phosphoserine and pd 184352

phosphoserine has been researched along with pd 184352 in 2 studies

Research

Studies (2)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's2 (100.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Centeno, F; Cuenda, A; Feijoo, C; Garner, C; Goedert, M; Hasegawa, M; Kuhlendahl, S; Leal-Ortiz, S; Reuver, S; Sabio, G; Thomas, GM1
Alfonso, M; Campbell, DG; Cohen, P; Mora, A; Murray, JT; Peggie, M1

Other Studies

2 other study(ies) available for phosphoserine and pd 184352

ArticleYear
Stress- and mitogen-induced phosphorylation of the synapse-associated protein SAP90/PSD-95 by activation of SAPK3/p38gamma and ERK1/ERK2.
    The Biochemical journal, 2004, May-15, Volume: 380, Issue:Pt 1

    Topics: Amino Acid Sequence; Animals; Benzamides; Cell Line; Enzyme Activation; Enzyme Inhibitors; Humans; Imidazoles; MAP Kinase Signaling System; Mice; Microscopy, Fluorescence; Mitogen-Activated Protein Kinase 1; Mitogen-Activated Protein Kinase 3; Mitogen-Activated Protein Kinases; Mitogens; Molecular Sequence Data; Nerve Tissue Proteins; Neurons; Osmotic Pressure; p38 Mitogen-Activated Protein Kinases; PC12 Cells; Phosphorylation; Phosphoserine; Phosphothreonine; Protein Interaction Mapping; Protein Processing, Post-Translational; Protein Structure, Tertiary; Pyridines; Rats; Rats, Sprague-Dawley; Recombinant Fusion Proteins; SAP90-PSD95 Associated Proteins; Stress, Physiological; Ultraviolet Rays

2004
Identification of filamin C as a new physiological substrate of PKBalpha using KESTREL.
    The Biochemical journal, 2004, Dec-15, Volume: 384, Issue:Pt 3

    Topics: 3-Phosphoinositide-Dependent Protein Kinases; Amino Acid Sequence; Androstadienes; Animals; Antibody Specificity; Benzamides; Cell Extracts; Cell Line; Contractile Proteins; Epidermal Growth Factor; Filamins; Humans; Immediate-Early Proteins; Insulin; Isoenzymes; Mice; Microfilament Proteins; Molecular Sequence Data; Molecular Weight; Muscle, Skeletal; Myoblasts; Myocardium; Nuclear Proteins; Phosphatidylinositol 3-Kinases; Phosphoinositide-3 Kinase Inhibitors; Phosphorylation; Phosphoserine; Protein Serine-Threonine Kinases; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-akt; Rabbits; Signal Transduction; Sirolimus; Substrate Specificity; Wortmannin

2004