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light-chain phosphorylation (5) 5
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American Journal of Physiology - Renal Physiology, ISSN 1931-857X, 12/2009, Volume 297, Issue 6, pp. 1534 - 1542
Smooth muscle contraction is regulated by phosphorylation of the myosin light chain (MLC) catalyzed by MLC kinase and dephosphorylation catalyzed by MLC... 
Bisindolylmaleimide-1 | CPI-17 | MLC phosphorylation | H-1152 | MLC phosphatase | Myosin phosphatase-targeting subunit | MYOSIN-BINDING SUBUNIT | PHYSIOLOGY | INHIBITORY PROTEIN | LIGHT-CHAIN PHOSPHATASE | URINARY-BLADDER | MEDIATED PHOSPHORYLATION | OUTLET OBSTRUCTION | SIGNAL-TRANSDUCTION | PHOSPHATASE TARGETING SUBUNIT | bisindolylmaleimide-1 | CA2+ SENSITIVITY | myosin phosphatase-targeting subunit | UROLOGY & NEPHROLOGY | CALCIUM SENSITIZATION | Protein Subunits | Isometric Contraction - drug effects | Male | Phosphoproteins - metabolism | rho-Associated Kinases - antagonists & inhibitors | Muscle, Smooth - drug effects | rho-Associated Kinases - metabolism | Protein Kinase C - metabolism | Muscle Proteins - metabolism | Muscle, Smooth - physiology | Phosphorylation - drug effects | Cholinergic Agonists - pharmacology | Rabbits | Urinary Bladder - metabolism | Muscle Tonus - drug effects | Protein Kinase C - antagonists & inhibitors | Muscle, Smooth - metabolism | Carbachol - pharmacology | Protein Phosphatase 1 - metabolism | Animals | Urinary Bladder - drug effects | Myosin Light Chains - metabolism | Protein Kinase Inhibitors - pharmacology | In Vitro Techniques | Urinary Bladder - physiology | Complications and side effects | Carbachol | Physiological aspects | Dosage and administration | Genetic aspects | Protein kinases | Muscle contraction
Journal Article
Journal Article
Biochemical Journal, ISSN 0264-6021, 05/2006, Volume 396, Issue 1, pp. 193 - 200
Sustained smooth-muscle contraction or its experimental counterpart, Ca2+ sensitization, by G(q/13)-coupled receptor agonists is mediated via RhoA-dependent... 
p21-activated kinase | Smooth muscle | Integrin-linked kinase | Myosin light chain phosphatase | coupled receptor | Protein kinase C potentiated inhibitor 17 kDa protein (CPI-17) | Receptor, Muscarinic M2 - agonists | Receptor, Adenosine A1 - physiology | GTP-Binding Protein alpha Subunits, Gi-Go - physiology | Receptor, Muscarinic M2 - physiology | Somatostatin - pharmacology | Calcium - physiology | Estrenes - pharmacology | Myosin-Light-Chain Phosphatase - metabolism | Receptors, Somatostatin - physiology | Phosphorylation - drug effects | Chromones - pharmacology | Receptors, G-Protein-Coupled - physiology | Rabbits | Cells, Cultured - drug effects | p38 Mitogen-Activated Protein Kinases - physiology | Imidazoles - pharmacology | Proto-Oncogene Proteins c-akt - physiology | Adenosine - pharmacology | Muscle Contraction - drug effects | Adenosine - analogs & derivatives | Muscle Contraction - physiology | p38 Mitogen-Activated Protein Kinases - antagonists & inhibitors | Cells, Cultured - metabolism | Myosin Light Chains - metabolism | Receptors, Opioid, delta - agonists | Adenosine A1 Receptor Agonists | p21-Activated Kinases | Recombinant Fusion Proteins - physiology | Phosphoproteins - metabolism | Proto-Oncogene Proteins c-akt - genetics | Receptors, Somatostatin - agonists | Transfection | Protein Processing, Post-Translational - drug effects | Pyrrolidinones - pharmacology | Muscle Proteins - metabolism | Protein-Serine-Threonine Kinases - antagonists & inhibitors | Myocytes, Smooth Muscle - metabolism | Protein-Serine-Threonine Kinases - physiology | RNA, Small Interfering - pharmacology | Protein-Serine-Threonine Kinases - genetics | Morpholines - pharmacology | Protein Processing, Post-Translational - physiology | Azepines - pharmacology | Animals | Enkephalin, D-Penicillamine (2,5)- - pharmacology | Phosphatidylinositol 3-Kinases - physiology | Signal Transduction - physiology | Pyridines - pharmacology | Receptors, Opioid, delta - physiology | MEK, MAPK | PI3K, phosphoinositide 3-kinase | smooth muscle | myosin light chain phosphatase | PP1c, protein phosphatase 1 catalytic subunit | Gi-coupled receptor | protein kinase C potentiated inhibitor 17 kDa protein (CPI-17) | ERK kinase | DTT, dithiothreitol | ETA receptor, endothelin A receptor | ERK, extracellular-signal-regulated kinase | PKB, protein kinase B | IP3, inositol 1,4,5-trisphosphate | 4-DAMP, 4-diphenylacetoxy-N-methylpiperidine | integrin-linked kinase | Pen, penicillamine | PAK1, p21-activated kinase 1 | CPA, cyclopentyl adenosine | PI, phosphoinositide | PKC, protein kinase C | Cdc42, cell division cycle 42 | ILK, integrin-linked kinase | MLC, myosin light chain | MYPT1, myosin phosphatase targeting subunit 1 | MLC20, 20 kDa regulatory light chain of myosin II | PHI-1, phosphatase holoenzyme inhibitor-1 | ML-9, 1-(5-chloronaphthalene-1-sulphonyl)-1H-hexahydro-1,4-diazepine hydrochloride | siRNA, small interfering RNA | CPI-17, protein kinase C potentiated inhibitor 17 kDa protein | ACh, acetylcholine | DPDPE, [D-Pen2,D-Pen5]enkephalin | MBP, myelin basic protein | MLCK, MLC kinase | ZIP kinase, zipper-interacting protein kinase | PLC-β3, phospholipase C-β3 | MAPK, mitogen-activated protein kinase
Journal Article
Journal Article
FEBS Letters, ISSN 0014-5793, 2010, Volume 584, Issue 12, pp. 2526 - 2538
Ser(Thr)-O-linked β-N-acetylglucosamine (O-GlcNAc) is a ubiquitous modification of nucleocytoplasmic proteins. Extensive crosstalk exists between... 
