Diabetologia, ISSN 0012-186X, 8/2005, Volume 48, Issue 8, pp. 1523 - 1533
Alpha1-proteinase inhibitor (α1-PI) has been considered a key player in inflammatory processes. In humans, the main production site of α1-PI is the liver, but...
Medicine | Human islets | Reverse haemolytic plaque assay | IL-1β | Oncostatin M | α1-Proteinase inhibitor | RHPA | oncostatin M | ALPHA-PROTEINASE INHIBITOR | INSULIN-SECRETION | alpha 1-PI | IL-1 beta | PLASMA PROTEINASE-INHIBITORS | ACUTE-PHASE RESPONSE | ALPHA-ACID GLYCOPROTEIN | IN-VITRO | reverse haemolytic plaque assay | EPITHELIAL-CELLS | human islets | ENDOCRINOLOGY & METABOLISM | ALPHA-1-PROTEINASE INHIBITOR | BETA-CELL | INFLAMMATORY CYTOKINES | alpha1-proteinase inhibitor | Immunohistochemistry | Islets of Langerhans - drug effects | alpha 1-Antitrypsin - genetics | Enzyme-Linked Immunosorbent Assay | Anti-Inflammatory Agents - pharmacology | Cell Separation | Humans | Cells, Cultured | 1-Methyl-3-isobutylxanthine - pharmacology | Blotting, Western | Microscopy, Immunoelectron | Interleukin-1 - pharmacology | Antibodies - pharmacology | Dexamethasone - pharmacology | alpha 1-Antitrypsin - biosynthesis | Islets of Langerhans - metabolism | Fluorescent Antibody Technique | Hemolytic Plaque Technique | Cytokines - pharmacology | Medical colleges | Pancreatic beta cells | Cytokines | Glucagon | Alpha 1-antitrypsin | Electron microscopy | Enzyme-linked immunosorbent assay
Medicine | Human islets | Reverse haemolytic plaque assay | IL-1β | Oncostatin M | α1-Proteinase inhibitor | RHPA | oncostatin M | ALPHA-PROTEINASE INHIBITOR | INSULIN-SECRETION | alpha 1-PI | IL-1 beta | PLASMA PROTEINASE-INHIBITORS | ACUTE-PHASE RESPONSE | ALPHA-ACID GLYCOPROTEIN | IN-VITRO | reverse haemolytic plaque assay | EPITHELIAL-CELLS | human islets | ENDOCRINOLOGY & METABOLISM | ALPHA-1-PROTEINASE INHIBITOR | BETA-CELL | INFLAMMATORY CYTOKINES | alpha1-proteinase inhibitor | Immunohistochemistry | Islets of Langerhans - drug effects | alpha 1-Antitrypsin - genetics | Enzyme-Linked Immunosorbent Assay | Anti-Inflammatory Agents - pharmacology | Cell Separation | Humans | Cells, Cultured | 1-Methyl-3-isobutylxanthine - pharmacology | Blotting, Western | Microscopy, Immunoelectron | Interleukin-1 - pharmacology | Antibodies - pharmacology | Dexamethasone - pharmacology | alpha 1-Antitrypsin - biosynthesis | Islets of Langerhans - metabolism | Fluorescent Antibody Technique | Hemolytic Plaque Technique | Cytokines - pharmacology | Medical colleges | Pancreatic beta cells | Cytokines | Glucagon | Alpha 1-antitrypsin | Electron microscopy | Enzyme-linked immunosorbent assay
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 06/2010, Volume 285, Issue 26, pp. 20399 - 20409
The serpin ZPI is a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa) despite having an unfavorable P1 Tyr. PZ accelerates the...
