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1-[(2R)-4-(4-benzylpiperazin-1-yl)-4-oxo-2-[(phenylmethanesulfonyl)amino]butanoyl]-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
3-cyclohexyl-N-(phenylmethanesulfonyl)-D-alanyl-N-[(4-carbamimidoylphenyl)methyl]-N6-decanoyl-L-lysinamide
peptide mimetic inhibitor. Cleavage of HA0 and the spread of A/Hamburg/09 in TMPRSS2-expressing cells are strongly inhibited by the decanoylated inhibitor. Only low amounts of progeny virions are detected in supernatants of inhibitor-treated cells at 24 h p.i. due to the suppression of proteolytic activation of HA and thus the suppression of virus propagation
3-[(2S)-2-[(2',4'-dichloro[1,1'-biphenyl]-3-sulfonyl)amino]-3-(4-[2-[(methylcarbamoyl)amino]ethyl]piperidin-1-yl)-3-oxopropyl]benzene-1-carboximidamide
-
3-[(2S)-2-[(2',4'-dimethoxy[1,1'-biphenyl]-3-sulfonyl)amino]-3-(4-[2-[(methylcarbamoyl)amino]ethyl]piperidin-1-yl)-3-oxopropyl]benzene-1-carboximidamide
-
3-[(2S)-3-[4-(2-aminoethyl)piperidin-1-yl]-2-[(2',4'-dichloro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
treatment of cells with 10 microM inhibitor causes a 10fold and 100fold reduction in virus titres of A/Hamburg H1N1 and A/Aichi H3N2 respectively, at 24 h
3-[(2S)-3-[4-[(cyclohexylcarbamoyl)amino]piperidin-1-yl]-2-[(2',4'-dichloro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
-
3-[(2S)-3-[4-[(cyclohexylcarbamoyl)amino]piperidin-1-yl]-2-[(2',4'-dimethoxy[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
-
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(2',3'-dichloro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
-
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(2',4'-dichloro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
-
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(2',4'-dimethoxy[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
-
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(2'-chloro-4'-ethoxy[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
-
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(2'-chloro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
-
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(2'-fluoro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
-
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(3',4'-dichloro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
-
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(3'-fluoro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
-
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(4'-chloro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
-
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(4'-ethoxy[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
-
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(4'-fluoro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
-
4-[4-[([1-[3-carbamimidoyl-N-(2',3'-dichloro[1,1'-biphenyl]-3-sulfonyl)-L-phenylalanyl]piperidin-4-yl]carbamoyl)amino]cyclohexyl]-N-methylbutanamide
-
4-[4-[([1-[3-carbamimidoyl-N-(2',4'-dichloro[1,1'-biphenyl]-3-sulfonyl)-L-phenylalanyl]piperidin-4-yl]carbamoyl)amino]cyclohexyl]-N-methylbutanamide
-
4-[4-[([1-[3-carbamimidoyl-N-(2',4'-dimethoxy[1,1'-biphenyl]-3-sulfonyl)-L-phenylalanyl]piperidin-4-yl]carbamoyl)amino]cyclohexyl]-N-methylbutanamide
-
4-[4-[([1-[3-carbamimidoyl-N-(2'-chloro-4'-ethoxy[1,1'-biphenyl]-3-sulfonyl)-L-phenylalanyl]piperidin-4-yl]carbamoyl)amino]cyclohexyl]-N-methylbutanamide
-
4-[4-[([1-[3-carbamimidoyl-N-(2'-fluoro[1,1'-biphenyl]-3-sulfonyl)-L-phenylalanyl]piperidin-4-yl]carbamoyl)amino]cyclohexyl]-N-methylbutanamide
-
4-[4-[([1-[3-carbamimidoyl-N-(3',4'-dichloro[1,1'-biphenyl]-3-sulfonyl)-L-phenylalanyl]piperidin-4-yl]carbamoyl)amino]cyclohexyl]-N-methylbutanamide
-
4-[4-[([1-[3-carbamimidoyl-N-(3'-fluoro[1,1'-biphenyl]-3-sulfonyl)-L-phenylalanyl]piperidin-4-yl]carbamoyl)amino]cyclohexyl]-N-methylbutanamide
-
4-[4-[([1-[3-carbamimidoyl-N-(4'-fluoro[1,1'-biphenyl]-3-sulfonyl)-L-phenylalanyl]piperidin-4-yl]carbamoyl)amino]cyclohexyl]-N-methylbutanamide
-
5-oxo-N-(phenylmethanesulfonyl)-5-[4-(pyrimidin-2-yl)piperazin-1-yl]-D-norvalyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
5-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-5-oxo-N-(phenylmethanesulfonyl)-D-norvalyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
benzyl 4-[(3R)-4-[(2S)-2-[[(4-carbamimidoylphenyl)methyl]carbamoyl]pyrrolidin-1-yl]-4-oxo-3-[(phenylmethanesulfonyl)amino]butanoyl]piperazine-1-carboxylate
-
bromhexine
treatment significantly reduces the migration and invasion phenotypes promoted by TMPRSS2-activated HGF
D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
D-homophenylalanyl-N-[(4-carbamimidoylphenyl)methyl]-L-alaninamide
-
D-homophenylalanyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
D-homotyrosinyl-N-[(4-carbamimidoylphenyl)methyl]-L-alaninamide
-
D-phenylalanyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
methyl 1-[3-carbamimidoyl-N-(naphthalene-2-sulfonyl)-L-phenylalanyl]piperidine-4-carboxylate
-
