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biochemistry & molecular biology (528) 528
actins - metabolism (476) 476
actin (376) 376
gelsolin - metabolism (346) 346
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gelsolin - physiology (99) 99
actins - physiology (96) 96
neurosciences (94) 94
muscle proteins (93) 93
microfilament proteins - physiology (91) 91
activation (89) 89
molecular weight (88) 88
analysis (87) 87
phosphorylation (87) 87
filaments (85) 85
microfilament proteins - chemistry (84) 84
electrophoresis, polyacrylamide gel (81) 81
actin cytoskeleton - metabolism (80) 80
microfilament proteins - genetics (80) 80
cell line (78) 78
protein conformation (78) 78
physiological aspects (77) 77
cytoskeleton - metabolism (75) 75
complex (74) 74
gelsolin - pharmacology (74) 74
signal transduction (72) 72
gene expression (71) 71
microscopy, electron (71) 71
physiology (71) 71
mutation (70) 70
actins (69) 69
carrier proteins - metabolism (69) 69
calcium-binding proteins - metabolism (68) 68
cattle (65) 65
time factors (64) 64
phosphatidylinositol 4,5-bisphosphate (62) 62
article (60) 60
biochemical research methods (60) 60
protein structure, tertiary (60) 60
binding proteins (59) 59
in vitro techniques (59) 59
actin-binding protein (58) 58
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blotting, western (54) 54
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cytoskeleton - physiology (52) 52
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multidisciplinary sciences (50) 50
calcium - pharmacology (49) 49
in-vitro (49) 49
models, molecular (49) 49
plasma (49) 49
regulatory protein (49) 49
actin depolymerizing factors (48) 48
biochemistry (48) 48
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Developmental Cell, ISSN 1534-5807, 07/2015, Volume 34, Issue 2, pp. 152 - 167
Journal Article
Journal of Proteomics, ISSN 1874-3919, 2011, Volume 74, Issue 7, pp. 1123 - 1134
Journal Article
The Journal of Pathology, ISSN 0022-3417, 11/2011, Volume 225, Issue 3, pp. 401 - 413
Epidermolysis bullosa (EB) is a severe genetic skin fragility syndrome characterized by blister formation. The molecular basis of EB is still largely unknown... 
TGF‐β | wound healing | type VII collagen | epidermolysis bullosa | Flightless | Flii | TGF-β | FLIGHTLESS-I PROTEIN | FIBROBLAST CELL THERAPY | PATHOLOGY | GELSOLIN FAMILY | ACTIN-REMODELING PROTEIN | TGF-beta | GROWTH-FACTOR-BETA | ONCOLOGY | VII COLLAGEN | SKIN | EXPRESSION | WOUND REPAIR | TETRASPANIN CD151 | Cell Proliferation | Cytoskeletal Proteins - genetics | Fibroblasts - physiology | Skin - metabolism | Humans | Receptors, Cytoplasmic and Nuclear - biosynthesis | Integrins - metabolism | Epidermolysis Bullosa Acquisita - metabolism | Autoimmune Diseases - genetics | Epidermolysis Bullosa Acquisita - genetics | Collagen Type VII - biosynthesis | Cytoskeletal Proteins - biosynthesis | Autoimmune Diseases - metabolism | Autoimmune Diseases - pathology | Cell Differentiation - physiology | Microfilament Proteins - genetics | Disease Models, Animal | Cells, Cultured | Gene Expression Regulation | Mice, Transgenic | Receptors, Cytoplasmic and Nuclear - genetics | Smad Proteins - physiology | Fibroblasts - pathology | Transforming Growth Factor beta1 - physiology | Microfilament Proteins - biosynthesis | Animals | Cell Adhesion - physiology | Signal Transduction - physiology | Mice | Mice, Inbred BALB C | Wound Healing - physiology | Epidermolysis Bullosa Acquisita - pathology | Animal models | Smad protein | Wound healing | Epidermolysis bullosa | Gels | Epidermolysis bullosa acquisita | Survival | Actin | Collagen | Fibrosis | Fibroblasts | Skin | Integrins | Index Medicus
Journal Article
Biochemistry, ISSN 0006-2960, 05/2010, Volume 49, Issue 20, pp. 4349 - 4360
Caenorhabditis elegans gelsolin-like protein-1 (GSNL-1) is a new member of the gelsolin family of actin regulatory proteins [Klaavuniemi, T., Yamashiro, S.,... 
