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Biochemical Journal, ISSN 0264-6021, 01/2005, Volume 385, Issue 2, pp. 399 - 408
We developed a high-throughput HTRF (homogeneous time-resolved fluorescence) assay for Akt kinase activity and screened approx. 270000 compounds for their... 
Allosteric inhibitor | Protein kinase B (PKB) | Inhibitor | Pleckstrin homology domain | Akt | Kinase | PROTEIN-KINASE-B | INDUCED APOPTOSIS | TYROSINE KINASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | pleckstrin homology domain | allosteric inhibitor | COWDEN-DISEASE | kinase | inhibitor | STRUCTURAL BASIS | protein kinase B (PKB) | TUMOR-SUPPRESSOR | MOLECULAR-CLONING | CELL-LINE LNCAP | HUMAN CANCER | Phosphoproteins - immunology | Prostatic Neoplasms - chemistry | Humans | Peptides - genetics | Blood Proteins - immunology | Male | Isoenzymes - chemistry | Phosphoproteins - chemistry | Carcinoma - chemistry | Peptides - metabolism | TNF-Related Apoptosis-Inducing Ligand | Blood Proteins - genetics | Adenosine Triphosphate - metabolism | Phosphorylation - drug effects | 3-Phosphoinositide-Dependent Protein Kinases | Protein-Serine-Threonine Kinases - metabolism | Peptides - immunology | Enzyme Inhibitors - pharmacology | Heterocyclic Compounds, 2-Ring - pharmacology | Tumor Necrosis Factor-alpha - pharmacology | Cell Line, Tumor | Prostatic Neoplasms - metabolism | Uterine Cervical Neoplasms - pathology | Quinoxalines - pharmacology | Caspases - metabolism | Uterine Cervical Neoplasms - metabolism | Cloning, Molecular | Protein-Serine-Threonine Kinases - antagonists & inhibitors | Female | Molecular Structure | Carcinoma - pathology | Binding, Competitive | Protein Structure, Tertiary | Proto-Oncogene Proteins - metabolism | Prostatic Neoplasms - pathology | Proto-Oncogene Proteins - antagonists & inhibitors | Peptides - chemistry | Membrane Glycoproteins - pharmacology | Blood Proteins - chemistry | Phosphoproteins - genetics | Enzyme Activation - drug effects | Proto-Oncogene Proteins c-akt | Sequence Homology, Amino Acid | Apoptosis Regulatory Proteins | Signal Transduction - physiology | Uterine Cervical Neoplasms - chemistry | Carcinoma - metabolism | Benzylamines - pharmacology | Isoenzymes - antagonists & inhibitors | Index Medicus | cdk2, cyclin-dependent kinase 2 | FGFR, fibroblast growth factor receptor | MEK, MAPK | SH, Src homology | PI3K, phosphoinositide 3-kinase | DOPS, 1,2-dioleoyl-sn-glycero-3-phospho-L-serine | ERK kinase | DOPC, 1,2-dioleoyl-sn-glycero-3-phosphocholine | DTT, dithiothreitol | PTEN, phosphatase and tensin homologue deleted on chromosome 10 | ERK, extracellular-signal-regulated kinase | PEG, poly(ethylene glycol) | PKC, protein kinase C | FLT, Fms-related tyrosine kinase | lymphoma 1 | GSK3, glycogen synthase kinase 3 | TRAIL, tumour-necrosis-factor-related apoptosis-inducing ligand | HTRF, homogeneous time-resolved fluorescence | PH, pleckstrin homology | MAPKK1, MAPK kinase 1 | FBS, foetal bovine serum | PDK, phosphoinositide-dependent kinase | TCL1, T-cell leukaemia | MAPK, mitogen-activated protein kinase | PKA, protein kinase A | SGK, serum- and glucocorticoid-inducible kinase
Journal Article
Journal Article
Journal Article
Biochemical Journal, ISSN 0264-6021, 02/2017, Volume 474, Issue 4, pp. 539 - 556
Kindlins co-activate integrins alongside talin. They possess, like talin, a FERM domain (4.1-erythrin-radixin-moiesin domain) comprising F0-F3 subdomains, but... 
