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Biochemical and biophysical research communications, ISSN 0006-291X, 2018, Volume 506, Issue 2, pp. 394 - 402
Journal Article
Journal Article
Journal of controlled release, ISSN 0168-3659, 2015, Volume 210, pp. 189 - 197
The intestinal epithelium functions to effectively restrict the causal uptake of luminal contents but has been demonstrated to transiently increase... 
Tight junction function | Myosin light chain phosphatase | Protein–protein interactions | Cell penetrating peptide | Paracellular transport | Insulin delivery | Abbreviations CPP Cell Penetrating Peptide | pMLC Phosphorylated myosin light chain | SPPS Solid phase peptide synthesis | TJ Tight junction | MLC Myosin light chain | PK/PD Pharmacokinetics/pharmacodynamics | SC Subcutaneous | MLCK Myosin light chain kinase | FD Fluorescent dextran | DAPI 4′ 6-diamidino-2-phenylindole | PBS Phosphate buffer saline | PKC Protein kinase C | FMC 9-fluorenylmethyloxycarbonyl | MLCP Myosin light chain phosphatase | ILI Intraluminal injection | MTS 3-(4,5-dimethylthiazol-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium | MYPT1 Myosin phosphatase target subunit | ABSORPTION ENHANCEMENT | PROTEIN PHOSPHATASE-1 | RHO-ASSOCIATED KINASE | MEMBRANE-PERMEANT PEPTIDE | MECHANISMS | CHEMISTRY, MULTIDISCIPLINARY | Protein-protein interactions | INTESTINAL-ABSORPTION | TIGHT JUNCTIONS | SMOOTH-MUSCLE | IN-VITRO | PHARMACOLOGY & PHARMACY | SODIUM CAPRATE | Caco-2 Cells | Insulin - pharmacology | Phosphorylation | Blood Glucose - analysis | Rats, Wistar | Humans | Insulin - administration & dosage | Male | Myosin-Light-Chain Phosphatase | Animals | Biological Transport | Myosin Light Chains - metabolism | Oligopeptides - administration & dosage | Oligopeptides - pharmacology | Phosphoprotein Phosphatases | Dextran | Biological products | Peptides | Blood sugar | Myosin | Permeability | Muscle proteins | Insulin | Phosphatases | Protein kinases | Index Medicus | PKC, Protein kinase C | MLC, Myosin light chain | pMLC, Phosphorylated myosin light chain | pharmacodynamics | TJ, Tight junction | PD, Pharmacokinetics | MTS, 3-(4,5-dimethylthiazol-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium | MLCK, Myosin light chain kinase | DAPI, 4′,6-diamidino-2-phenylindole | PBS, Phosphate buffer saline | MLCP, Myosin light chain phosphatase | MYPT1, Myosin phosphatase target subunit | CPP, Cell Penetrating Peptide | SC, Subcutaneous | FD, Fluorescent dextran | ILI, Intraluminal injection | FMC, 9-fluorenylmethyloxycarbonyl | SPPS, Solid phase peptide synthesis
Journal Article
Gene, ISSN 0378-1119, 2018, Volume 664, pp. 152 - 167
The MYH9 gene encodes the heavy chain of non-muscle myosin IIA, a widely expressed cytoplasmic myosin that participates in a variety of processes requiring the... 
Kidney disease | Actin-myosin cytoskeleton | Deafness | Inherited thrombocytopenia | Class II myosin | Mouse models | Cell-cell adhesion | Non-muscle myosin | MYH9-related disease | Tumor suppressor | MYH9 gene | PROTEIN-KINASE-C | INHERITED THROMBOCYTOPENIAS | GENOTYPE-PHENOTYPE CORRELATIONS | HEAVY-CHAIN IIA | PLATELET MYOSIN | SMOOTH-MUSCLE MYOSIN | GENETICS & HEREDITY | MAY-HEGGLIN | FOCAL SEGMENTAL GLOMERULOSCLEROSIS | FECHTNER-SYNDROME | Myosin Heavy Chains - chemistry | Cell Line | Phosphorylation | Deafness - genetics | Humans | Thrombocytopenia - congenital | Myosin Heavy Chains - genetics | Hearing Loss, Sensorineural - genetics | Molecular Motor Proteins - chemistry | Molecular Motor Proteins - genetics | Myosin Heavy Chains - metabolism | Nonmuscle Myosin Type IIA - metabolism | Thrombocytopenia - genetics | Animals | Neoplasms - genetics | Nonmuscle Myosin Type IIA - genetics | Renal Insufficiency, Chronic - genetics | Molecular Motor Proteins - metabolism | Mice | Mutation | Nonmuscle Myosin Type IIA - chemistry | Embryonic development | Squamous cell carcinoma | Fluorescence | Transforming growth factors | Embryonic stem cells | Muscle proteins | Chronic kidney failure | Casein | Actin | Analysis | Myosin | Protein kinases | Protein binding | mouse models | cell-cell adhesion | inherited thrombocytopenia | actin-myosin cytoskeleton | kidney disease | tumor suppressor | class II myosin | non-muscle myosin | deafness
Journal Article
Journal Article
The FEBS Journal, ISSN 1742-464X, 06/2015, Volume 282, Issue 12, pp. 2379 - 2393
Dilated cardiomyopathy (DCM) is a disease of the myocardium characterized by left ventricular dilatation and diminished contractile function. Here we describe... 
secondary structure | muscle contraction | RLC‐reconstituted β‐myosin | ATPase activity | phosphorylation | RLC-reconstituted β-myosin | Phosphorylation | Secondary structure | Muscle contraction | CA2+-SENSITIVITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | MOUSE | MUSCLE | RLC-reconstituted beta-myosin | HYPERTROPHIC CARDIOMYOPATHY | RLC PHOSPHORYLATION | DEPHOSPHORYLATION | HUMAN HEART | BINDING | I-TASSER | SUBFRAGMENT-1 | Myosin Heavy Chains - chemistry | Myosin Light Chains - genetics | Humans | Actins - metabolism | Male | Myosin Heavy Chains - metabolism | DNA Mutational Analysis | Adult | Female | Circular Dichroism | Cardiac Myosins - metabolism | Cardiomyopathy, Dilated - genetics | Recombinant Proteins - metabolism | Protein Structure, Secondary | Cardiac Myosins - genetics | Adenosine Triphosphatases - metabolism | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Cardiomyopathy, Dilated - metabolism | Animals | Pedigree | Myosin Light Chains - chemistry | Adenosine Triphosphatases - chemistry | Protein Conformation | Adenosine Triphosphatases - genetics | Myosin Light Chains - metabolism | Mutation | Cardiac Myosins - chemistry | Sus scrofa | Amino Acid Substitution | Genetic aspects | Muscle proteins | Cardiomyopathy | Heart diseases | Myosin | Genotype & phenotype | Myosin Regulatory Light Chain (RLC)
Journal Article