PROTHROMBIN | COMPLEX | AMINO-ACID-SEQUENCE | TICK ANTICOAGULANT PEPTIDE | ACTIVE-SITE | ALPHA-PROTEINASE INHIBITOR | SUBSTRATE | BIOCHEMISTRY & MOLECULAR BIOLOGY | COAGULATION FACTOR-XA | EXOSITE | BINDING | Factor Xa - chemistry | Calcium - metabolism | Glutamic Acid - genetics | Humans | Crystallography, X-Ray | Blood Proteins - metabolism | Serpins - chemistry | Calcium - chemistry | Cysteine - genetics | Blood Proteins - genetics | Light | Cell Membrane - metabolism | Cysteine - metabolism | Scattering, Radiation | Phospholipids - metabolism | Tyrosine - chemistry | Protein Structure, Tertiary | Serpins - genetics | Serpins - metabolism | Models, Molecular | Phospholipids - chemistry | Binding Sites - genetics | Blood Proteins - chemistry | Cysteine - chemistry | Factor Xa - metabolism | Tyrosine - metabolism | Protein Binding | Protein Conformation | Glutamic Acid - metabolism | Kinetics | Mutation | Glutamic Acid - chemistry | Tyrosine - genetics | Index Medicus | MUTAGENESIS | SPECIFICITY | BASIC BIOLOGICAL SCIENCES | ACYLATION | MEMBRANES | PHOSPHOLIPIDS | CRYSTALLOGRAPHY | SIMULATION | 60 APPLIED LIFE SCIENCES | CONFORMATIONAL CHANGES | ACCELERATION | TYROSINE | MUTATIONS | PROTEINS | RESIDUES | Protein Structure and Folding | Serpin | Protease | X-ray Crystallography | Coagulation Factors | Enzymology | Protease Inhibitor | Protein-Protein Interactions
PROTHROMBIN | COMPLEX | AMINO-ACID-SEQUENCE | TICK ANTICOAGULANT PEPTIDE | ACTIVE-SITE | ALPHA-PROTEINASE INHIBITOR | SUBSTRATE | BIOCHEMISTRY & MOLECULAR BIOLOGY | COAGULATION FACTOR-XA | EXOSITE | BINDING | Factor Xa - chemistry | Calcium - metabolism | Glutamic Acid - genetics | Humans | Crystallography, X-Ray | Blood Proteins - metabolism | Serpins - chemistry | Calcium - chemistry | Cysteine - genetics | Blood Proteins - genetics | Light | Cell Membrane - metabolism | Cysteine - metabolism | Scattering, Radiation | Phospholipids - metabolism | Tyrosine - chemistry | Protein Structure, Tertiary | Serpins - genetics | Serpins - metabolism | Models, Molecular | Phospholipids - chemistry | Binding Sites - genetics | Blood Proteins - chemistry | Cysteine - chemistry | Factor Xa - metabolism | Tyrosine - metabolism | Protein Binding | Protein Conformation | Glutamic Acid - metabolism | Kinetics | Mutation | Glutamic Acid - chemistry | Tyrosine - genetics | Index Medicus | MUTAGENESIS | SPECIFICITY | BASIC BIOLOGICAL SCIENCES | ACYLATION | MEMBRANES | PHOSPHOLIPIDS | CRYSTALLOGRAPHY | SIMULATION | 60 APPLIED LIFE SCIENCES | CONFORMATIONAL CHANGES | ACCELERATION | TYROSINE | MUTATIONS | PROTEINS | RESIDUES | Protein Structure and Folding | Serpin | Protease | X-ray Crystallography | Coagulation Factors | Enzymology | Protease Inhibitor | Protein-Protein Interactions
Journal Article
Food Chemistry, ISSN 0308-8146, 02/2016, Volume 192, pp. 1090 - 1097
Purification of proteinase inhibitor from common carp ( ) sarcoplasmic proteins resulted in 2.8% yield with purification fold of 111. Two inhibitors, namely...
Common carp | Sarcoplasmic proteins | Autolytic degradation | Proteinase inhibitor | Glycoprotein | ALPHA-PROTEINASE INHIBITOR | SEMINAL PLASMA | FOOD SCIENCE & TECHNOLOGY | HEAT DENATURATION | SKELETAL-MUSCLE | NUTRITION & DIETETICS | PURIFICATION | ALPHA-1-ANTITRYPSIN | ALPHA-1-PROTEINASE INHIBITOR | MAJOR PLASMA SERPIN | CHEMISTRY, APPLIED | TRYPSIN-INHIBITOR | CARBOHYDRATE MOIETY | alpha 1-Antitrypsin - chemistry | Animals | Molecular Weight | Drug Stability | Electrophoresis, Polyacrylamide Gel | alpha 1-Antitrypsin - pharmacology | Carps | Hot Temperature | Sarcoplasmic Reticulum - chemistry | alpha 1-Antitrypsin - analysis | Trypsin Inhibitors | Glycoproteins | Chemical properties
Common carp | Sarcoplasmic proteins | Autolytic degradation | Proteinase inhibitor | Glycoprotein | ALPHA-PROTEINASE INHIBITOR | SEMINAL PLASMA | FOOD SCIENCE & TECHNOLOGY | HEAT DENATURATION | SKELETAL-MUSCLE | NUTRITION & DIETETICS | PURIFICATION | ALPHA-1-ANTITRYPSIN | ALPHA-1-PROTEINASE INHIBITOR | MAJOR PLASMA SERPIN | CHEMISTRY, APPLIED | TRYPSIN-INHIBITOR | CARBOHYDRATE MOIETY | alpha 1-Antitrypsin - chemistry | Animals | Molecular Weight | Drug Stability | Electrophoresis, Polyacrylamide Gel | alpha 1-Antitrypsin - pharmacology | Carps | Hot Temperature | Sarcoplasmic Reticulum - chemistry | alpha 1-Antitrypsin - analysis | Trypsin Inhibitors | Glycoproteins | Chemical properties
Journal Article
BIOSCIENCE REPORTS, ISSN 0144-8463, 07/2019, Volume 39
Although wasting marmoset syndrome (WMS) is one of the biggest problems facing captive marmoset colonies, the mechanisms underlying its pathogenesis remain...
