Results 21 to 30 of about 19,090 (263)

Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments [PDF]

open access: yes, 2018
Reversible phosphorylation is a key mechanism that regulates many cellular processes in prokaryotes and eukaryotes. In prokaryotes, signal transduction includes two-component signaling systems, which involve a membrane sensor histidine kinase and a ...
Janczarek, Monika   +3 more
core   +1 more source

The Scaffold Immunophilin FKBP51 Is a Phosphoprotein That Undergoes Dynamic Mitochondrial-Nuclear Shuttling

open access: yesCells, 2022
The immunophilin FKBP51 forms heterocomplexes with molecular chaperones, protein-kinases, protein-phosphatases, autophagy-related factors, and transcription factors.
Nadia R. Zgajnar   +3 more
doaj   +1 more source

Global analysis of serine/threonine and tyrosine protein phosphatase catalytic subunit genes in Neurospora crassa reveals interplay between phosphatases and the p38 mitogen-activated protein kinase. [PDF]

open access: yes, 2013
Protein phosphatases are integral components of the cellular signaling machinery in eukaryotes, regulating diverse aspects of growth and development. The genome of the filamentous fungus and model organism Neurospora crassa encodes catalytic subunits for
Borkovich, Katherine A   +3 more
core   +2 more sources

Phosphoprotein Phosphatase 1 but Not 2A Activity Modulates Coupled-Clock Mechanisms to Impact on Intrinsic Automaticity of Sinoatrial Nodal Pacemaker Cells

open access: yesCells, 2021
Spontaneous AP (action potential) firing of sinoatrial nodal cells (SANC) is critically dependent on protein kinase A (PKA) and Ca2+/calmodulin-dependent protein kinase II (CaMKII)-dependent protein phosphorylation, which are required for the generation ...
Syevda Tagirova Sirenko   +13 more
doaj   +1 more source

The cell surface receptor Tartan is a potential in vivo substrate for the receptor tyrosine phosphatase Ptp52F [PDF]

open access: yes, 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
core   +2 more sources

Development of a novel pharmacophore model to screen specific inhibitors for the serine-threonine protein phosphatase calcineurin

open access: yesBiochemistry and Biophysics Reports, 2022
Calcineurin (CaN) is a calcium/calmodulin-dependent serine/threonine phosphatase with a crucial role in cellular homeostasis. It is also the target of the Food and Drug Administration (FDA) approved immunosuppressant drugs FK506 and cyclosporine A ...
Abhisek Mukherjee   +3 more
doaj   +1 more source

Endogenous inhibitor proteins that connect Ser/Thr kinases and phosphatases in cell signaling. [PDF]

open access: yes, 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

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

Use of intein-mediated phosphoprotein arrays to study substrate specificity of protein phosphatases

open access: yesBioTechniques, 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

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

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