N-(3-[[(2S)-1-[4-(2-aminoethyl)piperidin-1-yl]-3-(3-carbamimidoylphenyl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-(4-[2-[(benzylcarbamoyl)amino]ethyl]piperidin-1-yl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-(4-[2-[(cyclohexylcarbamoyl)amino]ethyl]piperidin-1-yl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-(4-[2-[(ethylcarbamoyl)amino]ethyl]piperidin-1-yl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-(4-[2-[(methylcarbamoyl)amino]ethyl]piperidin-1-yl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-(4-[2-[(phenylcarbamoyl)amino]ethyl]piperidin-1-yl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-[4-[(benzylcarbamoyl)amino]piperidin-1-yl]-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-[4-[(cyclohexylcarbamoyl)amino]piperidin-1-yl]-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-[4-[(ethylcarbamoyl)amino]piperidin-1-yl]-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-[4-[(methylcarbamoyl)amino]piperidin-1-yl]-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-[4-[(phenylcarbamoyl)amino]piperidin-1-yl]-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-[4-[2-(carbamoylamino)ethyl]piperidin-1-yl]-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
-
N-(phenylmethanesulfonyl)-4-carbamimidoyl-D-phenylalanyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
N-(phenylmethanesulfonyl)-4-cyano-D-phenylalanyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
N-(phenylmethanesulfonyl)-D-alanyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
N-(phenylmethanesulfonyl)-D-alpha-aspartyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
N-(phenylmethanesulfonyl)-D-cyclohexylalanyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
N-(phenylmethanesulfonyl)-D-leucyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
N-(phenylmethanesulfonyl)-D-phenylalanyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
N-(phenylmethanesulfonyl)-D-valyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
N-(phenylmethanesulfonyl)-L-leucyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
N-(phenylmethanesulfonyl)glycyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
N-[(4-carbamimidoylphenyl)methyl]-1-[(2R)-4-(morpholin-4-yl)-4-oxo-2-[(phenylmethanesulfonyl)amino]butanoyl]-L-prolinamide
-
N-[(4-carbamimidoylphenyl)methyl]-1-[(2R)-4-oxo-2-[(phenylmethanesulfonyl)amino]-4-(piperazin-1-yl)butanoyl]-L-prolinamide
-
N-[(4-carbamimidoylphenyl)methyl]-1-[(2R)-4-oxo-2-[(phenylmethanesulfonyl)amino]-4-[4-(propan-2-yl)piperazin-1-yl]butanoyl]-L-prolinamide
-
N-[(4-carbamimidoylphenyl)methyl]-1-[(2R)-4-oxo-2-[(phenylmethanesulfonyl)amino]-4-[4-(pyrimidin-2-yl)piperazin-1-yl]butanoyl]-L-prolinamide
-
N-[(4-carbamimidoylphenyl)methyl]-1-[(2R)-4-[4-(2-hydroxyethyl)piperazin-1-yl]-4-oxo-2-[(phenylmethanesulfonyl)amino]butanoyl]-L-prolinamide
-
N-[(4-carbamimidoylphenyl)methyl]-1-[(2R)-4-[4-(3,5-dimethylphenyl)piperazin-1-yl]-4-oxo-2-[(phenylmethanesulfonyl)amino]butanoyl]-L-prolinamide
-
N-[(4-carbamimidoylphenyl)methyl]-1-[(2R)-4-[4-[3-(dimethylamino)propyl]piperazin-1-yl]-4-oxo-2-[(phenylmethanesulfonyl)amino]butanoyl]-L-prolinamide
-
N-[3-([(2S)-3-(3-carbamimidoylphenyl)-1-[4-(carbamoylamino)piperidin-1-yl]-1-oxopropan-2-yl]sulfamoyl)phenyl]-beta-alaninamide
-
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-2-aminobutanoylamide
-
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-alaninamide
-
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-argininamide
-
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-isoleucinamide
-
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-leucinamide
-
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-norvalinamide
-
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-phenylalaninamide
-
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-serinamide
-
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-valinamide
-
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]glycinamide
-
N2-(phenylmethanesulfonyl)-D-arginyl-N-[[2-(aminomethyl)-5-chlorophenyl]methyl]-L-prolinamide
-
N2-(phenylmethanesulfonyl)-D-arginyl-N6-[(benzyloxy)carbonyl]-N-[(4-carbamimidoylphenyl)methyl]-L-lysinamide
-
N2-(phenylmethanesulfonyl)-D-homoarginyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
N2-(phenylmethanesulfonyl)-D-homophenylalanyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
N2-(phenylmethanesulfonyl)-D-lysyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
N2-(phenylmethanesulfonyl)-N-tert-butoxy-D-asparaginyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
N2-(phenylmethanesulfonyl)-N6-(benzyloxycarbonyl)-D-lysyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
N2-(phenylmethanesulfonyl)-O-(tert-butyl)-D-glutamyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
-
Nafamostat
potent inhibitor of protein-mediated membrane fusion, blocks MERS-CoV infection in vitro
tert-butyl N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-alpha-asparaginate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.000363
1-[(2R)-4-(4-benzylpiperazin-1-yl)-4-oxo-2-[(phenylmethanesulfonyl)amino]butanoyl]-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000011
3-[(2S)-2-[(2',4'-dichloro[1,1'-biphenyl]-3-sulfonyl)amino]-3-(4-[2-[(methylcarbamoyl)amino]ethyl]piperidin-1-yl)-3-oxopropyl]benzene-1-carboximidamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000013
3-[(2S)-2-[(2',4'-dimethoxy[1,1'-biphenyl]-3-sulfonyl)amino]-3-(4-[2-[(methylcarbamoyl)amino]ethyl]piperidin-1-yl)-3-oxopropyl]benzene-1-carboximidamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000005
