X
Search Filters
Format Format
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
animals (719) 719
phosphorylation (555) 555
index medicus (552) 552
humans (445) 445
myosin light chains - metabolism (389) 389
myosin (370) 370
cell biology (346) 346
mice (245) 245
biochemistry & molecular biology (226) 226
muscle proteins (207) 207
proteins (199) 199
male (193) 193
signal transduction (187) 187
myosin-light-chain kinase - metabolism (184) 184
myosin-light-chain phosphatase - metabolism (182) 182
physiology (174) 174
rats (171) 171
kinases (157) 157
cells, cultured (154) 154
article (152) 152
macromolecular substances (152) 152
smooth muscle (150) 150
actin (124) 124
female (120) 120
myosin light chains - genetics (120) 120
myosin light-chain (118) 118
rho-associated kinases - metabolism (118) 118
myosin phosphatase (114) 114
rho-associated kinase (114) 114
research (113) 113
cytoskeleton (112) 112
myosin-light-chain kinase - genetics (110) 110
activation (109) 109
molecular sequence data (108) 108
multidisciplinary sciences (107) 107
smooth-muscle (107) 107
calcium - metabolism (105) 105
amino acid sequence (104) 104
phosphatase (104) 104
actins - metabolism (103) 103
muscle contraction (103) 103
research article (103) 103
protein-serine-threonine kinases - metabolism (102) 102
rho-kinase (100) 100
contraction (95) 95
physiological aspects (95) 95
cells (93) 93
protein-kinase (88) 88
expression (87) 87
analysis (86) 86
medicine (86) 86
rho-associated kinases (86) 86
gene expression (84) 84
myosin-light-chain phosphatase - genetics (84) 84
phosphatases (84) 84
phosphorylation - drug effects (84) 84
science (82) 82
cell line (79) 79
myosin-light-chain phosphatase (79) 79
life sciences (78) 78
rhoa gtp-binding protein - metabolism (78) 78
signal-transduction (78) 78
mutation (77) 77
intracellular signaling peptides and proteins (75) 75
protein binding (74) 74
ca2+ sensitization (73) 73
inhibition (73) 73
enzyme inhibitors - pharmacology (70) 70
light-chain kinase (69) 69
phosphoprotein phosphatases - metabolism (69) 69
rats, sprague-dawley (69) 69
muscle contraction - physiology (68) 68
rodents (68) 68
biophysics (67) 67
myosin light chain (66) 66
in-vivo (65) 65
myosin light chain kinase (65) 65
oncology (65) 65
genetic aspects (64) 64
light-chain phosphatase (63) 63
signal transduction - drug effects (63) 63
pyridines - pharmacology (62) 62
rna interference (62) 62
amides - pharmacology (61) 61
cell line, tumor (61) 61
in vitro techniques (61) 61
myosins - metabolism (61) 61
phosphoproteins - metabolism (61) 61
biology (60) 60
blotting, western (60) 60
kinase (60) 60
contractility (59) 59
muscle contraction - drug effects (59) 59
mice, inbred c57bl (58) 58
muscle, smooth - physiology (58) 58
permeability (58) 58
signal transduction - physiology (58) 58
developmental biology (57) 57
mice, knockout (57) 57
biochemistry (56) 56
more...
Language Language
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Molecular and Cellular Biochemistry, ISSN 0300-8177, 4/2004, Volume 259, Issue 1, pp. 197 - 209
Phosphorylation of myosin II plays an important role in many cell functions, including smooth muscle contraction. The level of myosin II phosphorylation is... 
