X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (55990) 55990
Newsletter (10341) 10341
Publication (5567) 5567
Book Review (5368) 5368
Book Chapter (804) 804
Conference Proceeding (579) 579
Dissertation (237) 237
Newspaper Article (79) 79
Reference (33) 33
Magazine Article (29) 29
Book / eBook (21) 21
Government Document (16) 16
Transcript (10) 10
Web Resource (8) 8
Data Set (4) 4
Journal / eJournal (3) 3
Trade Publication Article (3) 3
Paper (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (43838) 43838
animals (32865) 32865
myosin (31022) 31022
muscle proteins (15780) 15780
humans (15215) 15215
cell biology (10810) 10810
research (10230) 10230
biochemistry & molecular biology (9597) 9597
male (8896) 8896
myosins - metabolism (8756) 8756
actin (8582) 8582
proteins (7525) 7525
rats (7515) 7515
mice (7284) 7284
phosphorylation (6963) 6963
female (6184) 6184
actins - metabolism (6058) 6058
analysis (5450) 5450
rabbits (5055) 5055
physiology (4667) 4667
physiological aspects (4401) 4401
cells (4351) 4351
protein binding (4320) 4320
reports (4261) 4261
kinetics (4110) 4110
expression (3933) 3933
biophysics (3836) 3836
molecular sequence data (3816) 3816
macromolecular substances (3768) 3768
cells, cultured (3749) 3749
amino acid sequence (3572) 3572
universities and colleges (3558) 3558
skeletal-muscle (3444) 3444
myosin heavy chains - metabolism (3376) 3376
article (3337) 3337
muscles (3233) 3233
mutation (3182) 3182
muscle contraction (3130) 3130
myosin heavy chains - genetics (3080) 3080
cytoskeleton (2882) 2882
gene expression (2874) 2874
calcium - metabolism (2844) 2844
biochemistry (2781) 2781
cardiac & cardiovascular systems (2773) 2773
models, biological (2730) 2730
multidisciplinary sciences (2669) 2669
myosins - genetics (2601) 2601
signal transduction (2531) 2531
adult (2527) 2527
protein (2510) 2510
myosin heavy-chain (2465) 2465
genetic aspects (2446) 2446
in vitro techniques (2419) 2419
binding sites (2402) 2402
myocardium - metabolism (2362) 2362
time factors (2338) 2338
adenosine triphosphatases - metabolism (2259) 2259
muscle, skeletal - metabolism (2246) 2246
protein conformation (2152) 2152
cell line (2138) 2138
developmental biology (2121) 2121
myosin light chains - metabolism (2115) 2115
calcium (2103) 2103
myosins - chemistry (2103) 2103
immunohistochemistry (2091) 2091
contraction (2090) 2090
activation (2073) 2073
heart (2061) 2061
muscle (2027) 2027
skeletal muscle (2014) 2014
muscle contraction - physiology (2007) 2007
neurosciences (1994) 1994
myosins - analysis (1986) 1986
myosins - physiology (1985) 1985
biology (1955) 1955
chickens (1950) 1950
base sequence (1933) 1933
adenosine triphosphate - metabolism (1925) 1925
middle aged (1914) 1914
genes (1894) 1894
electrophoresis, polyacrylamide gel (1891) 1891
phenotype (1888) 1888
smooth muscle (1866) 1866
microscopy, electron (1762) 1762
gene-expression (1753) 1753
binding (1746) 1746
f-actin (1733) 1733
rats, sprague-dawley (1724) 1724
rodents (1718) 1718
abridged index medicus (1712) 1712
research article (1712) 1712
muscles - metabolism (1671) 1671
life sciences (1650) 1650
myosin-ii (1607) 1607
identification (1602) 1602
myosins (1573) 1573
genetics & heredity (1567) 1567
gene (1558) 1558
muscle, skeletal - physiology (1554) 1554
space life sciences (1536) 1536
more...
Library Location Library Location
Library Location Library Location
X
Sort by Item Count (A-Z)
Filter by Count
Gerstein Science - Stacks (16) 16
Online Resources - Online (8) 8
UTL at Downsview - May be requested (4) 4
Chemistry (A D Allen) - Stacks (2) 2
Collection Dvlpm't (Acquisitions) - Closed Orders (2) 2
Earth Sciences (Noranda) - Stacks (2) 2
UofT at Mississauga - Stacks (1) 1
UofT at Scarborough - Withdrawn (1) 1
more...
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (65449) 65449
Japanese (552) 552
Russian (505) 505
French (213) 213
Chinese (212) 212
German (204) 204
Spanish (68) 68
Polish (52) 52
Portuguese (38) 38
Korean (30) 30
Ukrainian (30) 30
Italian (23) 23
Czech (10) 10
Hungarian (7) 7
Dutch (4) 4
Swedish (4) 4
Persian (3) 3
Bulgarian (2) 2
Estonian (2) 2
Turkish (2) 2
Catalan (1) 1
Indonesian (1) 1
Slovenian (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


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. e27 - e27
Journal Article
BBA - Bioenergetics, ISSN 0005-2728, 08/2016, Volume 1857, pp. e53 - e54
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
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
2008, Proteins and cell regulation, ISBN 1402065191, Volume 7
Web Resource
2008, Proteins and cell regulation, ISBN 1402065191, Volume 7
Web Resource