential Therapeutic Strategy for Treating Prostate Cancer

open access: yesMarine Drugs, 2015
Protein phosphatase 2A (PP2A) is a tumor suppressor complex that has recently been reported as a novel and highly relevant molecular target in prostate cancer (PCa). However, its potential therapeutic value remains to be fully clarified.
Ion Cristóbal   +8 more
doaj   +1 more source

PP2A-B55 Holoenzyme Regulation and Cancer

open access: yes, 2020
Protein phosphorylation is a post-translational modification essential for the control of the activity of most enzymes in the cell. This protein modification results from a fine-tuned balance between kinases and phosphatases.
Priya Amin   +17 more
core   +1 more source

Upregulated SET Promotes Cell Survival Through Activating Akt/NF-κB Signal in Colorectal Carcinoma

open access: yesCancer Management and Research, 2020
Jianjun Zhu,1 Lihong Shi,2 Genlai Du,1 Li Li,1 Ming Liu1 1Department of Medical Cellular Biology and Genetics, Shanxi Medical University, Taiyuan 030001, People’s Republic of China; 2Department of Human Anatomy, School of Basic Medicine, Shanxi ...
Zhu J, Shi L, Du G, Li L, Liu M
doaj  

Protein phosphatase 2A dysfunction in Alzheimer’s disease

open access: yesFrontiers in Molecular Neuroscience, 2014
Protein Phosphatase 2A (PP2A) is a large family of enzymes that account for the majority of brain Ser/Thr phosphatase activity. While PP2A enzymes collectively modulate most cellular processes, sophisticated regulatory mechanisms are ultimately ...
Jean-Marie eSontag, Estelle eSontag
doaj   +1 more source

Protein phosphatase 2A restrains DLK signaling to promote proper Drosophila synaptic development and mammalian cortical neuron survival

open access: yesNeurobiology of Disease, 2022
Protein phosphatase 2A (PP2A) is a major cellular phosphatase with many protein substrates. As expected for a signaling molecule with many targets, inhibition of PP2A disrupts fundamental aspects of cellular physiology including cell division and ...
Margaret Hayne, Aaron DiAntonio
doaj   +1 more source

Pleiotropy of PP2A Phosphatases in Cancer with a Focus on Glioblastoma IDH Wildtype [PDF]

open access: yes, 2022
Serine/Threonine protein phosphatase 2A (PP2A) is a heterotrimeric (or occasionally, heterodimeric) phosphatase with pleiotropic functions and ubiquitous expression.
Kashani, Elham   +3 more
core   +2 more sources

Protein phosphatase 2A regulation of GABAB receptors normalizes ischemia-induced aberrant receptor trafficking and provides neuroprotection

open access: yesFrontiers in Molecular Neuroscience, 2022
One major factor regulating the strength of GABAB receptor signaling and thereby neuronal excitability is the dynamic control of their cell surface expression.
Mohammad Hleihil   +5 more
doaj   +1 more source

Protein phosphatase 2A modulates podocyte maturation and glomerular functional integrity in mice

open access: yesCell Communication and Signaling, 2019
Background Protein phosphorylation & dephosphorylation are ubiquitous cellular processes that allow for the nuanced and reversible regulation of protein activity.
Xiujuan Zhu   +7 more
doaj   +1 more source

RT–PCR to detect the mRNA levels for the regulatory subunits of PP2A-Aα, PP2A-Aβ, PP2A-Bα, PP2A-Bβ, and PP2A-Bγ in the retina, lens epithelium, lens fiber, and cornea of the mouse eye

open access: yes, 2011
RT–PCR was conducted as described in . The primers used in the present studies are described in . The primers for each PP-2A regulatory subunit and for β-actin were added to the reactions at the same time.
David Wan-Cheng Li (90955)   +7 more
core   +1 more source

Selective Modulation of OTUB1 Noncanonical Function via a bioPhosTAC Strategy

open access: yesAdvanced Science, EarlyView.
This work positions the versatile performance of the peptide‐based bioPhosTAC platform for dissecting phosphorylation‐dependent biology and expanding the scope of induced‐proximity technologies. We demonstrated that selective manipulation of a tyrosine phosphorylation site is sufficient to propagate coordinated cellular consequences.
Seung Un Seo   +7 more
wiley   +1 more source

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