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Lancet, The, ISSN 0140-6736, 2014, Volume 383, Issue 9911, pp. 60 - 68
Summary Background Proprotein convertase subtilisin/kexin type 9 (PCSK9) binds to LDL receptors, leading to their degradation. Genetics studies have shown that... 
Internal Medicine | MEDICINE, GENERAL & INTERNAL | DENSITY-LIPOPROTEIN CHOLESTEROL | DOUBLE-STRANDED-RNA | PLASMA-CHOLESTEROL | METAANALYSIS | CARDIOVASCULAR-DISEASE | MONOCLONAL-ANTIBODY | HYPERCHOLESTEROLEMIA | STATINS | AMG 145 | ATORVASTATIN | Single-Blind Method | Serine Endopeptidases - biosynthesis | Humans | Middle Aged | RNA, Small Interfering - pharmacology | RNA, Small Interfering - adverse effects | Cholesterol, LDL - drug effects | Male | Healthy Volunteers | Proprotein Convertases - genetics | Dose-Response Relationship, Drug | Proprotein Convertases - biosynthesis | RNA Interference | Serine Endopeptidases - blood | Serine Endopeptidases - genetics | Adult | Cholesterol, LDL - blood | Female | Proprotein Convertases - blood | RNA, Small Interfering - administration & dosage | Genetic Therapy - adverse effects | Genetic Therapy - methods | Proprotein Convertase 9 | Enzymes | Research | Gene mutations | Properties | Gene expression | Identification and classification | Medical research | RNA | Low density lipoproteins | Anticholesteremic agents | Clinical trials | Aluminum compounds | Coronary heart disease | Cholesterol | Hypercholesterolemia | Analysis | Medicine, Experimental | Product development | Trans fatty acids | Blood proteins | Studies | Heart | Nanoparticles | Plasma | Nutrition research | Cardiovascular disease | Lipids | Mutation | Drug dosages | Statins
Journal Article
Nature Chemical Biology, ISSN 1552-4450, 03/2008, Volume 4, Issue 3, pp. 203 - 213
Newly replicated Plasmodium falciparum parasites escape from host erythrocytes through a tightly regulated process that is mediated by multiple classes of... 
CYSTEINE PROTEASE | PARASITOPHOROUS VACUOLE | VINYL SULFONES | STREPTOLYSIN-O | MEROZOITES | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL INVASION | I CATHEPSIN-C | SERINE-PROTEASE | SUBTILISIN-LIKE PROTEASE-1 | ANTIGEN | Cysteine Endopeptidases - chemistry | Plasmodium falciparum - enzymology | Parasitic Sensitivity Tests | Protozoan Proteins - antagonists & inhibitors | Stereoisomerism | Humans | Molecular Conformation | Subtilisins - chemistry | Plasmodium falciparum - drug effects | Cysteine Endopeptidases - drug effects | Sulfones - pharmacology | Serine Endopeptidases - drug effects | Dose-Response Relationship, Drug | Antigens, Protozoan - metabolism | Protease Inhibitors - pharmacology | Antigens, Protozoan - drug effects | Cysteine Endopeptidases - metabolism | Protozoan Proteins - metabolism | Isocoumarins - pharmacology | Sulfones - chemistry | Malaria, Falciparum - metabolism | Protozoan Proteins - chemistry | Subtilisins - metabolism | Plasmodium falciparum - physiology | Peptides - chemistry | Protease Inhibitors - chemistry | Serine Endopeptidases - chemistry | Subtilisins - antagonists & inhibitors | Peptides - pharmacology | Host-Parasite Interactions - drug effects | Malaria, Falciparum - parasitology | Animals | Small Molecule Libraries | Erythrocytes - metabolism | Serine Endopeptidases - metabolism | Erythrocytes - parasitology | Isocoumarins - chemistry | Biochemistry | Biomedical research | Parasites | Malaria | Proteases | Erythrocytes
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 12/2009, Volume 284, Issue 51, pp. 35412 - 35424
Heavy metals are known to generate reactive oxygen species that lead to the oxidation and fragmentation of proteins, which become toxic when accumulated in the... 
