Associated Papers
Identification of serine residues in the connexin43 carboxyl tail important for BCR-mediated spreading of B-lymphocytes.
Pournia F et al.
Journal of Cell Science, 2020
Phosphorylation of connexin 43 at MAPK, PKC or CK1 sites each distinctly alter the kinetics of epidermal wound repair.
Lastwika KJ et al.
Journal of Cell Science, 2019
Adenosine-triphosphate-sensitive K+ channel (Kir6.1): a novel phosphospecific interaction partner of connexin 43 (Cx43).
Ahmad Waza A et al.
Experimental Cell Research, 2012
Phosphorylation of serine residues in the C-terminal cytoplasmic tail of connexin43 regulates proliferation of ovarian granulosa cells.
Dyce PW et al.
The Journal of Membrane Biology, 2012
Connexin43 phosphorylation: structural changes and biological effects.
Solan JL et al.
The Biochemical Journal, 2009
Key connexin 43 phosphorylation events regulate the gap junction life cycle.
Solan JL et al.
The Journal of Membrane Biology, 2007
Regulation of connexin-43-mediated growth inhibition by a phosphorylatable amino-acid is independent of gap junction-forming ability.
Dang X et al.
Molecular and Cellular Biochemistry, 2006
Connexin phosphorylation as a regulatory event linked to gap junction channel assembly.
Solan JL et al.
Biochimica Et Biophysica Acta, 2005
Phosphorylation of serine 262 in the gap junction protein connexin-43 regulates DNA synthesis in cell-cell contact forming cardiomyocytes.
Doble BW et al.
Journal of Cell Science, 2004
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