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index medicus (568) 568
3-phosphoinositide-dependent protein kinases (434) 434
protein-serine-threonine kinases - metabolism (369) 369
animals (346) 346
humans (340) 340
biochemistry & molecular biology (332) 332
phosphorylation (325) 325
mice (188) 188
cell biology (173) 173
signal transduction (170) 170
activation (162) 162
protein-serine-threonine kinases - genetics (133) 133
pdk1 (123) 123
enzyme activation (118) 118
proto-oncogene proteins c-akt (115) 115
phosphatidylinositol 3-kinases - metabolism (112) 112
amino acid sequence (107) 107
cell line (106) 106
proto-oncogene proteins - metabolism (101) 101
molecular sequence data (96) 96
proto-oncogene proteins c-akt - metabolism (91) 91
protein-serine-threonine kinases - antagonists & inhibitors (86) 86
akt (83) 83
3-phosphoinositide-dependent protein kinase-1 (81) 81
in-vivo (76) 76
protein-serine-threonine kinases - chemistry (76) 76
protein binding (74) 74
phosphatidylinositol 3-kinase (72) 72
apoptosis (70) 70
binding sites (69) 69
male (67) 67
protein kinases (67) 67
insulin (65) 65
rats (65) 65
mutation (64) 64
protein kinase c - metabolism (64) 64
cell line, tumor (62) 62
cells, cultured (61) 61
pathway (61) 61
cancer (60) 60
protein structure, tertiary (60) 60
proteins (60) 60
signal transduction - drug effects (59) 59
protein-kinase (56) 56
kinases (55) 55
cells (53) 53
animal structures (52) 52
protein kinase inhibitors - pharmacology (52) 52
3-phosphoinositide-dependent protein kinases - metabolism (51) 51
enzyme inhibitors - pharmacology (51) 51
protein kinases - metabolism (51) 51
biophysics (50) 50
protein-serine-threonine kinases - physiology (50) 50
signal-transduction (49) 49
phosphoinositide 3-kinase (48) 48
article (47) 47
phosphorylation - drug effects (47) 47
female (46) 46
research (46) 46
transfection (46) 46
identification (45) 45
research article (44) 44
biochemistry (41) 41
enzyme activation - drug effects (41) 41
insulin - pharmacology (40) 40
oncology (40) 40
protein-kinase-b (40) 40
crystal-structure (38) 38
insulin - metabolism (38) 38
models, biological (38) 38
models, molecular (38) 38
ribosomal protein s6 kinases - metabolism (38) 38
signal transduction - physiology (37) 37
isoenzymes - metabolism (36) 36
domain (35) 35
growth (35) 35
phosphatidylinositol 3-kinases - antagonists & inhibitors (35) 35
pleckstrin homology domain (35) 35
serine - metabolism (35) 35
chemistry, medicinal (33) 33
expression (33) 33
recombinant proteins - metabolism (33) 33
structure-activity relationship (33) 33
tyrosine phosphorylation (32) 32
biology (31) 31
glycogen-synthase kinase-3 (31) 31
physiological aspects (31) 31
protein kinase b (31) 31
recombinant fusion proteins - metabolism (31) 31
time factors (31) 31
cos cells (30) 30
inhibition (30) 30
blotting, western (28) 28
docking site (28) 28
phosphatidylinositol phosphates - metabolism (28) 28
sequence homology, amino acid (28) 28
signaling pathway (28) 28
substrate specificity (28) 28
binding (27) 27
catalytic domain (27) 27
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Current Biology, ISSN 0960-9822, 04/2000, Volume 10, Issue 8, pp. 439 - 448
Background: Protein kinase B (PKB), and the p70 and p90 ribosomal S6 kinases (p70 S6 kinase and p90 Rsk, respectively), are activated by phosphorylation of two... 