LINKED-IMMUNOSORBENT-ASSAY | ALPHA-PROTEINASE INHIBITOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | PURIFICATION | FECES | ANALYTICAL VALIDATION | CALPROTECTIN | SERUM | GENERATION | REFERENCE VALUES | RADIOIMMUNOASSAY | CELL BIOLOGY
LINKED-IMMUNOSORBENT-ASSAY | ALPHA-PROTEINASE INHIBITOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | PURIFICATION | FECES | ANALYTICAL VALIDATION | CALPROTECTIN | SERUM | GENERATION | REFERENCE VALUES | RADIOIMMUNOASSAY | CELL BIOLOGY
Journal Article
PLoS ONE, ISSN 1932-6203, 04/2012, Volume 7, Issue 4, p. e35108
Exposure to oxidant air pollution is associated with increased respiratory morbidities and susceptibility to infections. Ozone is a commonly encountered...
OXIDATIVE STRESS | SECRETORY LEUKOPROTEASE INHIBITOR | SOUTHWEST MEXICO-CITY | BRONCHIAL EPITHELIAL-CELLS | ALPHA-PROTEINASE INHIBITOR | BIOLOGY | TRANSMEMBRANE SERINE PROTEASES | GENE-EXPRESSION | CIGARETTE-SMOKE | INFLAMMATORY RESPONSE | VIRAL-INFECTION | Ozone - adverse effects | Humans | Nasal Mucosa - enzymology | Cells, Cultured | Peptide Hydrolases - secretion | Protease Inhibitors - metabolism | Secretory Leukocyte Peptidase Inhibitor - analysis | Antioxidants - pharmacology | Nasal Mucosa - secretion | Influenza, Human - chemically induced | Virus Internalization | Peptide Hydrolases - biosynthesis | Virus Replication | Influenza A virus - pathogenicity | Adult | Air Pollutants - adverse effects | Secretory Leukocyte Peptidase Inhibitor - antagonists & inhibitors | Nasal Mucosa - drug effects | Photochemical smog | Swine influenza | Disease susceptibility | B cells | Virus diseases | Infection | Antioxidants | Influenza viruses | Trypsin | Protease inhibitors | Proteases | Lectins | Health aspects | Pandemics | Epithelial cells | Serine | Viruses | Infections | Respiratory tract | Proteolysis | Protease | Infectivity | Hemagglutinins | Cleavage | Influenza A | Chronic obstructive pulmonary disease | Pollutants | HA protein | Outdoor air quality | Ozone | Proteinase inhibitors | Exposure | Epithelium | Membrane proteins | White blood cells | Swine flu | Influenza | Replication | Air pollution | Viral infections | Leukocytes | Proteins | Oxidants | Data processing | Morbidity | Serine proteinase | pandemics
OXIDATIVE STRESS | SECRETORY LEUKOPROTEASE INHIBITOR | SOUTHWEST MEXICO-CITY | BRONCHIAL EPITHELIAL-CELLS | ALPHA-PROTEINASE INHIBITOR | BIOLOGY | TRANSMEMBRANE SERINE PROTEASES | GENE-EXPRESSION | CIGARETTE-SMOKE | INFLAMMATORY RESPONSE | VIRAL-INFECTION | Ozone - adverse effects | Humans | Nasal Mucosa - enzymology | Cells, Cultured | Peptide Hydrolases - secretion | Protease Inhibitors - metabolism | Secretory Leukocyte Peptidase Inhibitor - analysis | Antioxidants - pharmacology | Nasal Mucosa - secretion | Influenza, Human - chemically induced | Virus Internalization | Peptide Hydrolases - biosynthesis | Virus Replication | Influenza A virus - pathogenicity | Adult | Air Pollutants - adverse effects | Secretory Leukocyte Peptidase Inhibitor - antagonists & inhibitors | Nasal Mucosa - drug effects | Photochemical smog | Swine influenza | Disease susceptibility | B cells | Virus diseases | Infection | Antioxidants | Influenza viruses | Trypsin | Protease inhibitors | Proteases | Lectins | Health aspects | Pandemics | Epithelial cells | Serine | Viruses | Infections | Respiratory tract | Proteolysis | Protease | Infectivity | Hemagglutinins | Cleavage | Influenza A | Chronic obstructive pulmonary disease | Pollutants | HA protein | Outdoor air quality | Ozone | Proteinase inhibitors | Exposure | Epithelium | Membrane proteins | White blood cells | Swine flu | Influenza | Replication | Air pollution | Viral infections | Leukocytes | Proteins | Oxidants | Data processing | Morbidity | Serine proteinase | pandemics
Journal Article
Veterinary Clinical Pathology, ISSN 0275-6382, 06/2013, Volume 42, Issue 2, pp. 190 - 195
Background A chronic loss of canine 1-proteinase inhibitor (c1-PI) into the gastrointestinal (GI) tract could change the systemic proteinase-proteinase...