3-[(2S)-3-[4-[(cyclohexylcarbamoyl)amino]piperidin-1-yl]-2-[(2',4'-dichloro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000003
3-[(2S)-3-[4-[(cyclohexylcarbamoyl)amino]piperidin-1-yl]-2-[(2',4'-dimethoxy[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.0000027
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(2',3'-dichloro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.0000009
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(2',4'-dichloro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000001
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(2',4'-dimethoxy[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.0000078
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(2'-chloro-4'-ethoxy[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000028
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(2'-fluoro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000089
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(3',4'-dichloro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000072
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(3'-fluoro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.0000054 - 0.0000073
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(4'-chloro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
0.0000048
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(4'-ethoxy[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000028
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(4'-fluoro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000019
4-[4-[([1-[3-carbamimidoyl-N-(2',3'-dichloro[1,1'-biphenyl]-3-sulfonyl)-L-phenylalanyl]piperidin-4-yl]carbamoyl)amino]cyclohexyl]-N-methylbutanamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000004
4-[4-[([1-[3-carbamimidoyl-N-(2',4'-dichloro[1,1'-biphenyl]-3-sulfonyl)-L-phenylalanyl]piperidin-4-yl]carbamoyl)amino]cyclohexyl]-N-methylbutanamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.0000045
4-[4-[([1-[3-carbamimidoyl-N-(2',4'-dimethoxy[1,1'-biphenyl]-3-sulfonyl)-L-phenylalanyl]piperidin-4-yl]carbamoyl)amino]cyclohexyl]-N-methylbutanamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000017
4-[4-[([1-[3-carbamimidoyl-N-(2'-chloro-4'-ethoxy[1,1'-biphenyl]-3-sulfonyl)-L-phenylalanyl]piperidin-4-yl]carbamoyl)amino]cyclohexyl]-N-methylbutanamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.00004
4-[4-[([1-[3-carbamimidoyl-N-(2'-fluoro[1,1'-biphenyl]-3-sulfonyl)-L-phenylalanyl]piperidin-4-yl]carbamoyl)amino]cyclohexyl]-N-methylbutanamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000036
4-[4-[([1-[3-carbamimidoyl-N-(3',4'-dichloro[1,1'-biphenyl]-3-sulfonyl)-L-phenylalanyl]piperidin-4-yl]carbamoyl)amino]cyclohexyl]-N-methylbutanamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000207
4-[4-[([1-[3-carbamimidoyl-N-(3'-fluoro[1,1'-biphenyl]-3-sulfonyl)-L-phenylalanyl]piperidin-4-yl]carbamoyl)amino]cyclohexyl]-N-methylbutanamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000072
4-[4-[([1-[3-carbamimidoyl-N-(4'-fluoro[1,1'-biphenyl]-3-sulfonyl)-L-phenylalanyl]piperidin-4-yl]carbamoyl)amino]cyclohexyl]-N-methylbutanamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000821
5-oxo-N-(phenylmethanesulfonyl)-5-[4-(pyrimidin-2-yl)piperazin-1-yl]-D-norvalyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.001222
5-[4-[(benzyloxy)carbonyl]piperazin-1-yl]-5-oxo-N-(phenylmethanesulfonyl)-D-norvalyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000624
benzyl 4-[(3R)-4-[(2S)-2-[[(4-carbamimidoylphenyl)methyl]carbamoyl]pyrrolidin-1-yl]-4-oxo-3-[(phenylmethanesulfonyl)amino]butanoyl]piperazine-1-carboxylate
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.00022
D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.00009
D-homophenylalanyl-N-[(4-carbamimidoylphenyl)methyl]-L-alaninamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.00018
D-homophenylalanyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.00002
D-homotyrosinyl-N-[(4-carbamimidoylphenyl)methyl]-L-alaninamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.0029
D-phenylalanyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.00018
methyl 1-[3-carbamimidoyl-N-(naphthalene-2-sulfonyl)-L-phenylalanyl]piperidine-4-carboxylate
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000008
N-(3-[[(2S)-1-[4-(2-aminoethyl)piperidin-1-yl]-3-(3-carbamimidoylphenyl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000018
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-(4-[2-[(benzylcarbamoyl)amino]ethyl]piperidin-1-yl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000022
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-(4-[2-[(cyclohexylcarbamoyl)amino]ethyl]piperidin-1-yl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000011
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-(4-[2-[(ethylcarbamoyl)amino]ethyl]piperidin-1-yl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.00001
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-(4-[2-[(methylcarbamoyl)amino]ethyl]piperidin-1-yl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000007
