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1999, Molecular biology intelligence unit (Unnumbered), ISBN 1570595666, Volume 5, 165
Book
Journal of Controlled Release, ISSN 0168-3659, 07/2015, 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
Journal Article
BBA - Bioenergetics, ISSN 0005-2728, 08/2016, Volume 1857, pp. e53 - e54
Journal Article
BBA - Bioenergetics, ISSN 0005-2728, 08/2016, Volume 1857, pp. e27 - e27
Journal Article
Journal of Cell Science, ISSN 0021-9533, 08/2017, Volume 130, Issue 16, pp. e1602 - e1602
Journal Article
Biophysical Journal, ISSN 0006-3495, 01/2015, Volume 108, Issue 2, p. 596
Journal Article
Journal Article
Journal of Clinical Investigation, ISSN 0021-9738, 09/2009, Volume 119, Issue 9, pp. 2772 - 2786
Journal Article
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... 
secondary structure | muscle contraction | reconstituted β‐myosin | ase activity | RLC | ATP | phosphorylation | RLC-reconstituted β-myosin | Phosphorylation | ATPase activity | 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 | Index Medicus | Myosin Regulatory Light Chain (RLC)
Journal Article
Archives of Biochemistry and Biophysics, ISSN 0003-9861, 09/2013, Volume 537, Issue 2, p. 198
Display Omitted 
Myosin
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2009, Volume 106, Issue 52, pp. 22193 - 22198
Stable, single alpha-helix (SAH) domains are widely distributed in the proteome, including in myosins, but their functions are unknown. To test whether SAH... 
Molecules | Actins | Lead | Bending | Motors | Stiffness | Mathematical functions | Chimeras | Electron microscopy | Intelligence quotient | Optical trap | ATPase | Single alpha helix | HEAD | MOLECULE MECHANICS | NECK LENGTH | MULTIDISCIPLINARY SCIENCES | single alpha helix | MODEL | OPTICAL TWEEZERS | PROCESSIVITY | optical trap | MOTOR | KINETIC MECHANISM | MOVEMENT | electron microscopy | RABBIT | Myosin Heavy Chains - chemistry | Myosin Type V - chemistry | Myosin Type V - ultrastructure | Myosin Heavy Chains - ultrastructure | Actins - metabolism | Molecular Sequence Data | Myosin Heavy Chains - genetics | Protozoan Proteins - genetics | Myosin Heavy Chains - metabolism | Recombinant Fusion Proteins - metabolism | Myosins - ultrastructure | Protozoan Proteins - metabolism | Base Sequence | Myosins - metabolism | Protozoan Proteins - chemistry | Protein Structure, Tertiary | Amino Acid Sequence | DNA, Recombinant - genetics | Microscopy, Electron, Transmission | Myosin Type V - metabolism | Protein Structure, Secondary | Models, Molecular | Recombinant Fusion Proteins - chemistry | Myosins - chemistry | Myosins - genetics | Recombinant Fusion Proteins - ultrastructure | Animals | Myosin Type V - genetics | Models, Biological | Recombinant Fusion Proteins - genetics | Protozoan Proteins - ultrastructure | Mice | Adenosine Diphosphate - metabolism | In Vitro Techniques | Proteins | Myosin | Distribution | Physiological aspects | Biochemistry | Research | Structure | Rodents | Cells | Proteomics | Index Medicus | Biological Sciences
Journal Article
Journal Article
2008, Proteins and cell regulation, ISBN 1402065191, Volume 7
Web Resource
2008, Proteins and cell regulation, ISBN 1402065191, Volume 7
Web Resource
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 08/2017, Volume 114, Issue 35, pp. E7236 - E7244
Studies in fission yeast Schizosaccharomyces pombe have provided the basis for the most advanced models of the dynamics of the cytokinetic contractile ring.... 
Phosphorylation | Fission yeast | Cytokinesis | Myosin-II | CYTOKINETIC CONTRACTILE RING | PROTEIN | myosin-II | BUDDING YEAST | cytokinesis | MULTIDISCIPLINARY SCIENCES | NONMUSCLE | HEAVY-MEROMYOSIN | ASSEMBLY MECHANISM | TROPOMYOSIN | SMOOTH-MUSCLE MYOSIN | FILAMENTS | fission yeast | phosphorylation | SCHIZOSACCHAROMYCES-POMBE | Amino Acid Sequence | Myosin Type II - physiology | Actin Cytoskeleton - metabolism | Myosin Type V - metabolism | Schizosaccharomyces pombe Proteins - genetics | Down-Regulation | Actins - metabolism | Myosin Heavy Chains - genetics | Myosin Heavy Chains - metabolism | Schizosaccharomyces - metabolism | Myosin Type II - metabolism | Cytokinesis - physiology | Cell Division | Myosin Heavy Chains - physiology | Schizosaccharomyces pombe Proteins - metabolism | Cytoskeletal Proteins - metabolism | Myosins - metabolism | Microfilament Proteins - metabolism | Myosin Type II - genetics | Schizosaccharomyces pombe Proteins - physiology | Contractile Proteins | Physiological aspects | Saccharomyces | Observations | Actin | Salts | Yeast | Contractility | Cell division | Chains | Ultracentrifugation | Baculovirus | Sedimentation | Inclination | Fission | Cdc4 protein | Studies | Proteins | Insects | Light chains | Myosin | Affinity | Cell migration | Adenosine triphosphatase | Index Medicus | Biological Sciences | PNAS Plus
Journal Article