LONG-TERM | 1-PI | PROTEIN | ALPHA-PROTEINASE INHIBITOR | canine | DEFICIENCY | immunoassay | PANNICULITIS | ALPHA-ANTITRYPSIN CONCENTRATION | DISEASE | BIOLOGICAL VARIATION | biologic variation | ALPHA-1-ANTITRYPSIN | α1‐PI | Immunoassay | PI | Biologic variation | Canine | VETERINARY SCIENCES | Reproducibility of Results | Iodine Radioisotopes | alpha 1-Antitrypsin - blood | Male | Reference Values | Dogs - blood | alpha 1-Antitrypsin - standards | Dog Diseases - blood | Animals | Gastrointestinal Diseases - veterinary | Dog Diseases - enzymology | Gastrointestinal Diseases - blood | Radioimmunoassay - standards | Female | Radioimmunoassay - veterinary
LONG-TERM | 1-PI | PROTEIN | ALPHA-PROTEINASE INHIBITOR | canine | DEFICIENCY | immunoassay | PANNICULITIS | ALPHA-ANTITRYPSIN CONCENTRATION | DISEASE | BIOLOGICAL VARIATION | biologic variation | ALPHA-1-ANTITRYPSIN | α1‐PI | Immunoassay | PI | Biologic variation | Canine | VETERINARY SCIENCES | Reproducibility of Results | Iodine Radioisotopes | alpha 1-Antitrypsin - blood | Male | Reference Values | Dogs - blood | alpha 1-Antitrypsin - standards | Dog Diseases - blood | Animals | Gastrointestinal Diseases - veterinary | Dog Diseases - enzymology | Gastrointestinal Diseases - blood | Radioimmunoassay - standards | Female | Radioimmunoassay - veterinary
Journal Article
Journal of Biotechnology, ISSN 0168-1656, 08/2015, Volume 208, pp. 54 - 62
Serpins are a widely distributed family of serine proteases. A key determinant of their specificity is the reactive centre loop (RCL), a surface motif of ∼20...
Fluorescence-activated cell sorting | Expression library screening | Microtiter plate assays | Serpins | Alpha-1-proteinase inhibitor | Thrombin | Bacteria | Recombinant proteins | COMPLEX | MECHANISM | ALPHA-PROTEINASE INHIBITOR | HEPARIN-COFACTOR-II | PHAGE DISPLAY | SERPIN STRUCTURE | REACTIVE CENTER LOOP | PLASMINOGEN-ACTIVATOR | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | ALPHA-1-ANTITRYPSIN | alpha 1-Antitrypsin - genetics | Gene Library | Protein Structure, Secondary | Humans | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Mutation, Missense | Recombinant Proteins - biosynthesis | alpha 1-Antitrypsin - chemistry | alpha 1-Antitrypsin - biosynthesis | Escherichia coli - genetics | Thrombin - chemistry | Escherichia coli - metabolism | HEK293 Cells | Amino Acid Substitution | Libraries | Protease inhibitors | Comparative analysis | Residues | Inhibitors | Protease | Amino acids | API
Fluorescence-activated cell sorting | Expression library screening | Microtiter plate assays | Serpins | Alpha-1-proteinase inhibitor | Thrombin | Bacteria | Recombinant proteins | COMPLEX | MECHANISM | ALPHA-PROTEINASE INHIBITOR | HEPARIN-COFACTOR-II | PHAGE DISPLAY | SERPIN STRUCTURE | REACTIVE CENTER LOOP | PLASMINOGEN-ACTIVATOR | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | ALPHA-1-ANTITRYPSIN | alpha 1-Antitrypsin - genetics | Gene Library | Protein Structure, Secondary | Humans | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Mutation, Missense | Recombinant Proteins - biosynthesis | alpha 1-Antitrypsin - chemistry | alpha 1-Antitrypsin - biosynthesis | Escherichia coli - genetics | Thrombin - chemistry | Escherichia coli - metabolism | HEK293 Cells | Amino Acid Substitution | Libraries | Protease inhibitors | Comparative analysis | Residues | Inhibitors | Protease | Amino acids | API
Journal Article
RESPIRATORY MEDICINE, ISSN 0954-6111, 04/2015, Volume 109, Issue 4, pp. 490 - 499
Background: Alpha(1)-antitrypsin deficiency (AATD) is an underdiagnosed genetic disorder that results in early-onset emphysema due to low serum levels of...
