Results 21 to 30 of about 18,289 (229)
The cell surface receptor Tartan is a potential in vivo substrate for the receptor tyrosine phosphatase Ptp52F [PDF]
, 2009 Receptor-linked protein-tyrosine phosphatases (RPTPs) are essential regulators of axon guidance and synaptogenesis in Drosophila, but the signaling pathways in which they function are poorly defined.
Bugga, Lakshmi +2 more
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Use of intein-mediated phosphoprotein arrays to study substrate specificity of protein phosphatases
BioTechniques, 2007 Synthetic peptides incorporating various chemical moieties, for example, phosphate groups, are convenient tools for investigating protein modification enzymes, such as protein phosphatases (PPs). However, short peptides are sometimes poor substrates, and
Samvel Kochinyan +5 more
doaj +1 more source
Toxins, 2011 Cyclin D1 is a key regulator of the cell cycle that is over expressed in more than half of breast cancer patients. The levels of cyclin D1 are controlled primarily through post-translational mechanisms and phosphorylation of cyclin D1 at T286 induces its
David L. Brautigan, Jessica R. Edelson
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Regulation of PP2A, PP4, and PP6 holoenzyme assembly by carboxyl-terminal methylation
Scientific 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
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Protein phosphatase 5 regulates titin phosphorylation and function at a sarcomere-associated mechanosensor complex in cardiomyocytes. [PDF]
, 2018 Serine/threonine protein phosphatase 5 (PP5) is ubiquitously expressed in eukaryotic cells; however, its function in cardiomyocytes is unknown. Under basal conditions, PP5 is autoinhibited, but enzymatic activity rises upon binding of specific factors ...
Beckendorf, Lisa +10 more
core +3 more sources
Bio-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
Endogenous inhibitor proteins that connect Ser/Thr kinases and phosphatases in cell signaling. [PDF]
, 2012 Protein phosphatase activity acts as a primary determinant of the extent and duration of phosphorylation of cellular proteins in response to physiological stimuli. Ser/Thr protein phosphatase-1 (PP1) belongs to the PPP superfamily, and is associated with
Brautigan, David L, Eto, Masumi
core +2 more sources
Frontiers 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
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Large-scale phosphoproteome analysis in seedling leaves of Brachypodium distachyon L. [PDF]
, 2014 BACKGROUND: Protein phosphorylation is one of the most important post-translational modifications involved in the regulation of plant growth and development as well as diverse stress response. As a member of the Poaceae, Brachypodium distachyon L.
Ai-Qin Gu +7 more
core +1 more source
Cytokine-stimulated Phosphoflow of PBMC Using CyTOF Mass Cytometry
Bio-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