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-(4-[2-[(phenylcarbamoyl)amino]ethyl]piperidin-1-yl)-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000021
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-[4-[(benzylcarbamoyl)amino]piperidin-1-yl]-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000006
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-[4-[(cyclohexylcarbamoyl)amino]piperidin-1-yl]-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.00041
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-[4-[(ethylcarbamoyl)amino]piperidin-1-yl]-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000081
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-[4-[(methylcarbamoyl)amino]piperidin-1-yl]-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000017
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-[4-[(phenylcarbamoyl)amino]piperidin-1-yl]-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000016
N-(3-[[(2S)-3-(3-carbamimidoylphenyl)-1-[4-[2-(carbamoylamino)ethyl]piperidin-1-yl]-1-oxopropan-2-yl]sulfamoyl]phenyl)-beta-alaninamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000123
N-(phenylmethanesulfonyl)-4-carbamimidoyl-D-phenylalanyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000706
N-(phenylmethanesulfonyl)-4-cyano-D-phenylalanyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.001637
N-(phenylmethanesulfonyl)-D-alanyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.007344
N-(phenylmethanesulfonyl)-D-alpha-aspartyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000335
N-(phenylmethanesulfonyl)-D-cyclohexylalanyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000393
N-(phenylmethanesulfonyl)-D-leucyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000166
N-(phenylmethanesulfonyl)-D-phenylalanyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000322
N-(phenylmethanesulfonyl)-D-valyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.001633
N-(phenylmethanesulfonyl)glycyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000101
N-[(4-carbamimidoylphenyl)methyl]-1-[(2R)-4-(morpholin-4-yl)-4-oxo-2-[(phenylmethanesulfonyl)amino]butanoyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000045
N-[(4-carbamimidoylphenyl)methyl]-1-[(2R)-4-oxo-2-[(phenylmethanesulfonyl)amino]-4-(piperazin-1-yl)butanoyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000244
N-[(4-carbamimidoylphenyl)methyl]-1-[(2R)-4-oxo-2-[(phenylmethanesulfonyl)amino]-4-[4-(propan-2-yl)piperazin-1-yl]butanoyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000838
N-[(4-carbamimidoylphenyl)methyl]-1-[(2R)-4-oxo-2-[(phenylmethanesulfonyl)amino]-4-[4-(pyrimidin-2-yl)piperazin-1-yl]butanoyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000417
N-[(4-carbamimidoylphenyl)methyl]-1-[(2R)-4-[4-(2-hydroxyethyl)piperazin-1-yl]-4-oxo-2-[(phenylmethanesulfonyl)amino]butanoyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000111
N-[(4-carbamimidoylphenyl)methyl]-1-[(2R)-4-[4-(3,5-dimethylphenyl)piperazin-1-yl]-4-oxo-2-[(phenylmethanesulfonyl)amino]butanoyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000248
N-[(4-carbamimidoylphenyl)methyl]-1-[(2R)-4-[4-[3-(dimethylamino)propyl]piperazin-1-yl]-4-oxo-2-[(phenylmethanesulfonyl)amino]butanoyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000074
N-[3-([(2S)-3-(3-carbamimidoylphenyl)-1-[4-(carbamoylamino)piperidin-1-yl]-1-oxopropan-2-yl]sulfamoyl)phenyl]-beta-alaninamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000052
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-2-aminobutanoylamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000018
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-alaninamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000025
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-argininamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000499
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-isoleucinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000272
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-leucinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000068
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-norvalinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.00021
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-phenylalaninamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000019
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000143
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-serinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000409
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-valinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000068
N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]glycinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.00006
N2-(phenylmethanesulfonyl)-D-arginyl-N-[[2-(aminomethyl)-5-chlorophenyl]methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.00005
N2-(phenylmethanesulfonyl)-D-arginyl-N6-[(benzyloxy)carbonyl]-N-[(4-carbamimidoylphenyl)methyl]-L-lysinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000021
N2-(phenylmethanesulfonyl)-D-homoarginyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.00005
N2-(phenylmethanesulfonyl)-D-homophenylalanyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.00002
