Serine Protease

The transmembrane serine protease (TMPRSS3) mutated in deafness DFNB8/10 activates the epithelial sodium channel (ENaC) in vitro

Membrane Proteins / Western blotting / In Situ Hybridization / Biological Sciences / Humans / Mice / Female / Animals / Male / Human Molecular Genetics / Endoplasmic Reticulum / Deafness / Genotype / Rats / Voltage-Gated Sodium Channels / Xenopus laevis / organ of Corti / Rabbits / Oocytes / Serine Protease / Protein Transport / Spiral Ganglion / Stria Vascularis / DNA mutational analysis / Mice / Female / Animals / Male / Human Molecular Genetics / Endoplasmic Reticulum / Deafness / Genotype / Rats / Voltage-Gated Sodium Channels / Xenopus laevis / organ of Corti / Rabbits / Oocytes / Serine Protease / Protein Transport / Spiral Ganglion / Stria Vascularis / DNA mutational analysis

Wolbachia endosymbionts of Onchocerca volvulus express a putative periplasmic HtrA-type serine protease

Microbiology / Immunology / Medical Microbiology / Symbiosis / Drosophila melanogaster / PCR / Animals / Bacteria / Wolbachia / Alkaline phosphatase / Amino Acid Profile / SIGNAL PEPTIDE / Amino Acid Sequence / Larval Development / Serine Protease / Full Length Movies / Molecular Sequence Data / PCR / Animals / Bacteria / Wolbachia / Alkaline phosphatase / Amino Acid Profile / SIGNAL PEPTIDE / Amino Acid Sequence / Larval Development / Serine Protease / Full Length Movies / Molecular Sequence Data

Potent 4-amino-5-azaindole factor VIIa inhibitors

Organic Chemistry / PT / Pyridines / Bioorganic and medicinal Chemistry / Structure activity Relationship / Chemical Synthesis / Serine Protease / Tissue Factor / Molecular Structure / Selectivity / Chemical Synthesis / Serine Protease / Tissue Factor / Molecular Structure / Selectivity

C-Npys (S-3-nitro-2-pyridinesulfenyl) and peptide derivatives can inhibit a serine-thiol proteinase activity from Paracoccidioides brasiliensis

Fluorescence Resonance Energy Transfer / FRET / Peptides / Biochemical / Affinity chromatography / Fungal Pathogens / Pyridines / PCM / Cysteine endopeptidases / Serine Protease / Therapeutic Use / Paracoccidioides / Biochemistry and cell biology / Molecular Structure / Cysteine Proteinase Inhibitors / Fungal Pathogens / Pyridines / PCM / Cysteine endopeptidases / Serine Protease / Therapeutic Use / Paracoccidioides / Biochemistry and cell biology / Molecular Structure / Cysteine Proteinase Inhibitors

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