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Fish and Shellfish Immunology, ISSN 1050-4648, 11/2016, Volume 58, pp. 563 - 571
Tissue factor pathway inhibitors (TFPIs) are Kunitz-type serine protease inhibitors that reversibly regulate the blood coagulation induced by tissue factor.... 
TFPI-1 | C-terminal peptides | Antibacterial activity | Cynoglossus semilaevis | Expression | TFPI-2 | CANCER-CELLS | SERINE-PROTEASE INHIBITORS | BLOOD-COAGULATION | IMMUNOLOGY | IDENTIFICATION | TISSUE-FACTOR | FISHERIES | FACTOR-PATHWAY INHIBITOR | KUNITZ DOMAIN | MESSENGER-RNA | MARINE & FRESHWATER BIOLOGY | VETERINARY SCIENCES | CDNA CLONING | Gram-Positive Bacterial Infections - immunology | DNA Virus Infections - veterinary | Gram-Positive Bacteria - physiology | Lipoproteins - genetics | Glycoproteins - metabolism | Gram-Negative Bacterial Infections - immunology | Phylogeny | Gram-Negative Bacterial Infections - microbiology | Fish Proteins - genetics | Gram-Positive Bacterial Infections - microbiology | Lipoproteins - metabolism | Fish Diseases - immunology | Gram-Positive Bacterial Infections - genetics | Glycoproteins - chemistry | Gram-Negative Bacterial Infections - veterinary | Iridoviridae - physiology | Gram-Negative Bacteria - physiology | Gram-Positive Bacterial Infections - veterinary | Glycoproteins - genetics | Amino Acid Sequence | Gene Expression | Fish Diseases - microbiology | Fish Proteins - chemistry | Gram-Negative Bacterial Infections - genetics | Fish Proteins - metabolism | Lipoproteins - chemistry | DNA Virus Infections - genetics | Fish Diseases - genetics | Sequence Alignment | Animals | Fish Diseases - virology | DNA Virus Infections - immunology | DNA Virus Infections - virology | Flatfishes | Virus diseases | Peptides | Protease inhibitors | Analysis | Liver | Marine sciences | Thrombin | Skin | Antibacterial agents | Index Medicus
Journal Article
Fish and Shellfish Immunology, ISSN 1050-4648, 01/2017, Volume 60, pp. 466 - 473
Tissue factor pathway inhibitor 1 (TFPI-1) is a serine protease inhibitor that inhibits tissue factor (TF)-mediated coagulation. The C-terminal region of... 
Teleost | TFPI-1 | Antiviral | Antibacterial mechanism | Antimicrobial peptide | DNA-BINDING | EXPRESSION ANALYSIS | HEPCIDIN | ANTIMICROBIAL PEPTIDES | IMMUNOLOGY | IN-VITRO | FISHERIES | MARINE & FRESHWATER BIOLOGY | BIOLOGY | VETERINARY SCIENCES | FACTOR PATHWAY INHIBITOR | C-TERMINAL PEPTIDES | Gram-Positive Bacterial Infections - immunology | DNA Virus Infections - veterinary | Gram-Positive Bacteria - physiology | Lipoproteins - genetics | Gram-Negative Bacterial Infections - immunology | Gram-Negative Bacterial Infections - microbiology | Fish Proteins - genetics | Gram-Positive Bacterial Infections - microbiology | Lipoproteins - metabolism | Fish Diseases - immunology | Gram-Positive Bacterial Infections - genetics | Gram-Negative Bacterial Infections - veterinary | Iridoviridae - physiology | Gram-Negative Bacteria - physiology | Gram-Positive Bacterial Infections - veterinary | Fish Diseases - microbiology | Gram-Negative Bacterial Infections - genetics | Fish Proteins - metabolism | DNA Virus Infections - genetics | Fish Diseases - genetics | Animals | Fish Diseases - virology | DNA Virus Infections - immunology | Sequence Analysis, DNA - veterinary | DNA Virus Infections - virology | Flatfishes | Peptides | Protease inhibitors | RNA | Analysis | Marine biology | Thrombin | Amino acids | Health aspects | Antibacterial agents | Index Medicus
Journal Article
Journal Article
MOLECULAR MICROBIOLOGY, ISSN 0950-382X, 01/2005, Volume 55, Issue 1, pp. 250 - 260
The sigma(s) subunit of RNA polymerase (RNAP) is the master regulator of the general stress response in Escherichia coli. Nevertheless, the selectivity of... 
POLYMERASE ALPHA-SUBUNIT | PROTEIN | DNA | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSCRIPTION ACTIVATION | REGION 4 | MICROBIOLOGY | C-TERMINAL DOMAIN | BACTERIAL TRANSCRIPTION | FACTOR SELECTIVITY | IDENTIFICATION | RNA-POLYMERASE
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 01/2017, Volume 429, Issue 2, pp. 280 - 294
The epidermal growth factor receptor (EGFR) is a receptor tyrosine kinase (TK) that—once activated upon ligand binding—leads to receptor dimerization,... 