INSULIN | MECHANISM | PHOSPHORYLATION | PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | P70(S6K) | BIOLOGY | RIBOSOMAL S6 KINASE | C-ZETA | PHOSPHOINOSITIDE 3-KINASE | HOMOLOGY | PDK1 | Insulin-Like Growth Factor I - pharmacology | Tetradecanoylphorbol Acetate - pharmacology | Ribosomal Protein S6 Kinases - metabolism | Multienzyme Complexes - metabolism | Glycogen Synthase Kinase 3 | Immunoblotting | Proto-Oncogene Proteins - chemistry | AMP-Activated Protein Kinases | Stem Cells - enzymology | Gene Deletion | Calcium-Calmodulin-Dependent Protein Kinases - pharmacology | 3-Phosphoinositide-Dependent Protein Kinases | Protein-Serine-Threonine Kinases - metabolism | Cyclic AMP-Dependent Protein Kinases - metabolism | Proto-Oncogene Proteins - metabolism | Protein-Serine-Threonine Kinases - physiology | Cells, Cultured | Protein-Serine-Threonine Kinases - genetics | Enzyme Activation - drug effects | Enzyme Activation - radiation effects | Proto-Oncogene Proteins c-akt | Calcium-Calmodulin-Dependent Protein Kinases - chemistry | Animals | Mice | Protein-Serine-Threonine Kinases - pharmacology | Calcium-Calmodulin-Dependent Protein Kinases - metabolism | Ribosomal Protein S6 Kinases, 90-kDa | 3-phosphoinositide-dependent protein kinase 1 | ribosomal S6 kinase | Protein kinase B | MSK1 protein | AMP-activated protein kinase | AGC kinase | Index Medicus
Journal Article
BBA - Biomembranes, ISSN 0005-2736, 11/2016, Volume 1858, Issue 11, pp. 2709 - 2716
Phosphatidic acid (PA) is a crucial membrane phospholipid involved in de novo lipid synthesis and numerous intracellular signaling cascades. The signaling... 
PA target proteins | Epsin-like clathrin adaptor (ECA) | Membrane curvature stress | Type I and type II lipids | PA-binding | Phosphatidic acid | Liposome binding assays | TARGET | DIACYLGLYCEROL | PHOSPHOLIPASE-D | LIPID POLYMORPHISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | KINASE | BIOPHYSICS | LYSOPHOSPHATIDIC ACID | ARABIDOPSIS | IONIZATION | HYDROGEN BOND SWITCH | MODULATION | Qb-SNARE Proteins - chemistry | 3-Phosphoinositide-Dependent Protein Kinases - chemistry | Humans | Qb-SNARE Proteins - metabolism | Adaptor Proteins, Vesicular Transport - metabolism | Recombinant Fusion Proteins - metabolism | Arabidopsis Proteins - metabolism | Cell Membrane - chemistry | Qc-SNARE Proteins - metabolism | Proto-Oncogene Proteins c-raf - chemistry | Biological Assay | Carrier Proteins - chemistry | Adaptor Proteins, Vesicular Transport - chemistry | Cell Membrane - metabolism | Cell Membrane - drug effects | Repressor Proteins - metabolism | Lysophosphatidylcholines - pharmacology | Repressor Proteins - chemistry | Arabidopsis - chemistry | 3-Phosphoinositide-Dependent Protein Kinases - metabolism | Recombinant Fusion Proteins - chemistry | Proto-Oncogene Proteins c-raf - metabolism | Saccharomyces cerevisiae - chemistry | Liposomes - chemistry | Carrier Proteins - metabolism | Arabidopsis Proteins - chemistry | Phosphatidic Acids - chemistry | Qc-SNARE Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Liposomes - metabolism | Phosphatidic Acids - metabolism | Phosphatidylethanolamines - metabolism | Phosphatidylethanolamines - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Arabidopsis thaliana | Chemical properties | Binding proteins | Membrane proteins | Protein binding | Plant physiology | Analysis | Phospholipids
Journal Article
The EMBO Journal, ISSN 0261-4189, 10/2002, Volume 21, Issue 20, pp. 5396 - 5407
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2014, Volume 111, Issue 52, pp. 18590 - 18595
There is great interest in developing selective protein kinase inhibitors by targeting allosteric sites, but these sites often involve protein-protein or... 