N2-(phenylmethanesulfonyl)-D-lysyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000019
N2-(phenylmethanesulfonyl)-N-tert-butoxy-D-asparaginyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000184
N2-(phenylmethanesulfonyl)-N6-(benzyloxycarbonyl)-D-lysyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.00023
N2-(phenylmethanesulfonyl)-O-(tert-butyl)-D-glutamyl-N-[(4-carbamimidoylphenyl)methyl]-L-prolinamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.000738
tert-butyl N2-(phenylmethanesulfonyl)-D-arginyl-N-[(4-carbamimidoylphenyl)methyl]-L-alpha-asparaginate
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.0000054
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(4'-chloro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
0.0000073
3-[(2S)-3-[4-[2-([[4-(2-aminoethyl)cyclohexyl]carbamoyl]amino)ethyl]piperidin-1-yl]-2-[(4'-chloro[1,1'-biphenyl]-3-sulfonyl)amino]-3-oxopropyl]benzene-1-carboximidamide
50 mM Tris/HCl buffer, pH 8.0, 22°C
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drug target
TMPRSS2 is a secreted protease that is highly expressed in prostate and prostate cancer, making it a potential target for cancer therapy and diagnosis
malfunction
TMPRSS2 knockdown in cultured human airway epithelial cells (H441) reduces baseline proteolytic activation of endogenously expressed epithelial sodium channel (ENaC)
metabolism
angiotensin-converting enzyme-2 (ACE2) and the transmembrane serine protease 2 (TMPRSS2) seem to be positively related to IFN-gamma and TNF-alpha production in chronic rhinosinusitis patient. ACE2 and TMPRSS2 are co-expressed in the ciliated epithelium of their paranasal mucosa, implicating the paranasal epithelium as a portal for initial infection and transmission
physiological function
ACE2 processing by TMPRSS2 or HAT is required for augmentation of SARS-S-driven entry. In contrast, ACE2 cleavage is dispensable for activation of the viral S protein. Expression of TMPRSS2 increases cellular uptake of soluble SARS-S. TMPRSS2 competes with the metalloprotease ADAM17 for ACE2 processing, but only cleavage by TMPRSS2 results in augmented SARS-S-driven entry
physiological function
-
acute oxidative stress leads to redistribution of TMPRSS2 from cell membrane to cytoplasm in IPEC-J2 cells
physiological function
after experimental infectionusing MERS coronavirus, TMPRSS2-deficient mouse strains show reduced body weight loss and viral kinetics in the lungs. Lack of TMPRSS2 affects the primary sites of infection and virus spread within the airway, accompanied by less severe immunopathology. TMPRSS2-KO mice show weakened inflammatory chemokine and/or cytokine responses to intranasal stimulation with poly(IC), a Toll-like receptor 3 agonist
physiological function
after infection of Tmprss2 knockout mice with an H3N2 influenza virus, only a slight increase in survival is observed. Tmprss2-/- Tmprss4-/-x02double-knockout mice show a remarkably reduced virus spread and lung pathology, in addition to reduced body weight loss and mortality
physiological function
angiotensin-converting enzyme ACE2 and TMPRSS2 colocalize on cell surfaces and enhance the cell entry of both SARS S-pseudotyped HIV and authentic SARS-CoV. Enhanced entry correlates with TMPRSS2-mediated proteolysis of both S protein and ACE2
physiological function
-
both proteases HAT and TMPRSS2 are coexpressed with 2,6-linked sialic acids, the major receptor determinant of human influenza viruses, throughout the human respiratory tract. Coexpression of ACE2 and TMPRSS2 is frequently found in the upper and lower aerodigestive tract, with the exception of the vocal folds, epiglottis and trachea. Activation of influenza virus is conserved between human, avian and porcine TMPRSS2
physiological function
both proteases HAT and TMPRSS2 are coexpressed with 2,6-linked sialic acids, the major receptor determinant of human influenza viruses, throughout the human respiratory tract. Coexpression of ACE2 and TMPRSS2 is frequently found in the upper and lower aerodigestive tract, with the exception of the vocal folds, epiglottis and trachea. Activation of influenza virus is conserved between human, avian and porcine TMPRSS2
physiological function
compared to wild-type littermates, Tmprss2-/- mice develop normally, survive to adulthood with no differences in protein levels of prostatic secretions, and exhibit no discernible abnormalities in organ histology or function. Loss of TMPRSS2 activity does not influence fertility, reduce survival, result in prostate hyperplasia or carcinoma, or alter prostatic luminal epithelial cell regrowth following castration and androgen replacement
physiological function
cotransfection of mammalian cells with plasmids encoding hemagglutinin of influenza viruses and protease TMPRSS2 or HAT results in hemagglutinin cleavage in situ. Transient expression of either protease in MDCK cells enables multicycle replication of influenza viruses in these cells in the absence of exogenous trypsin
physiological function
-
expression of TMPRSS2 supports multicycle growth of H5 highly pathogenic avian influenza viruses recombinant vaccines Re-5 and Re-6 and H9 avian influenza virus recombinant vaccine Re-9 in the absence of trypsin
physiological function
