Results 201 to 210 of about 618,514 (262)
Defining the Protein Phosphatase 2A (PP2A) Subcomplexes That Regulate FoxO Transcription Factor Localization. [PDF]
CellsLuperchio AM, Salamango DJ.
europepmc +1 more source
Protein phosphatase PP2Cα S-glutathionylation regulates cell migration. [PDF]
J Biol ChemKukulage DSK +9 more
europepmc +1 more source
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Frontiers in Bioscience, 2002
The molecular mechanisms of signal transduction have been at the focus of increasingly intense scientific research. As a result, our understanding of protein tyrosine kinase-mediated signaling has advanced at an unprecedented pace during the past decade.
T, Mustelin +7 more
openaire +2 more sources
The molecular mechanisms of signal transduction have been at the focus of increasingly intense scientific research. As a result, our understanding of protein tyrosine kinase-mediated signaling has advanced at an unprecedented pace during the past decade.
T, Mustelin +7 more
openaire +2 more sources
Annual Review of Biochemistry, 1993
The process of reversible phosphorylation is perhaps the cell's most prevalent means of regulation at the molecular level. It has been estimated that up to 30% of all cellular proteins are phosphorylated, and phosphorylation has been shown to play a crucial regulatory role in such diverse cellular events as metabolism, growth and differentiation ...
K M, Walton, J E, Dixon
openaire +2 more sources
The process of reversible phosphorylation is perhaps the cell's most prevalent means of regulation at the molecular level. It has been estimated that up to 30% of all cellular proteins are phosphorylated, and phosphorylation has been shown to play a crucial regulatory role in such diverse cellular events as metabolism, growth and differentiation ...
K M, Walton, J E, Dixon
openaire +2 more sources
Annual Review of Plant Physiology and Plant Molecular Biology, 1996
▪ Abstract Posttranslational modification of proteins by phosphorylation is a universal mechanism for regulating diverse biological functions. Recognition that many cellular proteins are reversibly phosphorylated in response to external stimuli or intracellular signals has generated an ongoing interest in identifying and characterizing plant protein ...
Robert D., Smith, John C., Walker
openaire +2 more sources
▪ Abstract Posttranslational modification of proteins by phosphorylation is a universal mechanism for regulating diverse biological functions. Recognition that many cellular proteins are reversibly phosphorylated in response to external stimuli or intracellular signals has generated an ongoing interest in identifying and characterizing plant protein ...
Robert D., Smith, John C., Walker
openaire +2 more sources
Annual Review of Cell Biology, 1992
phosphatases, tyrosine phosphorylation, signal transduction, dephosphorylatio n.
H, Charbonneau, N K, Tonks
openaire +2 more sources
phosphatases, tyrosine phosphorylation, signal transduction, dephosphorylatio n.
H, Charbonneau, N K, Tonks
openaire +2 more sources
Current Opinion in Structural Biology, 1995
Protein phosphatases are signal transducing enzymes that dephosphorylate cellular phosphoproteins. The recently determined crystal structures of protein tyrosine and serine/threonine phosphatases reveal that these proteins adopt distinct structures and catalyze dephosphorylation reactions by means of different enzymatic mechanisms.
openaire +2 more sources
Protein phosphatases are signal transducing enzymes that dephosphorylate cellular phosphoproteins. The recently determined crystal structures of protein tyrosine and serine/threonine phosphatases reveal that these proteins adopt distinct structures and catalyze dephosphorylation reactions by means of different enzymatic mechanisms.
openaire +2 more sources
International Journal of Oncology, 1997
Protein tyrosine phosphatases (PTPases) balance the action of tyrosine kinases to maintain a set level of cellular tyrosine phosphorylation. Increases in tyrosine phosphorylation produced by transformation with constitutively active tyrosine kinases can initiate cellular proliferation. PTPases may act as tumor suppressors to counteract the transforming
B, Goldsmith, S, Koizumi
openaire +2 more sources
Protein tyrosine phosphatases (PTPases) balance the action of tyrosine kinases to maintain a set level of cellular tyrosine phosphorylation. Increases in tyrosine phosphorylation produced by transformation with constitutively active tyrosine kinases can initiate cellular proliferation. PTPases may act as tumor suppressors to counteract the transforming
B, Goldsmith, S, Koizumi
openaire +2 more sources