20S PROTEASOME | DEPENDENT PROTEOLYSIS | OXIDATIVE STRESS | PEA-PLANTS | UBIQUITIN-CONJUGATING ENZYMES | LENS EPITHELIAL-CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | OXIDIZED PROTEINS | 26S PROTEASOME | IMMUNOLOGICAL CHARACTERIZATION | LEUCINE AMINOPEPTIDASE | Gene Expression Regulation, Enzymologic - drug effects | Arabidopsis - enzymology | Serine Endopeptidases - biosynthesis | Muramidase - chemistry | Cadmium - pharmacology | Proteasome Endopeptidase Complex - chemistry | Serine Endopeptidases - chemistry | Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - chemistry | Enzyme Activation - drug effects | Proteasome Endopeptidase Complex - biosynthesis | Up-Regulation - drug effects | Gene Expression Regulation, Plant - drug effects | Animals | Arabidopsis Proteins - chemistry | Cattle | Arabidopsis Proteins - biosynthesis | Aminopeptidases - chemistry | Serum Albumin, Bovine - chemistry | Stress, Physiological - drug effects | Plant Leaves - enzymology | Aminopeptidases - biosynthesis | Dipeptidyl-Peptidases and Tripeptidyl-Peptidases - biosynthesis | Index Medicus | Up-Regulation | Cadmium | Arabidopsis | Aminopeptidases | Plant Leaves | Biochemistry, Molecular Biology | Stress, Physiological | Proteasome Endopeptidase Complex | Dipeptidyl-Peptidases and Tripeptidyl-Peptidases | Gene Expression Regulation, Enzymologic | Life Sciences | Arabidopsis Proteins | Muramidase | Serum Albumin, Bovine | Gene Expression Regulation, Plant | Serine Endopeptidases | Enzyme Activation | Protein Synthesis, Post-Translational Modification, and Degradation
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2016, Volume 291, Issue 7, pp. 3254 - 3267
Hepatitis C virus (HCV) relies on host lipids and lipid droplets for replication and morphogenesis. The accumulation of lipid droplets in infected hepatocytes... 
TARGET | liver injury | OXIDATIVE STRESS | SREBP | hepatitis virus | CHOLESTEROL | INTERLEUKIN-1-BETA | BIOCHEMISTRY & MOLECULAR BIOLOGY | lipid metabolism | NLRP3 inflammasome | DROPLETS | inflammation | PATHWAY | inflammasome | FATTY-ACID | CASPASES | INFECTION | EXPRESSION | Hepatitis C, Chronic - pathology | Inflammasomes - metabolism | Cytoskeletal Proteins - antagonists & inhibitors | Cytoskeletal Proteins - genetics | NLR Family, Pyrin Domain-Containing 3 Protein | Golgi Apparatus - drug effects | Humans | Hepatitis C, Chronic - virology | Non-alcoholic Fatty Liver Disease - etiology | Caspase 1 - metabolism | Host-Pathogen Interactions - drug effects | Intracellular Signaling Peptides and Proteins - metabolism | Protein Transport - drug effects | Sterol Regulatory Element Binding Protein 1 - agonists | RNA Interference | Hepacivirus - physiology | Sterol Regulatory Element Binding Protein 2 - metabolism | Endopeptidases - metabolism | Carrier Proteins - antagonists & inhibitors | Serine Endopeptidases - chemistry | Cysteine Proteinase Inhibitors - pharmacology | Cell Line, Tumor | Hepatocytes - virology | Sterol Regulatory Element Binding Protein 2 - agonists | Hepatitis C, Chronic - metabolism | Hepatitis C, Chronic - physiopathology | Hepatocytes - pathology | Golgi Apparatus - pathology | Hepatocytes - metabolism | Golgi Apparatus - virology | Caspase 1 - chemistry | Proteolysis - drug effects | Endopeptidases - chemistry | Inflammasomes - drug effects | Enzyme Induction - drug effects | Cytoskeletal Proteins - metabolism | Membrane Proteins - metabolism | Hepatocytes - drug effects | Sterol Regulatory Element Binding Protein 1 - metabolism | Hepacivirus - drug effects | Proprotein Convertases - metabolism | Proprotein Convertases - chemistry | Carrier Proteins - genetics | Carrier Proteins - metabolism | Caspase 1 - genetics | CARD Signaling Adaptor Proteins | Lipogenesis - drug effects | Golgi Apparatus - metabolism | Serine Endopeptidases - metabolism | Microbiology
Journal Article
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 06/2016, Volume 121, Issue 6, pp. 614 - 618
A rhizosphere strain of the bacterium Stenotrophomonas maltophilia N4 secretes the serine protease PN4, whose molecular mass is approximately 42 kDa. The... 
