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Food Analytical Methods, ISSN 1936-9751, 9/2018, Volume 11, Issue 9, pp. 2431 - 2437
Journal Article
PLoS ONE, ISSN 1932-6203, 01/2013, Volume 8, Issue 1, p. e53343
Kunitz-type serine protease inhibitors are involved in various physiological processes, such as ion channel blocking, blood coagulation, fibrinolysis, and... 
VENOM | KING COBRA | MULTIDISCIPLINARY SCIENCES | PSEUDONAJA-TEXTILIS | SILK PROTEIN | CHYMOTRYPSIN INHIBITOR | MOLECULAR-CLONING | BOOPHILUS-MICROPLUS | EXPRESSION | ARANEUS-VENTRICOSUS | PEPTIDE | Factor Xa - chemistry | Chymotrypsin - metabolism | Molecular Sequence Data | Baculoviridae - genetics | Tissue Plasminogen Activator - chemistry | Pancreatic Elastase - antagonists & inhibitors | Antifibrinolytic Agents - metabolism | Trypsin Inhibitors - chemistry | Serine Proteinase Inhibitors - chemistry | Spiders - metabolism | Aprotinin - genetics | Conserved Sequence | Antifibrinolytic Agents - chemistry | Spiders - chemistry | Protein Structure, Tertiary | Amino Acid Sequence | Gene Expression | Fibrinolysin - antagonists & inhibitors | Recombinant Proteins - chemistry | Arthropod Proteins - genetics | Recombinant Proteins - genetics | Trypsin - metabolism | Arthropod Proteins - chemistry | Fibrinolysin - chemistry | Sequence Alignment | Animals | Thrombin - chemistry | Trypsin Inhibitors - genetics | Chymotrypsin - antagonists & inhibitors | Pancreatic Elastase - chemistry | Aprotinin - chemistry | Serine Proteinase Inhibitors - genetics | Enzymes | Care and treatment | Protease inhibitors | Physiological aspects | Hydrolases | Inflammation | Research | Health aspects | Risk factors | Blood coagulation | Serine | Thrombin | Amino acids | Baculovirus | Plasmin | t-Plasminogen activator | Proteins | Protease | Ion channels | Elastase | Inhibition | Recombinant | Natural resources | Proteinase inhibitors | Potassium channels | Fibrinolysis | Chymotrypsin | Trypsin | Insects | Proteases | Lysine | Venom | Insect cells | Serine proteinase
Journal Article
Scientific Reports, ISSN 2045-2322, 12/2018, Volume 8, Issue 1, pp. 14502 - 10
Amphibian venom-derived peptides have high potential in the field of anticancer drug discovery. We have isolated a novel Bowman-Birk proteinase inhibitor... 
PROTEASE-ACTIVATED RECEPTORS | ODOROUS FROG | MESSENGER-RNA EXPRESSION | COLORECTAL-CANCER | MULTIDISCIPLINARY SCIENCES | AMPHIBIAN SKIN | HUMAN TISSUE KALLIKREINS | ANTIMICROBIAL PEPTIDES | HUMAN POLYMORPHONUCLEAR LEUKOCYTES | TRYPSIN-INHIBITOR | CLINICAL-SIGNIFICANCE | Anti-Infective Agents - isolation & purification | Rats, Wistar | Anti-Infective Agents - pharmacology | Escherichia coli - drug effects | Serine Proteinase Inhibitors - isolation & purification | Muscle, Smooth - drug effects | Candida albicans - drug effects | Antineoplastic Agents - isolation & purification | Base Sequence | Rana esculenta - metabolism | Female | Antineoplastic Agents - pharmacology | Serine Proteinase Inhibitors - pharmacology | Amino Acid Sequence | Serine Proteinase Inhibitors - chemical synthesis | RNA, Messenger - genetics | Models, Molecular | Rats | Skin - enzymology | Animals | Colonic Neoplasms - pathology | Amphibian Venoms - enzymology | Cell Line, Tumor | Protein Conformation | Molecular Docking Simulation | Muscle Relaxation - drug effects | Staphylococcus aureus - drug effects | Serine Proteinase Inhibitors - genetics | Drug Screening Assays, Antitumor | Peptidase | Epithelial cells | Secretion | Therapeutic applications | Serine | Colorectal carcinoma | Proteinase | Serine proteinase inhibitors | Amino acid sequence | Kallikrein | Cytotoxicity | Smooth muscle | mRNA | Proteinase inhibitors | Secretions | Polymerase chain reaction | Trypsin | Venom | Serine proteinase | Skin | Cancer
Journal Article
Tetrahedron, ISSN 0040-4020, 10/2014, Volume 70, Issue 42, pp. 7675 - 7680
Sunflower Trypsin Inhibitor (SFTI-1) analogues have been prepared from simple linear precursors produced either by chemical synthesis or following purification... 
