Results 31 to 40 of about 324,787 (261)

Free Fatty Acids Inhibit Protein Tyrosine Phosphatase 1B and Activate Akt

open access: yesCellular Physiology and Biochemistry, 2013
Background/Aims: Accumulating evidence has suggested that free fatty acids (FFAs) interact with protein kinases and protein phosphatases. The present study examined the effect of FFAs on protein phosphatases and Akt.
Eisuke Shibata   +6 more
doaj   +1 more source

Autoregulation of Protein Phosphatase Type 2A Expression [PDF]

open access: yesJournal of Biological Chemistry, 1998
Protein phosphatases are involved in many cellular processes. One of the most abundant of these enzymes, the serine/threonine-specific protein phosphatase type 2A (PP2A), is present in most eukaryotic cells and serves a variety of functions. However, the detailed study of its regulation and function has been hampered by the difficulty of manipulating ...
Z, Baharians, A H, Schönthal
openaire   +2 more sources

Generation of active protein phosphatase 2A is coupled to holoenzyme assembly. [PDF]

open access: yesPLoS Biology, 2007
Protein phosphatase 2A (PP2A) is a prime example of the multisubunit architecture of protein serine/threonine phosphatases. Until substrate-specific PP2A holoenzymes assemble, a constitutively active, but nonspecific, catalytic C subunit would constitute
Hans Hombauer   +6 more
doaj   +1 more source

Phosphorylation Promotes the Accumulation of PERIOD Protein Foci

open access: yesResearch, 2023
Circadian clock drives the 24-h rhythm in our behavior and physiology. The molecular clock consists of a series of transcriptional/translational feedback loops operated by a number of clock genes.
Mengna Li, Shujing Li, Luoying Zhang
doaj   +1 more source

Defects of protein phosphatase 2A causes corticosteroid insensitivity in severe asthma. [PDF]

open access: yesPLoS ONE, 2011
BACKGROUND: Corticosteroid insensitivity is a major barrier of treatment for some chronic inflammatory diseases, such as severe asthma, but the molecular mechanism of the insensitivity has not been fully elucidated.
Yoshiki Kobayashi   +3 more
doaj   +1 more source

From Basic Science to Clinical Practice: The Role of Cancerous Inhibitor of Protein Phosphatase 2A (CIP2A)/p90 in Cancer

open access: yesFrontiers in Genetics, 2023
Cancerous inhibitor of protein phosphatase 2A (CIP2A), initially reported as a tumor-associated antigen (known as p90), is highly expressed in most solid and hematological tumors. The interaction of CIP2A/p90, protein phosphatase 2A (PP2A), and c-Myc can
Beibei Chen   +5 more
doaj   +1 more source

A crosstalk between phosphorylation and ubiquitination of BNIP3 regulates mitophagy under hypoxia

open access: yesAutophagy Reports, 2023
BNIP3 (BCL2/adenovirus e1B 19 kDa protein interacting protein 3) is a mitochondrial outer membrane protein that is sensitive to hypoxia and mediates mitophagy, a process important for mitochondrial quality control and to maintain energetic and redox ...
Yun-Ling He   +4 more
doaj   +1 more source

Therapeutic reactivation of protein phosphatase 2A in acute myeloid leukemia

open access: yesFrontiers in Oncology, 2015
Protein phosphatase 2A (PP2A) is a serine/threonine phosphatase that is required for normal cell growth and development. PP2A is a potent tumor suppressor, which is inactivated in cancer cells as a result of genetic deletions and mutations.
Kavitha eRamaswamy   +2 more
doaj   +1 more source

The protein phosphatase 2A holoenzyme is a key regulator of starch metabolism and bradyzoite differentiation in Toxoplasma gondii

open access: yesNature Communications, 2022
Protein phosphorylation and dephosphorylation are essential aspects of biology. Wang et al., report that Toxoplasma gondiiprotein phosphatase 2A (PP2A) mediated dephosphorylation is critical for starch metabolism and bradyzoite differentiation.
Jin-Lei Wang   +7 more
doaj   +1 more source

Protein phosphatase 2A holoenzymes regulate leucine-rich repeat kinase 2 phosphorylation and accumulation

open access: yesNeurobiology of Disease, 2021
LRRK2 is a highly phosphorylated multidomain protein and mutations in the gene encoding LRRK2 are a major genetic determinant of Parkinson's disease (PD).
Matthieu Drouyer   +19 more
doaj   +1 more source

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