Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling.
By V. Janssens, J. Goris. Biochemical Journal, 2001
1,962 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/8d0db99e8ff80ae32b34e22d2c1a58122e9b5c41
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Citations in the corpus
- Protein phosphatase 1--targeted in many directions. (2002, background): “…for enhancing myosin phosphatase activity precedes the KVxF motif and is located within the first 35 residues, whereas the region involved in suppressing phosphorylase phosphatase activity requires the ankyrin repeats that follow the RVxF motif (Johnson et al., 1996; Tanaka et al., 1998).”
- Loss of human Greatwall results in G2 arrest and multiple mitotic defects due to deregulation of the cyclin B-Cdc2/PP2A balance (2010, background): “PP2A itself is a complicated ternary complex comprised of a catalytic subunit (C), a scaffold subunit (subunit A), and a regulatory B subunit (14).”
- Antagonistic regulation of PIN phosphorylation by PP2A and PINOID directs auxin flux. (2007, background): “In the case of PIN proteins, this mechanism enables switches in the direction of intercellular auxin fluxes, which mediate differential growth, tissue patterning, and organogenesis.”
- Serine/threonine phosphatases: mechanism through structure. (2009, background): “PP2A plays an important role in development, cell proliferation and death, cell mobility, cytoskeleton dynamics, the control of the cell cycle, and the regulation of numerous signaling pathways (Janssens and Goris, 2001); it is also likely to be an important tumor suppressor (Janssens et al.”
- Species- and cell type-specific requirements for cellular transformation. (2004, background): “It has recently been demonstrated that Virus production, infection, and cell lines suppression of PP2A B56 expression could replace ST in trans- Amphotropic retroviruses were produced by transient transfection of 293T formation of HEK cells (Chen et al., 2004), thereby suggesting cells with a retrov”
- CIP2A inhibits PP2A in human malignancies. (2007, positive): “PP2A is a widely conserved protein serine/threonine phosphatase (PSP) that functions as a trimeric protein complex consisting of a catalytic subunit (PP2Ac or C), a scaffold subunit (PR65 or A), and one of the alternative regulatory B subunits (Figure 1A) (Janssens and Goris, 2001).”
- Comparative biology of mouse versus human cells: modelling human cancer in mice (2003, background): “PP2A is responsible for the dephosphorylation of many (and possibly a vast throng of) cellular phosphoproteins that are phosphorylated on serine or threonine residue”
- Phosphatase‐mediated crosstalk between MAPK signaling pathways in the regulation of cell survival (2008, background): “small-t antigen and adenovirus E4orf4 protein (68, 87).”
- NADPH Oxidases in Cardiovascular Health and Disease (2006, neutral): “, hypertension), but the Nox isoform(s) involved remain unclear (162).”