KLK5 | Native chemical ligation | Sunflower trypsin inhibitor | Atopic dermatitis | CIRCULAR PROTEINS | MATRIPTASE | PROTEOLYTIC CASCADE | DESIGN | CHEMISTRY, ORGANIC | SERINE-PROTEASE | CANCER PROGRESSION | CYCLIC-PEPTIDES | Kallikrein | Trypsin | Peptides | Analysis
Journal Article
Biochemical Journal, ISSN 0264-6021, 03/2004, Volume 378, Issue 3, pp. 705 - 716
The proteins that inhibit peptidases are of great importance in medicine and biotechnology, but there has never been a comprehensive system of classification... 
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 11/2016, Volume 11, Issue 11, p. e0165572
Purpose This study was aimed to purify and characterize the Protease inhibitor (PI) from a plant Allium sativum (garlic) with strong medicinal properties and... 
SEEDS | PROTEINASE-INHIBITORS | ALPHA-AMYLASE INHIBITOR | STABILITY | MULTIDISCIPLINARY SCIENCES | PURIFICATION | DISEASE | RESISTANCE | CHEMOPREVENTION | CANCER | Plant Proteins - isolation & purification | Detergents - pharmacology | Oxidants - pharmacology | Temperature | Plant Proteins - pharmacology | Electrophoresis, Polyacrylamide Gel | Trypsin Inhibitors - pharmacology | Trypsin Inhibitors - isolation & purification | Garlic - chemistry | Chromatography, High Pressure Liquid | Serpins - pharmacology | Peptides - pharmacology | Peptides - isolation & purification | Protein Stability - drug effects | Serpins - isolation & purification | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Kinetics | Circular Dichroism | Hydrogen-Ion Concentration | Trypsin | Liquid chromatography | Protease inhibitors | Glycine | Proteases | Trypsin inhibitors | Biotechnology | Ammonium | Seeds | Disease | Oxidizing agents | Purity | Cytotoxicity | Amino acids | Helices | pH effects | Data bases | Molecular weight | Proteins | Databases | Hydrogen ions | Protease | Temperature effects | Lead | Oxidation | Inhibition | Allium sativum | Food | Columns (structural) | Medicinal plants | Spectroscopy | Enzymes | Fractionation | Tryptophan | Reducing agents | Interdisciplinary aspects | Secondary structure | Detergents | Substrates | Chemical modification | Ammonium sulfate | Lysine | Anion exchanging | Garlic | Protein structure | Cancer | Ammonium sulfates
Journal Article
Molecular Oncology, ISSN 1574-7891, 02/2018, Volume 12, Issue 2, pp. 224 - 238
The mitogen‐activated protein kinase (MAPK) pathway plays a central role in colorectal cancers (CRC). In particular, BRAF V600E‐mutant tumors, which represent... 
trametinib | BRAF V600E | colorectal cancer | SPINK1 | inhibitor | biomarker | ACTIVATION | TATI | PROLIFERATION | CANCER | ONCOLOGY | TRYPSINOGEN-2 | RESISTANCE | PROGNOSTIC MARKER | EXPRESSION | KINASES | Colorectal Neoplasms - genetics | Humans | Middle Aged | Male | Trypsin Inhibitor, Kazal Pancreatic - genetics | Trypsin Inhibitor, Kazal Pancreatic - metabolism | Adenocarcinoma - metabolism | Colorectal Neoplasms - drug therapy | Female | Pyrimidinones - pharmacology | Adenocarcinoma - genetics | Colorectal Neoplasms - metabolism | Caco-2 Cells | Pyrimidinones - therapeutic use | Activating Transcription Factor 4 - genetics | Piperazines - therapeutic use | Adenocarcinoma - drug therapy | Piperazines - pharmacology | HT29 Cells | Indazoles - pharmacology | Activating Transcription Factor 4 - metabolism | Mitogen-Activated Protein Kinases - antagonists & inhibitors | Protein Kinase Inhibitors - therapeutic use | Proto-Oncogene Proteins B-raf - genetics | Cell Line, Tumor | Aged | Protein Kinase Inhibitors - pharmacology | Pyridones - therapeutic use | Indazoles - therapeutic use | Pyridones - pharmacology | Cohort Studies | Mitogen-Activated Protein Kinases - metabolism | Adenocarcinoma | Phosphorylation | Immunoglobulins | Prognosis | Peptidase | Secretion | Serine | Activating transcription factor 4 | Colorectal cancer | Melanoma | Extracellular signal-regulated kinase | MAP kinase | Kinases | Gene expression | Cancer therapies | Trypsin | Epidermal growth factor | Protein kinase | Medical prognosis | Mutation | Serine peptidase | Cellular stress response | Deoxyribonucleic acid--DNA | Tumors
Journal Article
PLoS ONE, ISSN 1932-6203, 11/2016, Volume 11, Issue 11, p. e0166268
Journal Article