Stenotrophomonas maltophilia | Serine protease | Nematocidal activity | Biocontrol | FOOD SCIENCE & TECHNOLOGY | BREVIBACILLUS-LATEROSPORUS G4 | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | NEMATODES | ENZYMES | PURIFICATION | PATHOGENIC FACTOR | SERINE-PROTEASE | CHITINASE | BIOLOGICAL-CONTROL | BACILLUS | STRAIN | Temperature | Molecular Weight | Bacterial Proteins - chemistry | Molecular Sequence Data | Serine Endopeptidases - pharmacology | Substrate Specificity | Endopeptidases - chemistry | Stenotrophomonas maltophilia - genetics | Cloning, Molecular | Serine Endopeptidases - genetics | Protein Domains | Antinematodal Agents - metabolism | Antinematodal Agents - pharmacology | Rhabditida - drug effects | Amino Acid Sequence | Endopeptidases - metabolism | Bacterial Proteins - genetics | Enzyme Stability | Serine Endopeptidases - chemistry | Antinematodal Agents - chemistry | Bacterial Proteins - pharmacology | Animals | Caenorhabditis elegans - drug effects | Endopeptidases - genetics | Bacterial Proteins - metabolism | Serine Endopeptidases - metabolism | Endopeptidases - pharmacology | Hydrogen-Ion Concentration | Stenotrophomonas maltophilia - enzymology | Keratin | Protease inhibitors | Casein | Cloning | Genes | Thrombin | Amino acids | Genetic aspects | Enzymes | Biological control | Albumin | Pests | Biocides | Zinc compounds
Journal Article
The New England Journal of Medicine, ISSN 0028-4793, 03/2012, Volume 366, Issue 12, pp. 1108 - 1118
A monoclonal antibody to PCSK9 was studied in two single-dose trials in healthy volunteers and one multiple-dose trial in patients with familial or nonfamilial... 
POPULATION | MEDICINE, GENERAL & INTERNAL | STATIN | MICE | MUTATIONS | Proprotein Convertases - antagonists & inhibitors | Injections, Intravenous | Heptanoic Acids - therapeutic use | Humans | Middle Aged | Antibodies, Monoclonal - adverse effects | Male | Hypercholesterolemia - drug therapy | Dose-Response Relationship, Drug | Injections, Subcutaneous | Serine Endopeptidases - immunology | Adult | Cholesterol, LDL - blood | Female | Hyperlipoproteinemia Type II - drug therapy | Drug Therapy, Combination | Pyrroles - therapeutic use | Proprotein Convertases - metabolism | Receptors, LDL - metabolism | Lipoproteins - blood | Anticholesteremic Agents - adverse effects | Proprotein Convertases - immunology | Hyperlipoproteinemia Type II - metabolism | Atorvastatin Calcium | Anticholesteremic Agents - therapeutic use | Antibodies, Monoclonal - administration & dosage | Anticholesteremic Agents - administration & dosage | Least-Squares Analysis | Serine Endopeptidases - metabolism | Receptors, LDL - drug effects | Hypercholesterolemia - metabolism | Proprotein Convertase 9 | Drugs | Dose-response relationship (Biochemistry) | Hypercholesterolemia | Monoclonal antibodies | Cholesterol, LDL | Dosage and administration | Product/Service Evaluations | Research | Drug therapy | Health aspects | Studies | Lipoproteins (low density) | Kexin | Serine | Atorvastatin | Cardiovascular disease | Subtilisin | Low density lipoprotein | Cholesterol
Journal Article
Neuron, ISSN 0896-6273, 10/2012, Volume 76, Issue 2, pp. 353 - 369
Birthdate-dependent neuronal layering is fundamental to neocortical functions. The extracellular protein Reelin is essential for the establishment of the... 
Integrin alpha5beta1 - genetics | Embryo, Mammalian | Humans | Cell Adhesion Molecules, Neuronal - drug effects | Green Fluorescent Proteins - genetics | Cell Movement - genetics | Cell Movement - physiology | Mice, Neurologic Mutants | Serine Endopeptidases - drug effects | Neurons - physiology | Serine Endopeptidases - genetics | Female | Somatosensory Cortex - cytology | Cell Adhesion Molecules, Neuronal - metabolism | Proto-Oncogene Proteins c-crk - metabolism | Neurons - drug effects | Extracellular Matrix Proteins - metabolism | rap1 GTP-Binding Proteins - metabolism | Cell Adhesion - genetics | Gene Expression Regulation - genetics | Extracellular Matrix Proteins - genetics | Gene Expression Regulation - physiology | Electroporation | Mice, Transgenic | Signal Transduction - genetics | Cell Adhesion - drug effects | Mutation - genetics | Nerve Tissue Proteins - drug effects | Nerve Tissue Proteins - genetics | Cell Adhesion Molecules, Neuronal - genetics | Extracellular Matrix Proteins - drug effects | Mice, Inbred ICR | Nuclear Proteins | Gene Expression Regulation - drug effects | Nerve Tissue Proteins - metabolism | Pregnancy | Cell Movement - drug effects | Adaptor Proteins, Signal Transducing | Animals | Analysis of Variance | Cell Adhesion - physiology | Signal Transduction - physiology | Mice | Serine Endopeptidases - metabolism | Cell Line, Transformed | Integrin alpha5beta1 - metabolism
Journal Article
American Journal of Respiratory Cell and Molecular Biology, ISSN 1044-1549, 03/2016, Volume 54, Issue 3, pp. 359 - 369
Proteases are important regulators of pulmonary remodeling and airway inflammation. Recently, we have characterized the enzyme prolyl endopeptidase (PE), a... 