Biochemistry, general | cGMP-dependent protein kinase | myosin phosphatase | MYPT1 | Rho-kinase | smooth muscle | Medical Biochemistry | Oncology | type 1 phosphatase | CPI-17 | Life Sciences | Rho | Ca 2+ sensitization | Cardiology | Myosin phosphate | Type 1 phosphatase | Smooth muscle | sensitization | INDUCED CA2+ SENSITIZATION | RHO-ASSOCIATED KINASE | INTEGRIN-LINKED KINASE | LIGHT-CHAIN PHOSPHATASE | DEPENDENT PROTEIN-KINASE | TARGETING SUBUNIT | Ca2+ sensitization | CELL BIOLOGY | SIGNAL-TRANSDUCTION | BINDING SUBUNIT | SMOOTH-MUSCLE CONTRACTION | CORONARY-ARTERY SPASM | Calcium - metabolism | Humans | Phosphoprotein Phosphatases - metabolism | Phosphoproteins - metabolism | Cyclic GMP-Dependent Protein Kinases - metabolism | Cyclic GMP-Dependent Protein Kinases - genetics | Protein Subunits - metabolism | Myosin Type II - metabolism | Gene Expression Regulation, Developmental | Myosin-Light-Chain Phosphatase - metabolism | Muscle Proteins - metabolism | Membrane Proteins - metabolism | Myosin Type II - genetics | Protein Phosphatase 1 | Protein Subunits - genetics | Membrane Proteins - genetics | Myosin-Light-Chain Phosphatase - genetics | Rats | Phosphoproteins - genetics | Muscle Proteins - genetics | Animals | Muscle Contraction | Phosphoprotein Phosphatases - genetics | Myosin-Light-Chain Phosphatase - chemistry | Mice | Myosin Type II - chemistry | Muscle, Smooth - enzymology | Proteins | Phosphorylation | Muscular system | Kinases
Journal Article
American Journal of Physiology - Heart and Circulatory Physiology, ISSN 0363-6135, 06/2018, Volume 314, Issue 6, pp. H1192 - H1202
Mutations in genes encoding components of the sarcomere cause cardiomyopathy, which is often associated with abnormal Ca2+ sensitivity of muscle contraction.... 
Heart failure | Myosin phosphatase | Calcium sensitivity | Cardiomyopathy | Transgenic mice | PATHWAYS | heart failure | RHO-ASSOCIATED KINASE | PROTEIN PHOSPHATASE | ACTIVATION | CARDIAC & CARDIOVASCULAR SYSTEMS | PHYSIOLOGY | PHOSPHORYLATION | myosin phosphatase | DILATED CARDIOMYOPATHY | IDENTIFICATION | calcium sensitivity | transgenic mice | DISEASE | PERIPHERAL VASCULAR DISEASE | MUTATIONS | cardiomyopathy | SMOOTH-MUSCLE CONTRACTION | Protein Subunits | Up-Regulation | Phosphorylation | Ventricular Function, Left | Heart Failure - enzymology | Humans | Heart Failure - physiopathology | Cardiomyopathies - enzymology | Arrhythmias, Cardiac - physiopathology | Arrhythmias, Cardiac - pathology | Myocytes, Cardiac - enzymology | Cardiomyopathies - genetics | Cardiomyopathies - physiopathology | Ventricular Remodeling | Ventricular Dysfunction, Left - genetics | rho-Associated Kinases - metabolism | Myosin-Light-Chain Phosphatase - metabolism | Ventricular Dysfunction, Left - enzymology | Arrhythmias, Cardiac - genetics | Calcium Signaling | Cardiac Myosins - metabolism | Disease Models, Animal | Myocardial Contraction | Heart Rate | Genetic Predisposition to Disease | Mice, Inbred C57BL | Myosin-Light-Chain Phosphatase - genetics | Heart Failure - genetics | Mice, Transgenic | Heart Failure - pathology | Ventricular Dysfunction, Left - physiopathology | Myocytes, Cardiac - pathology | Phenotype | Animals | Fibrosis | Arrhythmias, Cardiac - enzymology | Myosin Light Chains - metabolism | Genetic aspects | Phosphatases | Gene expression | Health aspects | Myosin
Journal Article
The Journal of Physiology, ISSN 0022-3751, 10/2017, Volume 595, Issue 19, pp. 6231 - 6247
Key points Smooth muscle myosin regulatory light chain (RLC) is phosphorylated by Ca2+/calmodulin‐dependent myosin light chain kinase and dephosphorylated by... 