GRP1 PH DOMAIN | PERIPHERAL MEMBRANE-PROTEINS | MOLECULAR-DYNAMICS | MODEL MEMBRANES | ALPHA-IIB-BETA-3 | INTEGRIN ACTIVATION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | FORCE-FIELD | CELL-ADHESION | SIMULATIONS | Cytoskeletal Proteins - genetics | Crystallography, X-Ray | Phosphatidylcholines - metabolism | Receptors, Cytoplasmic and Nuclear - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Cytoskeletal Proteins - metabolism | Phosphatidylinositols - metabolism | Protein Interaction Domains and Motifs | Binding Sites | Pleckstrin Homology Domains | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | Phosphatidylinositols - chemistry | Phosphatidylserines - metabolism | Phosphatidylserines - chemistry | Recombinant Proteins - chemistry | Receptors, Cytoplasmic and Nuclear - genetics | Recombinant Proteins - genetics | Cytoskeletal Proteins - chemistry | Phosphatidylcholines - chemistry | Molecular Dynamics Simulation | Sequence Homology, Amino Acid | Sequence Alignment | Animals | Protein Conformation, beta-Strand | Escherichia coli - genetics | Protein Binding | Mice | Kinetics | Receptors, Cytoplasmic and Nuclear - metabolism | Index Medicus | X-ray crystallography | 1 | lipid clustering | s | 4 | surface plasmon resonance | 18 | 8 | 51 | molecular dynamics | PH domain
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 05/2011, Volume 286, Issue 21, pp. 18650 - 18657
Four-phosphate-adaptor protein 1 (FAPP1) regulates secretory transport from the trans-Golgi network (TGN) to the plasma membrane. FAPP1 is recruited to the... 
APOPTOSIS | MECHANISM | STRUCTURAL BASIS | MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PTDINSP | ACIDIFICATION | PROTEINS | BINDING | SOFTWARE | FYVE DOMAIN | Adaptor Proteins, Signal Transducing - chemistry | Protein Structure, Tertiary | Phosphatidylinositol Phosphates - metabolism | Humans | Crystallography, X-Ray | Structure-Activity Relationship | Intracellular Membranes - chemistry | Phosphatidylinositol Phosphates - genetics | trans-Golgi Network - genetics | Phosphatidylinositol Phosphates - chemistry | Protein Folding | trans-Golgi Network - metabolism | Biological Transport | Mutagenesis | Adaptor Proteins, Signal Transducing - genetics | Nuclear Magnetic Resonance, Biomolecular | Protein Binding | ADP-Ribosylation Factor 1 - metabolism | ADP-Ribosylation Factor 1 - genetics | Adaptor Proteins, Signal Transducing - metabolism | trans-Golgi Network - chemistry | ADP-Ribosylation Factor 1 - chemistry | Intracellular Membranes - metabolism | Index Medicus | MEMBRANE PROTEINS | MUTAGENESIS | PROTEIN STRUCTURE | BASIC BIOLOGICAL SCIENCES | RESOLUTION | MEMBRANES | CRYSTAL STRUCTURE | 60 APPLIED LIFE SCIENCES | FASTENING | TRANSPORT | PLASMA | RESONANCE | AFFINITY | LIPIDS | Membrane Proteins | Phosphatidylinositol | ARF1 | Lipids | Membrane Lipids | Protein Structure | PH Domain | Phosphatidylinositol 4-Phosphate | Protein-Protein Interactions | FAPP1
Journal Article
Biochemical Journal, ISSN 0264-6021, 10/2000, Volume 351, Issue 1, pp. 19 - 31
Journal Article
Nature, ISSN 0028-0836, 09/1994, Volume 371, Issue 6493, pp. 168 - 170
THE pleckstrin homology (PH) domain is a new protein module of around 100 amino acids found in several proteins involved in signal transduction(1-5). Although... 
PH DOMAIN | ADRENERGIC-RECEPTOR KINASE | EXPRESSION | SIGNALING PROTEINS | MULTIDISCIPLINARY SCIENCES | PHOSPHOLIPASE C-DELTA-1 | Amino Acid Sequence | Cell Line | Phosphatidylinositol 4,5-Diphosphate | Phosphatidylinositol Phosphates - metabolism | Magnetic Resonance Spectroscopy |