DIAGNOSIS | CARDIAC & CARDIOVASCULAR SYSTEMS | Alpha-proteinase inhibitor | LUNG-FUNCTION | Alpha-antitrypsin deficiency | SPARTA | CT densitometry | RESPIRATORY SYSTEM | EMPHYSEMA | REPLACEMENT THERAPY | Chronic obstructive pulmonary disease | Prolastin-C | ALPHA-1-ANTITRYPSIN DEFICIENCY | COPD
DIAGNOSIS | CARDIAC & CARDIOVASCULAR SYSTEMS | Alpha-proteinase inhibitor | LUNG-FUNCTION | Alpha-antitrypsin deficiency | SPARTA | CT densitometry | RESPIRATORY SYSTEM | EMPHYSEMA | REPLACEMENT THERAPY | Chronic obstructive pulmonary disease | Prolastin-C | ALPHA-1-ANTITRYPSIN DEFICIENCY | COPD
Journal Article
Applied Biochemistry and Biotechnology, ISSN 0273-2289, 5/2016, Volume 179, Issue 2, pp. 220 - 236
Expression of recombinant therapeutic proteins in transgenic plants has a tremendous impact on safe and economical production of biomolecules for...
Biochemistry, general | Biotechnology | Chemistry | Protein purification | Transgenic tomato plants | Downstream processing | Heterologous protein expression | Recombinant therapeutic proteins | Molecular pharming | Serine proteinase inhibitor | BIOCHEMISTRY & MOLECULAR BIOLOGY | MONOCLONAL-ANTIBODY | HUMAN ALPHA-PROTEINASE INHIBITOR | FUNCTIONAL HUMAN ALPHA-1-ANTITRYPSIN | ENHANCED STABILITY | EXTRACTION | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | CELL SUSPENSION-CULTURES | BIOLOGICAL-ACTIVITY | TOMATO PLANTS | SEED | EXPRESSION | alpha 1-Antitrypsin - isolation & purification | alpha 1-Antitrypsin - genetics | Plants, Genetically Modified - genetics | Humans | Plants, Genetically Modified - chemistry | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Recombinant Proteins - biosynthesis | Recombinant Proteins - isolation & purification | alpha 1-Antitrypsin - chemistry | Chromatography, Affinity | alpha 1-Antitrypsin - biosynthesis | Lycopersicon esculentum - genetics | Protein Conformation | Lycopersicon esculentum - chemistry | Genetically modified plants | Protease inhibitors | Serine | Thrombin | Genetic engineering | Chemical properties | Plants | Precipitation (Meteorology) | Recombinant proteins | Chromatography | Enzymes | Protein expression | Transgenic plants
Biochemistry, general | Biotechnology | Chemistry | Protein purification | Transgenic tomato plants | Downstream processing | Heterologous protein expression | Recombinant therapeutic proteins | Molecular pharming | Serine proteinase inhibitor | BIOCHEMISTRY & MOLECULAR BIOLOGY | MONOCLONAL-ANTIBODY | HUMAN ALPHA-PROTEINASE INHIBITOR | FUNCTIONAL HUMAN ALPHA-1-ANTITRYPSIN | ENHANCED STABILITY | EXTRACTION | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | CELL SUSPENSION-CULTURES | BIOLOGICAL-ACTIVITY | TOMATO PLANTS | SEED | EXPRESSION | alpha 1-Antitrypsin - isolation & purification | alpha 1-Antitrypsin - genetics | Plants, Genetically Modified - genetics | Humans | Plants, Genetically Modified - chemistry | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Recombinant Proteins - biosynthesis | Recombinant Proteins - isolation & purification | alpha 1-Antitrypsin - chemistry | Chromatography, Affinity | alpha 1-Antitrypsin - biosynthesis | Lycopersicon esculentum - genetics | Protein Conformation | Lycopersicon esculentum - chemistry | Genetically modified plants | Protease inhibitors | Serine | Thrombin | Genetic engineering | Chemical properties | Plants | Precipitation (Meteorology) | Recombinant proteins | Chromatography | Enzymes | Protein expression | Transgenic plants
Journal Article
RESEARCH IN VETERINARY SCIENCE, ISSN 0034-5288, 04/2015, Volume 99, pp. 17 - 22
Fecal alphal-proteinase inhibitor (alpha(1)-PI) concentration has been to diagnose enteric protein loss in dogs and cats. Chronic lymphocytic enteritis is...