airway smooth muscle | contraction | myosin light chain phosphatase | myosin regulatory light chain phosphorylation | myosin light chain kinase | LIGHT-CHAIN KINASE | PROTEIN PHOSPHATASE-1 | RHO-ASSOCIATED KINASE | CA2+ SENSITIZATION | SKELETAL-MUSCLE | PHYSIOLOGY | MYOGENIC RESPONSE | SALT-INDUCED HYPERTENSION | NEUROSCIENCES | BLOOD-PRESSURE | PHOSPHATASE TARGETING SUBUNIT-1 | CALCIUM SENSITIZATION | Phosphorylation | Signal Transduction | Trachea - cytology | Mice, Inbred C57BL | Myosin-Light-Chain Phosphatase - genetics | Cells, Cultured | Myocytes, Smooth Muscle - physiology | Male | Trachea - metabolism | Carbachol - pharmacology | Protein Phosphatase 1 - metabolism | Animals | Cattle | Myosin-Light-Chain Phosphatase - metabolism | Protein Phosphatase 1 - genetics | Mice | Myosin Light Chains - metabolism | Protein Processing, Post-Translational | Myocytes, Smooth Muscle - drug effects | Myocytes, Smooth Muscle - metabolism | Cholinergic Agonists - pharmacology | Phosphatases | Genetically modified organisms | Myosin | Physiological aspects | Smooth muscle | Calcium-binding proteins | Muscle proteins | Electric fields | Protein kinase C | Calcium | Acetylcholine receptors (muscarinic) | Phosphoprotein phosphatase | Modules | Chains | Stimulation | Dephosphorylation | Phosphatase | Physiological responses | Myosin-light-chain kinase | Myosin-light-chain-phosphatase | Proteins | Respiratory tract | Neostigmine | Rodents | Calcium-binding protein | Light | Nerves | Physiology | Catalysis | Trachea | Genetic modification | Calmodulin | Pharmacology | Muscle contraction | Cholinesterase | Signaling | Sensitivity | Inhibitors | Carbachol | Protein phosphatase | Mutation | Paxillin | Molecular and Cellular | Research Paper
Journal Article
PLoS ONE, ISSN 1932-6203, 07/2013, Volume 8, Issue 7, p. e70502
Journal Article
Nature communications, ISSN 2041-1723, 2018, Volume 9, Issue 1, pp. 4826 - 16
Angiogenesis is a dynamic process relying on endothelial cell rearrangements within vascular tubes, yet the underlying mechanisms and functional relevance are... 
ACTIN POLYMERIZATION | MULTIDISCIPLINARY SCIENCES | NOTCH | VE-CADHERIN | RETINAL ANGIOGENESIS | ADHERENS JUNCTIONS | VESSEL FUSION | SPROUTING ANGIOGENESIS | MYOSIN PHOSPHATASE | DEVELOPING ZEBRAFISH | MASS-SPECTROMETRY | Protein Kinases - metabolism | Protein Kinases - genetics | Retina - metabolism | Retina - growth & development | Human Umbilical Vein Endothelial Cells - metabolism | Embryo, Mammalian | Humans | Gene Expression Profiling | Phosphatidylinositol 3-Kinases - metabolism | Lung - cytology | Phosphoproteins - metabolism | Actomyosin - genetics | Retina - cytology | Gene Expression Regulation, Developmental | Human Umbilical Vein Endothelial Cells - cytology | Myosin-Light-Chain Phosphatase - metabolism | Lung - metabolism | Repressor Proteins - metabolism | Signal Transduction | Neovascularization, Physiologic - genetics | Mice, Inbred C57BL | Myosin-Light-Chain Phosphatase - genetics | Intercellular Junctions - metabolism | Repressor Proteins - genetics | Mice, Transgenic | Zebrafish | Phosphoproteins - genetics | Actomyosin - metabolism | Phosphatidylinositol 3-Kinases - genetics | Animals | Embryo, Nonmammalian | Lung - growth & development | Mice | Intercellular Junctions - ultrastructure | Lung - blood supply | Body Patterning - genetics | Pattern formation | Phosphorylation | Actomyosin | Contractility | Phosphatase | Kinases | Endothelial cells | 1-Phosphatidylinositol 3-kinase | Myosin-light-chain-phosphatase | Proteins | Angiogenesis | Signal transduction | Clonal deletion | Myosin | Deletion | Tubes | Proteïnes quinases | Regulació genètica | Neovascularization | Genetic regulation | Gene expression | Angiogènesi | Protein kinases | Expressió gènica
Journal Article
PloS one, ISSN 1932-6203, 2013, Volume 8, Issue 9, p. e75766
Journal Article