hemagglutinin is cleaved by membrane-bound TMPRSS2 and protease HAT and not by soluble forms released into the supernatant. TMPRSS2 cleaves newly synthesized hemagglutinin within the cell and is not able to support the proteolytic activation of hemagglutinin of incoming virions. Cleavage activation of hemagglutinin and virus spread in TMPRSS2-expressing cells can be suppressed by peptide mimetic protease inhibitors
physiological function
Huh7-25-CD81 cell clones stably expressing TMPRSS2- wild-type and inactive TMPRSS2-mutant genes show positive and negative enhancement of their susceptibility to cell-culture-derived hepatitis C virus infection, respectively. The cell-surface protease activity of TMPRSS2-wild-type cells is markedly active in the cleavage of peptides QAR and QGR
physiological function
in Vero cells expressing TMPRSS2, large syncytia are induced by SARS-CoV infection. Lysosome-tropic reagents fail to inhibit, whereas the heptad repeat peptide efficiently inhibits viral entry into cells. Production of virus in TMPRSS2-expressing cells does not result in S-protein cleavage or increased infectivity of the resulting virus. TMPRSS2 needs to be expressed in the opposing (target) cell membrane to activate S protein rather than in the producer cell
physiological function
knockdown of active TMPRSS2 using a phosphorodiamidate morpholino oligomer that interferes with splicing of TMPRSS2 pre-mRNA prevents proteolytic activation and multiplication of influenza virus H7N9 IAV in Calu-3 cells and viruses H1N1pdm, H7N9, and H3N2 IAV in primary human bronchial epithelial cells and primary type II alveolar epithelial cells. Phosphorodiamidate morpholino oligomer treatment also inhibits the activation and spread of influenza B virus in primary type II alveolar epithelial cells but does not affect influenza B virus activation in primary human bronchial epithelial cells and Calu-3 cells
physiological function
MDCK cells with inducible expression of either TMPRSS2 or protease HAT support growth of human and avian influenza viruses of different subtypes in the absence of exogenous trypsin. Multicycle viral replication in both cell lines is markedly suppressed in the presence of serine protease inhibitors
physiological function
overexpression of the cell surface protease TMPRSS2 greatly enhances entry of the highly neurovirulent mouse hepatitis virus strain JHM.SD to host cells. TMPRSS2 overexpression decreases mouse hepatitis virus structural protein expression, release of infectious particles, and syncytium formation, and endogenous serine protease activity does not contribute greatly to infection, while inhibition of matrix metalloproteinase and a disintegrin and metalloprotease-family zinc metalloproteases markedly decreases both entry and cell-cell fusion
physiological function
pre-cleavage of the S-protein substrate at the S1/S2 motif (RSVR) is important although not essential for subsequent MERS-S activation by TMPRSS2. The S2' site (RSAR) is required for robust viral entry into all cell lines tested and the integrity of one of the two arginines is sufficient for efficient entry. Cleavage at S2' is carried out by proteases recognizing a single arginine, most likely TMPRSS2 and cathepsin L. Mutation of the proposed cathepsin L site does not impact viral entry and double mutation of S1/S2 and S2' site is compatible with cathepsin L- but not TMPRSS2-dependent host cell entry
physiological function
prostate cancer cells show a high prevalence of TMPRSS2-ERG rearrangements which leads to androgenic induction of the ETS-related gene (ERG) expression. ERG knockdown in TMPRSS2-ERG expressing CaP cells induces striking morphological changes and inhibits cell growth. ERG mediates activation of C-MYC oncogene and the repression of prostate epithelial differentiation genes PSA and SLC45A3/prostein
physiological function
proteases TMPRSS2 and HAT cleave the HCoV-229E spike protein (229E-S) and augment 229E-S-driven cell-cell fusion. Engineered expression of TMPRSS2 and HAT renders 229E-S-driven virus-cell fusion insensitive to an inhibitor of cathepsin L. Activation by TMPRSS2 rescues 229E-S-dependent cell entry from inhibition by interferon-inducible host cell IFITM proteins. TMPRSS2 is coexpressed with CD13, the HCoV-229E receptor, in human airway epithelial cells, and CD13+ TMPRSS2+ cells are preferentially targeted by HCoV-229E
physiological function
replication of serotype I feline infectious peritonitis virus is enhanced by ectopic expression of host serine protease, TMPRSS2
physiological function
SARS spike (S) protein is cleaved into several fragments upon coexpression of TMPRSS2 (cis-cleavage) and upon contact between SARS S-expressing cells and TMPRSS2-positive cells (trans-cleavage). cis-Cleavage results in release of SARS S fragments into the cellular supernatant and in inhibition of antibody-mediated neutralization. trans-Cleavage activates SARS S on effector cells for fusion with target cells and allows efficient SARS S-driven viral entry into targets treated with a lysosomotropic agent or a cathepsin inhibitor. ACE2, the cellular receptor for SARSCoV, and TMPRSS2 are coexpressed by type II pneumocytes
physiological function