PROTEINASE-INHIBITORS | Purification | BIOMEDICAL-RESEARCH | LINKED-IMMUNOSORBENT-ASSAY | ANALYTICAL VALIDATION | TRYPSIN-INHIBITORS | SERUM | STATISTICAL-MODEL | Characterization | PLASMA | Common marmoset | ALPHA-1-ANTITRYPSIN | VETERINARY SCIENCES | ALPHA-1-PROTEINASE INHIBITOR | alpha-proteinase inhibitor
PROTEINASE-INHIBITORS | Purification | BIOMEDICAL-RESEARCH | LINKED-IMMUNOSORBENT-ASSAY | ANALYTICAL VALIDATION | TRYPSIN-INHIBITORS | SERUM | STATISTICAL-MODEL | Characterization | PLASMA | Common marmoset | ALPHA-1-ANTITRYPSIN | VETERINARY SCIENCES | ALPHA-1-PROTEINASE INHIBITOR | alpha-proteinase inhibitor
Journal Article
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 6, p. e21525
Heparin has been shown to regulate human neutrophil elastase (HNE) activity. We have assessed the regulatory effect of heparin on Tissue Inhibitor of...
SULFATE PROTEOGLYCANS | MATRIX METALLOPROTEINASES | SUBSTRATE-SPECIFICITY | SECRETORY LEUKOPROTEASE INHIBITOR | PORCINE PANCREATIC ELASTASE | SERINE PROTEASES | TERMINAL DOMAIN | ALPHA-PROTEINASE INHIBITOR | BIOLOGY | HUMAN-LEUKOCYTE ELASTASE | CATHEPSIN-G | Leukocyte Elastase - metabolism | Catalytic Domain | Hydrolysis - drug effects | Leukocyte Elastase - pharmacology | Humans | Fluorescent Dyes - metabolism | Models, Molecular | Up-Regulation - drug effects | Tissue Inhibitor of Metalloproteinase-1 - metabolism | Peptides - metabolism | Substrate Specificity - drug effects | Protein Processing, Post-Translational - drug effects | Hydrogen-Ion Concentration - drug effects | Fluorescence Resonance Energy Transfer | Kinetics | Heparin - pharmacology | Hydrolysis | Fluorescence | Heparin | Peptides | Proteases | Acylation | Embolisms | Biochemistry | Tissue inhibitor of metalloproteinase 1 | pH effects | Hemorrhage | Molecular weight | Molecular docking | Degradation | Ischemia | Reaction kinetics | Extracellular matrix | Cleavage | Physiology | Elastase | Fluorescence resonance energy transfer | Recombinant | Heparan sulfate | Enzymes | Stroke | Neutrophils | Thrombosis | Steady state | Inhibitors | Collaboration | Lag phase | Deacylation | Clinical medicine | Potassium
SULFATE PROTEOGLYCANS | MATRIX METALLOPROTEINASES | SUBSTRATE-SPECIFICITY | SECRETORY LEUKOPROTEASE INHIBITOR | PORCINE PANCREATIC ELASTASE | SERINE PROTEASES | TERMINAL DOMAIN | ALPHA-PROTEINASE INHIBITOR | BIOLOGY | HUMAN-LEUKOCYTE ELASTASE | CATHEPSIN-G | Leukocyte Elastase - metabolism | Catalytic Domain | Hydrolysis - drug effects | Leukocyte Elastase - pharmacology | Humans | Fluorescent Dyes - metabolism | Models, Molecular | Up-Regulation - drug effects | Tissue Inhibitor of Metalloproteinase-1 - metabolism | Peptides - metabolism | Substrate Specificity - drug effects | Protein Processing, Post-Translational - drug effects | Hydrogen-Ion Concentration - drug effects | Fluorescence Resonance Energy Transfer | Kinetics | Heparin - pharmacology | Hydrolysis | Fluorescence | Heparin | Peptides | Proteases | Acylation | Embolisms | Biochemistry | Tissue inhibitor of metalloproteinase 1 | pH effects | Hemorrhage | Molecular weight | Molecular docking | Degradation | Ischemia | Reaction kinetics | Extracellular matrix | Cleavage | Physiology | Elastase | Fluorescence resonance energy transfer | Recombinant | Heparan sulfate | Enzymes | Stroke | Neutrophils | Thrombosis | Steady state | Inhibitors | Collaboration | Lag phase | Deacylation | Clinical medicine | Potassium
Journal Article
THROMBOSIS AND HAEMOSTASIS, ISSN 0340-6245, 05/2012, Volume 107, Issue 5, pp. 972 - 984
The variant serpin alpha(1)-PI M358R inhibits thrombin and other proteases such as activated protein C (APC) and factor Xla. We previously described...