Proteins | Molecules | Phosphorylation | Prodrugs | Sulfonamides | Allosteric site | Competitive binding | Ligands | Chemicals | Crystal structure | Peptide mimicry | Allostery | Drug discovery | Protein-protein interaction | SITE | ACTIVATION | FLUORESCENCE POLARIZATION | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | PIF-POCKET | CATALYTIC DOMAIN | MECHANISMS | IDENTIFICATION | DISCOVERY | drug discovery | PRODRUGS | peptide mimicry | protein-protein interaction | allostery | 3-Phosphoinositide-Dependent Protein Kinases - chemistry | Humans | Crystallography, X-Ray | Neoplasm Proteins - antagonists & inhibitors | Neoplasm Proteins - metabolism | Protein Kinase Inhibitors - chemistry | Neoplasms - genetics | HEK293 Cells | Antineoplastic Agents - pharmacology | Neoplasm Proteins - genetics | Allosteric Regulation - drug effects | Peptides - chemistry | Protein Structure, Secondary | 3-Phosphoinositide-Dependent Protein Kinases - genetics | Neoplasms - enzymology | Neoplasm Proteins - chemistry | 3-Phosphoinositide-Dependent Protein Kinases - antagonists & inhibitors | 3-Phosphoinositide-Dependent Protein Kinases - metabolism | Antineoplastic Agents - chemistry | Amino Acid Motifs | Neoplasms - drug therapy | Peptides - pharmacology | Allosteric Site | Molecular Docking Simulation | Protein Kinase Inhibitors - pharmacology | Neoplasms - pathology | Physiological aspects | Protein research | Research | Peptides | Protein kinases | Protein-protein interactions | Mutation | Kinases | Molecular weight | Index Medicus | protein–protein interaction | Biological Sciences
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 06/2011, Volume 286, Issue 25, pp. 22017 - 22027
Pkh1, -2, and -3 are the yeast orthologs of mammalian 3-phosphoinositide- dependent protein kinase-1 (PDK1). Although essential for viability, their... 
AGC KINASES | CATALYTIC SUBUNIT | PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | BINDING POCKET | SACCHAROMYCES-CEREVISIAE | ADENYLATE-CYCLASE | RAS PROTEINS | DOCKING SITE | Protein-Serine-Threonine Kinases - deficiency | Sequence Deletion | Phosphorylation | Cyclic AMP-Dependent Protein Kinases - chemistry | Saccharomyces cerevisiae - drug effects | Saccharomyces cerevisiae Proteins - biosynthesis | Saccharomyces cerevisiae - metabolism | Nitrogen - pharmacology | 3-Phosphoinositide-Dependent Protein Kinases | Protein-Serine-Threonine Kinases - metabolism | Catalytic Domain | Proto-Oncogene Proteins c-akt - chemistry | Protein-Serine-Threonine Kinases - genetics | Cell Size | Saccharomyces cerevisiae Proteins - genetics | Protein-Serine-Threonine Kinases - biosynthesis | Saccharomyces cerevisiae - cytology | Sequence Homology, Amino Acid | Animals | Mutagenesis | Saccharomyces cerevisiae Proteins - metabolism | Hydrophobic and Hydrophilic Interactions | Protein Binding | Saccharomyces cerevisiae - enzymology | Protein-Serine-Threonine Kinases - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Index Medicus | Site-directed Mutagenesis | Protein Kinase A (PKA) | Yeast | Signal Transduction | Protein Kinases | PKB | Sch9 | Protein Phosphorylation | Saccharomyces cerevisiae | PDK1 | Pkh1–3
Journal Article
Journal Article
FEBS Letters, ISSN 0014-5793, 09/2012, Volume 586, Issue 19, pp. 3471 - 3476
► TPCK inhibits all tested AGC kinases with phenylalanine-directed, cysteine-containing activation loops, including RSK1, Akt1, S6K1, MSK1 and MSK2. ► Mass... 
Signal transduction | Reversible phosphorylation | Mass spectrometry | Kinase inhibitor | TPCK | MSK | mitogen and stress-activated protein kinase | phosphatidylinositol-3 kinase | related to protein kinase A, protein kinase G and protein kinase C | PKA | S6 kinase | S6K | RSK | N-alpha-tosyl | PI3K | ribosomal S6 kinase | 3-phosphoinositide dependent protein kinase-1 | protein kinase A | phenylalanyl chloromethyl ketone | AGC | PDK1 | ERK | extracellular signal regulated kinase | SIGNAL | PROTEIN KINASE-1 | PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | IDENTIFICATION | CANCER | CELL BIOLOGY | BIOPHYSICS | PATHWAY | RESISTANCE | MURINE BRAIN | S6 KINASE | Amino Acid Sequence | Protein Kinases - genetics | Mutagenesis, Site-Directed | Proto-Oncogene Proteins c-akt - chemistry | Humans | Molecular Sequence Data | Protein Kinases - chemistry | DNA Primers - genetics | Cysteine - chemistry | Ribosomal Protein S6 Kinases, 90-kDa - chemistry | Proto-Oncogene Proteins c-akt - genetics | Amino Acid Motifs | Sequence Homology, Amino Acid | Phenylalanine - chemistry | Base Sequence | Ribosomal Protein S6 Kinases, 90-kDa - genetics | HEK293 Cells | Ribosomal Protein S6 Kinases, 90-kDa - antagonists & inhibitors | Conserved Sequence | Protein Kinase Inhibitors - pharmacology | Tosylphenylalanyl Chloromethyl Ketone - pharmacology | Protein-Serine-Threonine Kinases - metabolism | Proto-Oncogene Proteins c-akt - antagonists & inhibitors | Amino Acid Substitution | Amino acids | Thiols | Mitogens | Protein kinases | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 4/2015, Volume 112, Issue 14, pp. 4298 - 4303
Journal Article
European Journal of Medicinal Chemistry, ISSN 0223-5234, 08/2016, Volume 118, pp. 47 - 63
The phosphoinositide-dependent kinase-1 (PDK1) is one of the main components of the PI3K/Akt pathway. Also named the “master kinase” of the AGC family, PDK1... 
