Results 81 to 90 of about 446,560 (302)

The Molecular Mechanism of Alpha-Synuclein Dependent Regulation of Protein Phosphatase 2A Activity

open access: yesCellular Physiology and Biochemistry, 2018
Background/Aims: Alpha-synuclein (α-Syn) is a neuronal protein that is highly implicated in Parkinson’s disease (PD), and protein phosphatase 2A (PP2A) is an important serine/threonine phosphatase that is associated with neurodegenerative diseases, such ...
Jing Qu   +8 more
doaj   +1 more source

Protein phosphatase 2A inactivation induces microsatellite instability, neoantigen production and immune response

open access: yesNature Communications, 2021
Microsatellite instability (MSI), caused by deficiency of the DNA mismatch repair system, has been associated with improved response to immune checkpoint blockade (ICB).
Yu-Ting Yen   +9 more
doaj   +1 more source

Discovery of Protein Phosphatase 2A Substrates

open access: yesThe FASEB Journal, 2018
The protein ser/thr phosphatases (PSPs) dephosphorylate 1000s of key biological targets, making them attractive therapeutic targets. The serine/threonine protein phosphatases 1 and 2B (PP1; PP2B or calcineurin/CN) bind substrates and regulatory proteins using short functional sequences known as Short Linear Motifs (SLiMs).
Xinru Wang, Rebecca Page, Peti Wolfgang
openaire   +1 more source

PYCR1 inhibition in bone marrow stromal cells enhances bortezomib sensitivity in multiple myeloma cells by altering their metabolism

open access: yesMolecular Oncology, EarlyView.
This study investigated how PYCR1 inhibition in bone marrow stromal cells (BMSCs) indirectly affects multiple myeloma (MM) cell metabolism and viability. Culturing MM cells in conditioned medium from PYCR1‐silenced BMSCs impaired oxidative phosphorylation and increased sensitivity to bortezomib.
Inge Oudaert   +13 more
wiley   +1 more source

NEURONAL FUNCTIONS OF PROTEIN PHOSPHATASE 2A [PDF]

open access: yesAmerican Journal of Neuroscience, 2013
Reversible protein phosphorylation is a common and important form of protein posttranslational modification which determines the proteins’ activities, substrate specificity and inhibitions or degradations, depending on the specific amino acid residue, or combination of residues, being targeted.
openaire   +1 more source

Inhibition of CDK9 enhances AML cell death induced by combined venetoclax and azacitidine

open access: yesMolecular Oncology, EarlyView.
The CDK9 inhibitor AZD4573 downregulates c‐MYC and MCL‐1 to induce death of cytarabine (AraC)‐resistant AML cells. This enhances VEN + AZA‐induced cell death significantly more than any combination of two of the three drugs in AraC‐resistant AML cells.
Shuangshuang Wu   +18 more
wiley   +1 more source

Activation of type II calcium/calmodulin-dependent protein kinase by Ca^(2+)/calmodulin is inhibited by autophosphorylation of threonine within the calmodulin-binding domain [PDF]

open access: yes, 1990
It is now well established that autophosphorylation of a threonine residue located next to each calmodulin-binding domain in the subunits of type II Ca^(2+)/calmodulin-dependent protein kinase causes the kinase to remain active, although at a reduced ...
Kennedy, Mary B.   +2 more
core  

Molecular Control of the Amount, Subcellular Location and Activity State of Translation Elongation Factor 2 (eEF-2) in Neurons Experiencing Stress [PDF]

open access: yes, 2013
Eukaryotic elongation factor 2 (eEF-2) is an important regulator of the protein translation machinery wherein it controls the movement of the ribosome along the mRNA.
Argüelles-Castilla, Sandro   +5 more
core   +1 more source

The serine/threonine protein phosphatase 2A controls autoimmunity [PDF]

open access: yesClinical Immunology, 2018
Protein phosphatase 2A (PP2A) is the first serine/threonine phosphatase recognized to contribute to human and murine lupus immunopathology. PP2A expression in SLE is controlled both epigenetically and genetically, and it is increased in patients with SLE, which contributes to decreased IL-2 production, decreased CD3ζ and increased FcRγ expression on ...
Amir, Sharabi   +2 more
openaire   +2 more sources

A synthetic benzoxazine dimer derivative targets c‐Myc to inhibit colorectal cancer progression

open access: yesMolecular Oncology, EarlyView.
Benzoxazine dimer derivatives bind to the bHLH‐LZ region of c‐Myc, disrupting c‐Myc/MAX complexes, which are evaluated from SAR analysis. This increases ubiquitination and reduces cellular c‐Myc. Impairing DNA repair mechanisms is shown through proteomic analysis.
Nicharat Sriratanasak   +8 more
wiley   +1 more source

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