molecular biology | SERPIN | VENA-CAVA THROMBOSIS | Serpins | HEPARIN-COFACTOR-II | coagulation | DEFICIENCY | INACTIVATION | protein engineering | thrombosis | REACTIVE CENTER LOOP | HIRUDIN | ANTITHROMBIN | ALPHA-1-ANTITRYPSIN | PERIPHERAL VASCULAR DISEASE | ALPHA-1-PROTEINASE INHIBITOR | heparin cofactor II | HEMATOLOGY | alpha-proteinase inhibitor
molecular biology | SERPIN | VENA-CAVA THROMBOSIS | Serpins | HEPARIN-COFACTOR-II | coagulation | DEFICIENCY | INACTIVATION | protein engineering | thrombosis | REACTIVE CENTER LOOP | HIRUDIN | ANTITHROMBIN | ALPHA-1-ANTITRYPSIN | PERIPHERAL VASCULAR DISEASE | ALPHA-1-PROTEINASE INHIBITOR | heparin cofactor II | HEMATOLOGY | alpha-proteinase inhibitor
Journal Article
VETERINARY JOURNAL, ISSN 1090-0233, 01/2016, Volume 207, pp. 131 - 139
Gastrointestinal (GI) protein loss, due to lymphangiectasia or chronic inflammation, can be challenging to diagnose. This study evaluated the diagnostic...
Crypt abscess | alpha-Proteinase inhibitor | Fecal | Radioimmunoassay | DISEASE | VALIDATION | VETERINARY SCIENCES | PROTEIN-LOSING ENTEROPATHY | Lacteal dilation | LIPOGRANULOMATOUS LYMPHANGITIS | Canine
Crypt abscess | alpha-Proteinase inhibitor | Fecal | Radioimmunoassay | DISEASE | VALIDATION | VETERINARY SCIENCES | PROTEIN-LOSING ENTEROPATHY | Lacteal dilation | LIPOGRANULOMATOUS LYMPHANGITIS | Canine
Journal Article
Nature Communications, ISSN 2041-1723, 04/2015, Volume 6, Issue 1, p. 6722
An imbalance between neutrophil-derived proteases and extracellular inhibitors is widely regarded as an important pathogenic mechanism for lung injury. Despite...
PROTEINASE-INHIBITORS | CHYMOTRYPSIN | EVOLUTION | DISEASES | SERINE PROTEASES | ALPHA-PROTEINASE INHIBITOR | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | EMPHYSEMA | HUMAN-LEUKOCYTE ELASTASE | ALPHA-1-ANTITRYPSIN DEFICIENCY | Leukocyte Elastase - metabolism | Small Molecule Libraries - pharmacology | Peptides - antagonists & inhibitors | Humans | Molecular Sequence Data | Leukocyte Elastase - antagonists & inhibitors | Peptides - administration & dosage | Pulmonary Emphysema - chemically induced | Lung - enzymology | Leukocyte Elastase - administration & dosage | Peptides - metabolism | Proteolysis | HEK293 Cells | Female | Neutrophils - pathology | Recombinant Proteins - metabolism | Amino Acid Sequence | Catalytic Domain | Gene Expression | Lung - pathology | Macrophages - pathology | Neutrophils - enzymology | Peptides - chemistry | Mice, Inbred C57BL | Neutrophils - drug effects | Pulmonary Emphysema - pathology | Recombinant Proteins - chemistry | Pulmonary Emphysema - drug therapy | Recombinant Proteins - administration & dosage | Sequence Homology, Amino Acid | Proteinase Inhibitory Proteins, Secretory - pharmacology | Animals | Leukocyte Elastase - chemistry | Lung - drug effects | alpha 1-Antitrypsin - pharmacology | Macrophages - drug effects | Mice | Cytokines - biosynthesis | Pulmonary Emphysema - enzymology
PROTEINASE-INHIBITORS | CHYMOTRYPSIN | EVOLUTION | DISEASES | SERINE PROTEASES | ALPHA-PROTEINASE INHIBITOR | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | EMPHYSEMA | HUMAN-LEUKOCYTE ELASTASE | ALPHA-1-ANTITRYPSIN DEFICIENCY | Leukocyte Elastase - metabolism | Small Molecule Libraries - pharmacology | Peptides - antagonists & inhibitors | Humans | Molecular Sequence Data | Leukocyte Elastase - antagonists & inhibitors | Peptides - administration & dosage | Pulmonary Emphysema - chemically induced | Lung - enzymology | Leukocyte Elastase - administration & dosage | Peptides - metabolism | Proteolysis | HEK293 Cells | Female | Neutrophils - pathology | Recombinant Proteins - metabolism | Amino Acid Sequence | Catalytic Domain | Gene Expression | Lung - pathology | Macrophages - pathology | Neutrophils - enzymology | Peptides - chemistry | Mice, Inbred C57BL | Neutrophils - drug effects | Pulmonary Emphysema - pathology | Recombinant Proteins - chemistry | Pulmonary Emphysema - drug therapy | Recombinant Proteins - administration & dosage | Sequence Homology, Amino Acid | Proteinase Inhibitory Proteins, Secretory - pharmacology | Animals | Leukocyte Elastase - chemistry | Lung - drug effects | alpha 1-Antitrypsin - pharmacology | Macrophages - drug effects | Mice | Cytokines - biosynthesis | Pulmonary Emphysema - enzymology
Journal Article
Journal of Biotechnology, ISSN 0168-1656, 12/2013, Volume 168, Issue 4, pp. 373 - 381
Exhaustive mutagenesis studies of the reactive centre loop (RCL), a key structural component of proteins belonging to the serpin superfamily of protease...