the knockout of androgen receptor-activated enhancers E1 or E2 simultaneously impairs the transcription of long noncoding RNA prostate cancer-associated transcript PRCAT38 and TMPRSS2 and inhibits cell growth and migration. E1 and E2 show chromatin looping with the promoters for PRCAT38 and TMPRSS2. The loop formation and enhancer activity are mediated by AR/FOXA1 binding and the activity of acetyltransferase p300
physiological function
TMPRSS2 cleaves SARS-spike protein S at multiple sites and activates SARS-S only in trans. TMPRSS2 expression renders SARS-S-driven virus-cell fusion independent of cathepsin activity
physiological function
TMPRSS2 isoform 1 colocalizes with influenza A virus hemagglutinin and cleaves and activates hemagglutinin. Isoform 1 activates the SARS-CoV spike protein for cathepsin L-independent entry into target cells
physiological function
TMPRSS2 silencing significantly abrogates dihydrotestosteron-induced prostate cancer cell invasion
physiological function
treatment of cells with a peptide-conjugated phosphorodiamidate morpholino oligomer designed to interfere with TMPRSS2 pre-mRNA splicing results in TMPRSS2 mRNA lacking exon 5 and consequently the expression of a truncated and enzymatically inactive form of TMPRSS2. Altered splicing of TMPRSS2 mRNA by the peptide-conjugated phosphorodiamidate morpholino oligomer prevents hemagglutinin cleavage in different human seasonal and pandemic influenza A viruses and suppresses viral titers by 2 to 3 log10 units
physiological function
treatment of LNCaP cells with a cellular immunopurified TMPRSS2 protease induces a transient increase in intracellular calcium. This calcium mobilization is inhibited by cellular pretreatment with a specific PAR-2 antagonist and also by cellular pretreatment with suramin or 2-APB (2-aminoethoxydiphenyl borate)
physiological function
upregulation of TMPRSS2 and downregulation of Forkhead box A1 Foxa1 in the medial amygdala of neonatal male rats that are subcutaneously administered with bisphenol A
physiological function
Vero cells constitutively expressing TMPRSS2 show larger syncytia at 18 h after infection with Middle East respiratory syndrome coronavirus MERS-CoV than after infection with other coronaviruses. The susceptibility of Vero-TMPRSS2 cells to MERS-CoV is 100fold higher than that of non-TMPRSS2-expressing parental Vero cells. Simultaneous treatment with inhibitors of cathepsin L and TMPRSS2 completely blocks virus entry into Vero-TMPRSS2 cells. A single camostat treatment suppresses MERS-CoV entry into human bronchial submucosal gland-derived Calu-3 cells by 10fold and virus growth by 270fold
physiological function
SARS-CoV-2 uses TMPRSS2 for priming its spike protein to infect target cells. SMYD2 inhibition downregulates TMPRSS2 and blocks viral replication
physiological function
the coexpression of ACE2 and TMPRSS2 proteins in the MII oocytes, zygotes, and BLs demonstrates that these gametes and embryos have the cellular machinery required and, thus, are potentially susceptible to SARS-CoV-2 infection if exposed to the virus
physiological function
the enzyme is responsible for priming the SARS-CoV-2 spike protein
physiological function
TMPRSS2 is likely to contribute to proteolytic epithelial sodium channel (ENaC) activation in epithelial tissues in vivo
physiological function
-
TMPRSS2 is the canonical protease mediating cellular entry for coronaviruses, including SARS-CoV-2
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Yamamoto, M.; Matsuyama, S.; Li, X.; Takeda, M.; Kawaguchi, Y.; Inoue, J.I.; Matsuda, Z.
Identification of nafamostat as a potent inhibitor of Middle East respiratory syndrome coronavirus S protein-mediated membrane fusion using the split-protein-based cell-cell fusion assay
Antimicrob. Agents Chemother.
60
6532-6539
2016
Homo sapiens (O15393)
brenda
Wilson, S.; Greer, B.; Hooper, J.; Zijlstra, A.; Walker, B.; Quigley, J.; Hawthorne, S.
The membrane-anchored serine protease, TMPRSS2, activates PAR-2 in prostate cancer cells
Biochem. J.
388
967-972
2005
Homo sapiens (O15393)
brenda
Meyer, D.; Sielaff, F.; Hammami, M.; Boettcher-Friebertshaeuser, E.; Garten, W.; Steinmetzer, T.
Identification of the first synthetic inhibitors of the type II transmembrane serine protease TMPRSS2 suitable for inhibition of influenza virus activation
Biochem. J.
452
331-343
2013
Homo sapiens (O15393)
brenda
Wen, Z.; Wu, C.; Chen, W.; Zeng, X.; Shi, J.; Ge, J.; Chen, H.; Bu, Z.
Establishment of MDCK stable cell lines expressing TMPRSS2 and MSPL and their applications in propagating influenza vaccine viruses in absence of exogenous trypsin
Biotechnol. Res. Int.
2015
402628
2015
Homo sapiens
brenda
Lucas, J.M.; Heinlein, C.; Kim, T.; Hernandez, S.A.; Malik, M.S.; True, L.D.; Morrissey, C.; Corey, E.; Montgomery, B.; Mostaghel, E.; Clegg, N.; Coleman, I.; Brown, C.M.; Schneider, E.L.; Craik, C.; Simon, J.A.; Bedalov, A.; Nelson, P.S.
The androgen-regulated protease TMPRSS2 activates a proteolytic cascade involving components of the tumor microenvironment and promotes prostate cancer metastasis
Cancer Discov.
4
1310-1325
2014
Homo sapiens (O15393), Mus musculus (Q9JIQ8)
brenda
Ko, C.J.; Huang, C.C.; Lin, H.Y.; Juan, C.P.; Lan, S.W.; Shyu, H.Y.; Wu, S.R.; Hsiao, P.W.; Huang, H.P.; Shun, C.T.; Lee, M.S.
