Results 21 to 30 of about 10,021 (178)

Regulation of PP2A, PP4, and PP6 holoenzyme assembly by carboxyl-terminal methylation

open access: yesScientific Reports, 2021
The family of Phosphoprotein Phosphatases (PPPs) is responsible for most cellular serine and threonine dephosphorylation. PPPs achieve substrate specificity and selectivity by forming multimeric holoenzymes. PPP holoenzyme assembly is tightly controlled,
Scott P. Lyons   +4 more
doaj   +1 more source

Phosphatase Protection Assay: 14-3-3 Binding Protects the Phosphate group of RSG from λ Protein Phosphatase

open access: yesBio-Protocol, 2015
14-3-3 proteins regulate diverse cellular processes in eukaryotes by binding to phospho-serine or threonine of target proteins. One of the physiological functions of 14-3-3 is to bind and protect phosphate groups of the target proteins against ...
Takeshi Ito, Yohsuke Takahashi
doaj   +1 more source

Quantum-based modeling implies that bidentate Arg89-substrate binding enhances serine/threonine protein phosphatase-2A(PPP2R5D/PPP2R1A/PPP2CA)-mediated dephosphorylation

open access: yesFrontiers in Cell and Developmental Biology, 2023
PP2A-serine/threonine protein phosphatases function as heterotrimeric holoenzymes, composed of a common scaffold (A-subunit encoded by PPP2R1A/PPP2R1B), a common catalytic (C-subunit encoded by PPP2CA/PPP2CB), and one of many variable regulatory (B ...
E. Alan Salter   +3 more
doaj   +1 more source

Cytokine-stimulated Phosphoflow of PBMC Using CyTOF Mass Cytometry

open access: yesBio-Protocol, 2015
Phosphorylation of tyrosine, serine, and threonine residues is critical for the control of protein activity involved in various cellular events. An assortment of kinases and phosphatases regulate intracellular protein phosphorylation in many different ...
Rosemary Fernandez, Holden Maecker
doaj   +1 more source

Calcineurin regulates homologous desensitization of natriuretic peptide receptor-A and inhibits ANP-induced testosterone production in MA-10 cells. [PDF]

open access: yesPLoS ONE, 2012
Receptor desensitization is a ubiquitous regulatory mechanism that defines the activatable pool of receptors, and thus, the ability of cells to respond to environmental stimuli. In recent years, the molecular mechanisms controlling the desensitization of
Michelle B Henesy   +7 more
doaj   +1 more source

Cyclic AMP-sensitive activation of hepatic sterol synthesis and 3-hydroxy-3-methylglutaryl coenzyme A reductase.

open access: yesJournal of Lipid Research, 1978
We previously showed that preincubation of a 10,000 g supernatant (S(10)) from rat liver for 20 min at 37 degrees C dramatically increased the subsequent incorporation of [(14)C]acetate into sterols.
C D Goodwin, S Margolis
doaj   +1 more source

Phosphoprotein Phosphatase Activity in the Thyroid

open access: yesExperimental Biology and Medicine, 1975
Phosphoprotein phosphatase activity in the calf thyroid was found in various subcellular fractions. The relative amount in each fraction varied according to the substrate used: The 500g fraction had the highest specific activity when protamine was used, while the 5000g fraction was highest when histone was used. Triton X-100 tended to increase activity
S W, Spaulding, G N, Burrow
openaire   +2 more sources

Special Sensitization Pattern in Adenosine-Induced Myocardial Responses After Thyroxine-Treatment

open access: yesJournal of Pharmacological Sciences, 2003
Chronic thyroxine treatment reduces the susceptibility of atrial myocardium to adenosine. While the possible role of membrane adenosine receptors in this action is supported by several studies, the involvement of intracellular adenosine mechanisms has ...
Rudolf Gesztelyi   +5 more
doaj   +1 more source

Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation

open access: yesFEBS Letters, EarlyView.
Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe   +3 more
wiley   +1 more source

LRRK2 Kinase Activity and Biology are Not Uniformly Predicted by its Autophosphorylation and Cellular Phosphorylation Site Status

open access: yesFrontiers in Molecular Neuroscience, 2014
Missense mutations in the Leucine Rich Repeat protein Kinase 2 (LRRK2) gene are the most common genetic predisposition to develop Parkinson’s disease (PD) LRRK2 is a large multi-domain phosphoprotein with a GTPase domain and a serine/threonine protein ...
April eReynolds   +4 more
doaj   +1 more source

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