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Protein dephosphorylation

Known as: Dephosphorylation, protein amino acid dephosphorylation 
The covalent chemical or post-translational biochemical removal of a phosphate group(s) from a peptide or protein, by phosphatases. (NCI)
National Institutes of Health

Papers overview

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Highly Cited
2008
Highly Cited
2008
Changes in mitochondrial morphology that occur during cell cycle, differentiation, and death are tightly regulated by the balance… Expand
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Highly Cited
2005
Highly Cited
2005
Most protein phosphatases have little intrinsic substrate specificity, making selective pharmacological inhibition of specific… Expand
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Review
2005
Review
2005
  • Robert Roskoski
  • Biochemical and biophysical research…
  • 2005
  • Corpus ID: 9275112
Src and Src-family protein-tyrosine kinases are regulatory proteins that play key roles in cell differentiation, motility… Expand
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Highly Cited
2001
Highly Cited
2001
Phosphorylation of the α subunit of eukaryotic translation initiation factor 2 (eIF2α) on serine 51 integrates general… Expand
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Highly Cited
2000
Highly Cited
2000
The reversible protein phosphorylation on serine or threonine residues that precede proline (pSer/Thr-Pro) is a key signaling… Expand
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Highly Cited
1999
Highly Cited
1999
The Ca2+-activated protein phosphatase calcineurin induces apoptosis, but the mechanism is unknown. Calcineurin was found to… Expand
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Highly Cited
1999
Highly Cited
1999
Interactions between receptor tyrosine kinases of the Eph family and their ligands, ephrins, are implicated in establishment of… Expand
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Highly Cited
1998
Highly Cited
1998
Phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) is a key molecule involved in cell growth signaling. We demonstrated… Expand
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Highly Cited
1998
Highly Cited
1998
Brief bath application of N-methyl-D-aspartate (NMDA) to hippocampal slices produces long-term synaptic depression (LTD) in CA1… Expand
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Highly Cited
1995
Highly Cited
1995
Human protein phosphatase-2C alpha (PP2C alpha) was purified to homogeneity after expression in Escherichia coli. AMP inhibited… Expand
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