non-small cell lung cancer | protein–protein interaction | two-hybrid screening | oncogenic signaling | EGFR | Protein-protein interaction | PATHWAYS | ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | KINASE | FAMILY | ACIDIC COILED-COIL | TACC3 | protein-protein interaction | FUSIONS | PROTEINS | EXPRESSION | AURORA | RNA, Small Interfering - genetics | Receptor, Epidermal Growth Factor - genetics | Phosphorylation | Immunoprecipitation | Microtubule-Associated Proteins - genetics | Signal Transduction | Carcinoma, Non-Small-Cell Lung - genetics | Cell Survival | Microtubule-Associated Proteins - metabolism | Humans | Computational Biology | Gene Expression Regulation, Neoplastic | Receptor, Epidermal Growth Factor - metabolism | Gene Deletion | HEK293 Cells | Mitogen-Activated Protein Kinases - genetics | Protein Interaction Domains and Motifs | HeLa Cells | Mitogen-Activated Protein Kinases - metabolism | RNA, Small Interfering - metabolism | Tyrosine | Epidermal growth factor | Drug discovery | Lung cancer, Non-small cell | Mitogens | Protein kinases | Protein-protein interactions | Index Medicus | FGFR, fibroblast growth factor receptor | SH, Src homology | EGF, epidermal growth factor | TF, transcription factor | EGFR-ex19del, EGFR-exon19 deletion | TACC, transforming acidic coiled-coil protein | PBS, phosphate-buffered saline | DMEM, Dulbecco's modified Eagle's medium | PEI, polyethylenimine | Nub, N-terminal half of ubiquitin | SRE, serum response element | GFP, green fluorescent protein | NSCLC, non-small cell lung cancer | GO, gene ontology | TKI, TK inhibitor | EGFR, epidermal growth factor receptor | TK, tyrosine kinase | ERK, extracellular signal-regulated kinase | EGFR-WT, EGFR-wildtype | MOI, multiplicity of infection | MaMTH, mammalian membrane two-hybrid | KM, Kaplan–Meier | Grb2, growth factor receptor-bound protein 2 | Cub, C-terminal half of ubiquitin | MAPK, mitogen-activated protein kinase
Journal Article
FEBS Letters, ISSN 0014-5793, 04/2014, Volume 588, Issue 7, pp. 1087 - 1093
Botulinum neurotoxins (BoNTs) inhibit neurotransmitter release by hydrolysing SNARE proteins. The most important serotype BoNT/A employs the synaptic vesicle... 
Monoclonal antibody | Protein receptor binding site | Neutralisation | Botulinum neurotoxin A | SV2 | ganglioside binding site | heavy chain | circular dichroism | mice phrenic nerve hemidiaphragm assay | G, H | E, H | fragment of serotype A-G, C-terminal Streptag | fragment of BoNT serotype A, E, F, G or A-G respectively | glutathion-S-transferase | carboxyl-terminal half of HC | light chain | GBS | synaptotagmin | H6F3H | rat synaptic vesicle glycoprotein 2 isoform A, B, or C | MPN assay | amino-terminal half of HC | GST | BoNT | botulinum neurotoxin | A, H | F, H | rSV2A, B, C | mAb | Syt | scFv | single-chain variable fragments | N-terminal 6× His tag, 3× Flag tag, H | monoclonal antibody | ENTRY | PROTEIN-RECEPTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | MOLECULAR EVOLUTION | LIGHT-CHAIN | ANTIBODY | GANGLIOSIDES | SYNAPTOTAGMIN-II | CELL BIOLOGY | BIOPHYSICS | AFFINITY | H-CC-DOMAIN | Neurotoxins - chemistry | Mutagenesis, Site-Directed | Humans | Membrane Glycoproteins - chemistry | Mice, Inbred C57BL | Botulinum Toxins, Type A - chemistry | Neurotoxins - genetics | Botulinum Toxins, Type A - pharmacology | Neurotoxins - pharmacology | Botulinum Toxins, Type A - genetics | Nerve Tissue Proteins - chemistry | Animals | Phrenic Nerve - drug effects | Inhibitory Concentration 50 | Protein Binding | Mice | Neural Conduction - drug effects | Protein Interaction Domains and Motifs | Binding Sites | Phrenic Nerve - physiology | Amino Acid Substitution | Index Medicus | protein receptor binding site | botulinum neurotoxin A | neutralisation
Journal Article
FEBS Letters, ISSN 0014-5793, 11/2013, Volume 587, Issue 23, pp. 3831 - 3836
Botulinum neurotoxins translocate their enzymatic domain across vesicular membranes. The molecular triggers of this process are unknown. Here, we tested the... 
Translocation | Botulinum neurotoxin | Bafilomycin A1 | pH sensor | Phrenic nerve hemidiaphragm toxicity test | heavy chain | C-terminal half of HC | MPN | VAMP-2 | foetal bovine serum | triple mutant | soluble N-ethyl maleimide sensitive factor attachment protein receptors | a pheochromocytoma cell line | vesicle associated membrane protein 2 | minimum essential medium | botulinum neurotoxin/serotype X | CGNs | FBS | C-terminal domain of the H | SNAREs | light chain | BoNT/X | SNAP-25 | PBS | SV2 | cerebellar granule neurons | N-terminal half of HC | PC12 | fragment | MEM | synaptosomal-associated protein of 25 kDa | mice phrenic nerve | phosphate buffered saline | BafA1 | synaptic vesicle (glyco-)protein 2 | bafilomycin A1 | N-terminal domain of the H | wild-type | SYNAPTIC VESICLES | ENTRY | PROTEIN-RECEPTOR | TETANUS | TOXIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | MEMBRANE INTERACTION | CELL BIOLOGY | BIOPHYSICS | LOW PH | NEURONS | BINDING-SITE | T-DOMAIN | Protons | Botulinum Toxins - genetics | Neurotoxins - chemistry | Catalytic Domain | Botulinum Toxins - metabolism | Glutamic Acid - genetics | Cells, Cultured | Neurotoxins - genetics | Neurotoxins - toxicity | Protein Transport | Aspartic Acid - genetics | Botulinum Toxins - toxicity | Animals | Botulinum Toxins, Type A | Botulinum Toxins - chemistry | Cytosol - metabolism | Neurotoxins - metabolism | Cell Membrane - metabolism | Mice | Aspartic Acid - chemistry | Mutation | Neurons - drug effects | Glutamic Acid - chemistry | Hydrogen-Ion Concentration | Enzymes | Index Medicus
Journal Article