PDK1 inhibitors | Oxindole derivatives | GBM stem cells | Kinase inhibitors | Pyridonyl derivatives | Glioblastoma | MASTER KINASE | CHEMISTRY, MEDICINAL | PHOSPHOINOSITIDE-DEPENDENT KINASE-1 | CHARGES | CELL-PROLIFERATION | CANCER | DISCOVERY | PATHWAY | DYNAMICS | FORCE-FIELD | INHIBITORS | 3-Phosphoinositide-Dependent Protein Kinases - chemistry | Apoptosis - drug effects | Antineoplastic Agents - chemical synthesis | Humans | Indoles - chemical synthesis | Enzyme Inhibitors - chemical synthesis | Antineoplastic Agents - metabolism | Indoles - metabolism | Enzyme Inhibitors - chemistry | Drug Design | Protein Domains | Indoles - pharmacology | Antineoplastic Agents - pharmacology | Enzyme Inhibitors - metabolism | Enzyme Inhibitors - pharmacology | 3-Phosphoinositide-Dependent Protein Kinases - antagonists & inhibitors | 3-Phosphoinositide-Dependent Protein Kinases - metabolism | Antineoplastic Agents - chemistry | Molecular Dynamics Simulation | Amino Acid Motifs | Cell Movement - drug effects | Signal Transduction - drug effects | Glioblastoma - pathology | Cell Line, Tumor | Cell Proliferation - drug effects | Molecular Docking Simulation | Indoles - chemistry | Molecular dynamics | Drugstores | Metastasis | Phosphotransferases | Pharmacy | Derivatives (Financial instruments) | Glioblastoma multiforme | Stem cells | Index Medicus
Journal Article
Biochemical Journal, ISSN 0264-6021, 01/2011, Volume 433, Issue 2, pp. 357 - 369
PDK1 (3-phosphoinositide-dependent protein kinase I) activates a group of protein kinases belonging to the AGC [PKA (protein kinase A)/PKG (protein kinase... 
p70 ribosomal S6 kinase (S6K) | Akt/Akt1 | 3-phosphoinositide-dependent protein kinase | Phosphoinositide 3-kinase (PI3K) | p90 ribosomal S6 kinase (RSK) | Kinase inhibitor | Serum- and glucocorticoid-induced protein kinase (SGK) | Cancer | PDK1 | IN-VIVO ROLE | 3-PHOSPHOINOSITIDE-DEPENDENT PROTEIN KINASE-1 | PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | UCN-01 7-HYDROXYSTAUROSPORINE | P70 S6 KINASE | kinase inhibitor | phosphoinositide 3-kinase (PI3K) | KNOCKIN MUTATION | CAENORHABDITIS-ELEGANS | SMALL-MOLECULE INHIBITORS | HYDROPHOBIC MOTIF PHOSPHORYLATION | cancer | Akt/Akt 1 | serum- and glucocorticoid-induced protein kinase (SGK) | Cyclic AMP-Dependent Protein Kinases - metabolism | Indazoles - chemistry | Ribosomal Protein S6 Kinases, 70-kDa - metabolism | Ribosomal Protein S6 Kinases, 70-kDa - antagonists & inhibitors | Humans | Cells, Cultured | Substrate Specificity | Pyrimidines - pharmacology | Pyrimidines - chemistry | Indazoles - pharmacology | Protein Kinase Inhibitors - chemistry | Animals | Signal Transduction - drug effects | Protein-Serine-Threonine Kinases - antagonists & inhibitors | Mice | Molecular Structure | Protein Kinase Inhibitors - pharmacology | Cyclic AMP-Dependent Protein Kinases - antagonists & inhibitors | Phosphorylation - drug effects | Protein-Serine-Threonine Kinases - metabolism | Index Medicus
Journal Article