Cystic fibrosis | Exosome | Protease | Pulmonary | Toll-like receptor 4 | NEUTROPHILIC INFLAMMATION | LUNG | VESICLES | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRAFFICKING | pulmonary | MICROVESICLES | CELL BIOLOGY | protease | BIOGENESIS | RESPIRATORY SYSTEM | cystic fibrosis | PROTEIN SECRETION | EXTRACELLULAR-MATRIX DEGRADATION | CYSTIC-FIBROSIS | CELL-DERIVED EXOSOMES | exosome | Exosomes - drug effects | Bronchi - microbiology | Pseudomonas aeruginosa - isolation & purification | Bronchi - enzymology | Cystic Fibrosis - enzymology | Epithelial Cells - drug effects | Humans | Male | Case-Control Studies | Bronchi - drug effects | Dose-Response Relationship, Drug | Young Adult | Transfection | RNA Interference | Mitochondrial Proteins - metabolism | Toll-Like Receptor 4 - agonists | Adult | Female | Cell Line | Signal Transduction | Cystic Fibrosis - microbiology | Toll-Like Receptor 4 - genetics | Toll-Like Receptor 4 - metabolism | Mice, Inbred C3H | Mice, Knockout | Exosomes - microbiology | Animals | Cystic Fibrosis - genetics | Epithelial Cells - microbiology | Epithelial Cells - enzymology | Lipopolysaccharides - pharmacology | Exosomes - enzymology | Serine Endopeptidases - metabolism | Proteins | Signal transduction | Enzymes | Immunoglobulins | Laboratories | Lung diseases | Colleges & universities | Homeostasis | Ligands | Pattern recognition | Communication
Journal Article
Circulation, ISSN 0009-7322, 12/2002, Volume 106, Issue 23, pp. 2973 - 2979
Background-Erythropoietin (EPO) is a critical regulator for the proliferation of immature erythroid precursors, but its role as a potential cytoprotectant in... 
Cytochrome c | Proteins, mitochondrial | Proteins, proto-oncogene | Cysteine endopeptidases | Apoptosis | CARDIAC & CARDIOVASCULAR SYSTEMS | IN-VIVO EVIDENCE | INJURY | apoptosis | PROGRAMMED CELL-DEATH | proteins, proto-oncogene | cysteine endopeptidases | ENDOTHELIAL-CELLS | NEURONS | PERIPHERAL VASCULAR DISEASE | cytochrome c | HEMATOLOGY | proteins, mitochondrial | BRAIN | ERYTHROID PROGENITORS | Endothelium, Vascular - cytology | Erythropoietin - pharmacology | Mitochondria - enzymology | Cell Hypoxia - physiology | Microcirculation - metabolism | Intracellular Membranes - physiology | Apoptosis - drug effects | Endothelium, Vascular - drug effects | Cytoprotection - physiology | Cysteine Endopeptidases - drug effects | Microcirculation - drug effects | Brain - blood supply | Cysteine Endopeptidases - metabolism | Cytoprotection - drug effects | Cell Membrane - metabolism | Proto-Oncogene Proteins | DNA Fragmentation - drug effects | Mitochondria - chemistry | Cell Membrane - drug effects | Protein-Serine-Threonine Kinases - metabolism | Membrane Potentials - drug effects | Cell Survival - drug effects | Phosphatidylserines - metabolism | Cells, Cultured | Enzyme Inhibitors - pharmacology | Rats | Mitochondria - drug effects | Enzyme Activation - drug effects | Rats, Sprague-Dawley | Antibodies - pharmacology | Proto-Oncogene Proteins c-akt | Microcirculation - cytology | Animals | Signal Transduction - drug effects | Endothelium, Vascular - metabolism | Erythropoietin - antagonists & inhibitors | Intracellular Membranes - drug effects
Journal Article
Journal of Cell Science, ISSN 0021-9533, 2016, Volume 129, Issue 20, pp. 3792 - 3802
Journal Article
Journal Article
American Journal of Physiology - Lung Cellular and Molecular Physiology, ISSN 1040-0605, 02/2011, Volume 300, Issue 2, pp. L255 - L265
Journal Article