Library screening | Alpha-1-proteinase inhibitor | Bacteria | Recombinant proteins | Microtiter plate assays | Serpins | ANTI-THROMBIN | SERINE PROTEINASES | ALPHA-PROTEINASE INHIBITOR | HUMAN ANTITHROMBIN-III | HEPARIN-COFACTOR-II | PHAGE DISPLAY | SERPIN STRUCTURE | REACTIVE CENTER LOOP | PLASMINOGEN-ACTIVATOR | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | Genetic Variation | Serpins - genetics | alpha 1-Antitrypsin - genetics | Serpins - metabolism | Escherichia coli - genetics | Humans | Thrombin - antagonists & inhibitors | Recombinant Proteins - genetics | alpha 1-Antitrypsin - metabolism | Amino Acid Sequence - genetics | Kinetics | Gene Expression Regulation, Bacterial | Thrombin | Libraries | Inhibitors | API | Encoding | Assaying | Pools
Library screening | Alpha-1-proteinase inhibitor | Bacteria | Recombinant proteins | Microtiter plate assays | Serpins | ANTI-THROMBIN | SERINE PROTEINASES | ALPHA-PROTEINASE INHIBITOR | HUMAN ANTITHROMBIN-III | HEPARIN-COFACTOR-II | PHAGE DISPLAY | SERPIN STRUCTURE | REACTIVE CENTER LOOP | PLASMINOGEN-ACTIVATOR | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | Genetic Variation | Serpins - genetics | alpha 1-Antitrypsin - genetics | Serpins - metabolism | Escherichia coli - genetics | Humans | Thrombin - antagonists & inhibitors | Recombinant Proteins - genetics | alpha 1-Antitrypsin - metabolism | Amino Acid Sequence - genetics | Kinetics | Gene Expression Regulation, Bacterial | Thrombin | Libraries | Inhibitors | API | Encoding | Assaying | Pools
Journal Article
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, ISSN 0304-4165, 01/2014, Volume 1840, Issue 1, pp. 416 - 427
Background: Human ai-proteinase inhibitor (alpha 1PI) is the most abundant serine protease inhibitor in the blood and the heterologous expression of...
HYDROPHOBIC CORE | Single amino acid substitution | HUMAN ALPHA-ANTITRYPSIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | Protein stability | TRANSGENIC TOMATO PLANTS | PROTEASE INHIBITOR | Oxidation resistance | BIOPHYSICS | Human alpha-proteinase inhibitor | REACTIVE CENTER | BIOLOGICAL-ACTIVITY | Transgenic plant | Recombinant therapeutic protein | HUMAN ALPHA-1-ANTITRYPSIN | NATIVE STRAIN | HUMAN ALPHA-1-PROTEINASE INHIBITOR
HYDROPHOBIC CORE | Single amino acid substitution | HUMAN ALPHA-ANTITRYPSIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | Protein stability | TRANSGENIC TOMATO PLANTS | PROTEASE INHIBITOR | Oxidation resistance | BIOPHYSICS | Human alpha-proteinase inhibitor | REACTIVE CENTER | BIOLOGICAL-ACTIVITY | Transgenic plant | Recombinant therapeutic protein | HUMAN ALPHA-1-ANTITRYPSIN | NATIVE STRAIN | HUMAN ALPHA-1-PROTEINASE INHIBITOR
Journal Article