Signaling | Phosphorylation | OGA | O-GlcNAcylation | OGT | Mass spectrometry | O-GlcNAc | eNOS | GABAA receptor-associated protein | IRS1 | reverse phase high performance liquid chromatography | posttranslational modification | CaMKIV | succinylated Wheat-Germ Agglutinin | stable isotope labeling with amino acids in cell culture | Pro, Glu, Ser and Thr | tagging-via-substrate | Alzheimer's disease | uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyl transferase | β-D-N-acetylglucosaminidase | mitogen activated protein kinase | gamma-aminobutyric acid | sWGA | l-glutamine: d-fructose-6-phosphate aminotransferase | hOGA | PEST | paired helical filamentous tau | O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate | calcium/calmodulin-dependent kinase IV | AMPK | myosin phosphatase targeting subunit 1 | hexosamine biosynthetic pathway | β-elimination followed by Michael Addition with DTT | RNA interference | kDa | heat shock protein | IKKβ | okadaic acid | UDP-GlcNAc | TPR | electron capture dissociation | dithiothreitol | RNAP II | Iκ kinase β | tetratricopeptide repeats | ECD | Fourier transform ion cyclotron resonance | phosphatidylinositol 3,4,5-triphosphate | PHF-tau | GRIF | PGC-1α | RP-HPLC | coactivator-associated arginine methyltransferase1 | embryonic stem | GFAT | ETD | neurofilament | adenosine triphosphate | transcription factor II D | HAT | ATP | QUIC-tag | collision induced dissociation | histone acetyltransferase | TAS | Forkhead box O1 | electron transfer dissociation | human OGA | HBP | endothelial nitric oxide synthase | CID | photocleavable biotin | peroxisome proliferator activated receptor γ coactivator-1α | collision activated dissociation | RNAi | Hsp | TATA-binding protein-associated factor | CAD | PKA | quantitative isotopic and chemoenzymatic tag | PC-biotin | MAPK | TFIID | GABA | PIP3 | UDP-GlcNAz | PUGNAc | FoxO1 | kilodalton | carboxyl terminal domain | GalT | tandem mass tags | DTT | Thiamet G | O-linked β-N-acetylglucosamine | PTM | AMP-activated protein kinase | BEMAD | FT-ICR | galactosyltransferse | UDP-N-azidoacetylglucosamine | protein kinase A | GSK | uridine diphospho-N-acetylglucosamine | estrogen receptor | TAFII110 | MYPT1 | isobaric tags for relative and absolute quantification | SILAC | TMG | CTD | insulin receptor substrate 1 | CARM1 | glycogen synthase kinase | iTRAQ | TMT | RNA polymerase II | QUANTITATIVE PROTEOMICS | MUTATIONAL HOT-SPOT | BIOCHEMISTRY & MOLECULAR BIOLOGY | C-MYC | POSTTRANSLATIONAL MODIFICATIONS | CELL BIOLOGY | ESTROGEN-RECEPTOR-BETA | BIOPHYSICS | INSULIN-RESISTANCE | GLCNAC-MODIFIED PROTEINS | DISSOCIATION MASS-SPECTROMETRY | NUCLEOCYTOPLASMIC PROTEINS | LINKED N-ACETYLGLUCOSAMINE | Signal Transduction | Humans | Models, Molecular | N-Acetylglucosaminyltransferases - metabolism | Protein Processing, Post-Translational - physiology | Acetylglucosamine - metabolism | Animals | Acetylglucosaminidase - metabolism | Models, Biological | Mass Spectrometry | Acetylation | Binding Sites
Journal Article