F-ACTIN | SITE | MECHANISM | TERMINAL HALF | BIOCHEMISTRY & MOLECULAR BIOLOGY | DYNAMICS | INTERACTING PROTEIN-1 | PLASMA GELSOLIN | REGULATORS | DEPOLYMERIZING FACTOR/COFILIN | IDENTIFICATION | Actin Capping Proteins - metabolism | Actin Depolymerizing Factors - physiology | Molecular Weight | Actin Depolymerizing Factors - genetics | Intracellular Calcium-Sensing Proteins - genetics | Gelsolin - metabolism | Caenorhabditis elegans Proteins - chemistry | Intracellular Calcium-Sensing Proteins - physiology | Actins - metabolism | Caenorhabditis elegans Proteins - metabolism | Intracellular Calcium-Sensing Proteins - chemistry | Actin Depolymerizing Factors - metabolism | Phosphatidylinositols - metabolism | Gelsolin - physiology | Actin Cytoskeleton - metabolism | Caenorhabditis elegans - metabolism | Actin Capping Proteins - chemistry | Mutant Proteins - metabolism | Intracellular Calcium-Sensing Proteins - metabolism | Protein Interaction Mapping | Actin Capping Proteins - physiology | Animals | Models, Biological | Mutant Proteins - chemistry | Caenorhabditis elegans Proteins - physiology | Gelsolin - chemistry | Caenorhabditis elegans Proteins - genetics | Actin Depolymerizing Factors - chemistry | Protein Binding - physiology | Protein Structure, Tertiary - physiology | Caenorhabditis elegans | Phosphoinositides | Actin | Physiological aspects | Genetic aspects | Chemical properties | Structure | Index Medicus
Journal Article
Journal of Cell Biology, ISSN 0021-9525, 07/2013, Volume 202, Issue 2, pp. 365 - 379
Journal Article
Journal Article
Journal Article
Journal of Leukocyte Biology, ISSN 0741-5400, 02/2008, Volume 83, Issue 2, pp. 245 - 253
Serum amyloid A (SAA) is one of the acute‐phase reactants, a group of plasma proteins that increases immensely in concentration during microbial infections and... 
WRW4 | G protein‐coupled receptor | FPRL1 | rheumatoid arthritis | G protein-coupled receptor | Rheumatoid arthritis | RHEUMATOID-ARTHRITIS | RESPIRATORY BURST | POLYMORPHONUCLEAR LEUKOCYTES | INFLAMMATORY ARTHRITIS | IMMUNOLOGY | CELL BIOLOGY | SIGNAL-TRANSDUCTION | GRAM-NEGATIVE BACTERIA | PROTEIN-COUPLED RECEPTOR | NADPH-OXIDASE ACTIVATION | MET-VAL-MET | HEMATOLOGY | NF-KAPPA-B | Reactive Oxygen Species - metabolism | Recombinant Fusion Proteins - pharmacology | Serum Amyloid A Protein - pharmacology | Humans | Receptors, Formyl Peptide - antagonists & inhibitors | Receptors, Lipoxin - antagonists & inhibitors | NADPH Oxidases - metabolism | Receptors, Lipoxin - physiology | Recombinant Fusion Proteins - physiology | Peptide Fragments - pharmacology | Respiratory Burst - drug effects | Recombinant Fusion Proteins - antagonists & inhibitors | Transfection | Neutrophils - secretion | Receptors, Lipoxin - genetics | Receptors, G-Protein-Coupled - drug effects | Receptors, Formyl Peptide - physiology | Pertussis Toxin - pharmacology | Phosphatidylinositol 4,5-Diphosphate - physiology | Receptors, G-Protein-Coupled - physiology | Neutrophils - enzymology | Neutrophils - drug effects | Enzyme Activation - drug effects | Tumor Necrosis Factor-alpha - pharmacology | Gelsolin - pharmacology | Signal Transduction - drug effects | Calcium Signaling - drug effects | Lipopolysaccharides - pharmacology | HL-60 Cells | Signal Transduction - physiology | Oligopeptides - pharmacology | Organelles - metabolism | Receptors, Formyl Peptide - genetics | Serum Amyloid A Protein - physiology | Index Medicus | Peptide Fragments | Phosphatidylinositol 4,5-Diphosphate | Reactive Oxygen Species | Oligopeptides | Respiratory Burst | Innate immunity | Recombinant Fusion Proteins | Lipopolysaccharides | Life Sciences | Immunology | Receptors, Formyl Peptide | Gelsolin | Serum Amyloid A Protein | Calcium Signaling | Receptors, Lipoxin | Signal Transduction | Receptors, G-Protein-Coupled | Neutrophils | Pertussis Toxin | Tumor Necrosis Factor-alpha | Organelles | Enzyme Activation | NADPH Oxidase | MEDICIN OCH HÄLSOVETENSKAP | MEDICAL AND HEALTH SCIENCES
Journal Article
Journal Article