Androgen-induced TMPRSS2 activates matriptase and promotes extracellular matrix degradation, prostate cancer cell invasion, tumor growth, and metastasis
Cancer Res.
75
2949-2960
2015
Homo sapiens (O15393)
brenda
Chen, Z.; Song, X.; Li, Q.; Xie, L.; Guo, T.; Su, T.; Tang, C.; Chang, X.; Liang, B.; Huang, D.
Androgen receptor-activated enhancers simultaneously regulate oncogene TMPRSS2 and lncRNA PRCAT38 in prostate cancer
Cells
8
864
2019
Homo sapiens (O15393)
brenda
Hayashi, H.; Kubo, Y.; Izumida, M.; Takahashi, E.; Kido, H.; Sato, K.; Yamaya, M.; Nishimura, H.; Nakayama, K.; Matsuyama, T.
Enterokinase enhances influenza A virus infection by activating trypsinogen in human cell lines
Front. Cell. Infect. Microbiol.
8
91
2018
Homo sapiens (O15393)
brenda
Ubuka, T.; Moriya, S.; Soga, T.; Parhar, I.
Identification of transmembrane protease serine 2 and forkhead box A1 as the potential bisphenol A responsive genes in the neonatal male rat brain
Front. Endocrinol. (Lausanne)
9
139
2018
Rattus norvegicus (Q6P7D7), Rattus norvegicus
brenda
Wang, S.; Zhang, Q.; Xu, D.; Pan, Y.; Lv, Y.; Chen, X.; Zuo, Y.; Yang, L.
Characterize the difference between TMPRSS2-ERG and non-TMPRSS2-ERG fusion patients by clinical and biological characteristics in prostate cancer
Gene
679
186-194
2018
Homo sapiens
brenda
Sabaliauskaite, R.; Jarmalaite, S.; Petroska, D.; Dasevicius, D.; Laurinavicius, A.; Jankevicius, F.; Lazutka, J.R.
Combined analysis of TMPRSS2-ERG and TERT for improved prognosis of biochemical recurrence in prostate cancer
Genes Chromosomes Cancer
51
781-791
2012
Homo sapiens (O15393)
brenda
Paoloni-Giacobino, A.; Chen, H.; Peitsch, M.C.; Rossier, C.; Antonarakis, S.E.
Cloning of the TMPRSS2 gene, which encodes a novel serine protease with transmembrane, LDLRA, and SRCR domains and maps to 21q22.3
Genomics
44
309-320
1997
Homo sapiens (O15393)
brenda
Esumi, M.; Ishibashi, M.; Yamaguchi, H.; Nakajima, S.; Tai, Y.; Kikuta, S.; Sugitani, M.; Takayama, T.; Tahara, M.; Takeda, M.; Wakita, T.
Transmembrane serine protease TMPRSS2 activates hepatitis C virus infection
Hepatology
61
437-446
2015
Homo sapiens (O15393), Homo sapiens
brenda
Paszti-Gere, E.; Barna, R.F.; Kovago, C.; Szauder, I.; Ujhelyi, G.; Jakab, C.; Meggyeshzi, N.; Szekacs, A.
Changes in the distribution of type II transmembrane serine protease, TMPRSS2 and in paracellular permeability in IPEC-J2 cells exposed to oxidative stress
Inflammation
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2015
Sus scrofa
brenda
Ferrara, F.; Molesti, E.; Boettcher-Friebertshaeuser, E.; Cattoli, G.; Corti, D.; Scott, S.D.; Temperton, N.J.
The human transmembrane protease serine 2 is necessary for the production of group 2 influenza A virus pseudotypes
J. Mol. Genet. Med.
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309-314
2012
Homo sapiens (O15393), Homo sapiens
brenda
Vaarala, M.H.; Porvari, K.S.; Kellokumpu, S.; Kyllnen, A.P.; Vihko, P.T.
Expression of transmembrane serine protease TMPRSS2 in mouse and human tissues
J. Pathol.
193
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2001
Homo sapiens (O15393), Mus musculus (Q9JIQ8)
brenda
Boettcher, E.; Matrosovich, T.; Beyerle, M.; Klenk, H.D.; Garten, W.; Matrosovich, M.
Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium
J. Virol.
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2006
Homo sapiens (O15393)
brenda
Matsuyama, S.; Nagata, N.; Shirato, K.; Kawase, M.; Takeda, M.; Taguchi, F.
Efficient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2
J. Virol.
84
12658-12664
2010
Homo sapiens (O15393)
brenda
Boettcher-Friebertshaeuser, E.; Freuer, C.; Sielaff, F.; Schmidt, S.; Eickmann, M.; Uhlendorff, J.; Steinmetzer, T.; Klenk, H.D.; Garten, W.
Cleavage of influenza virus hemagglutinin by airway proteases TMPRSS2 and HAT differs in subcellular localization and susceptibility to protease inhibitors
J. Virol.
84
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2010
Homo sapiens (O15393)
brenda
Bertram, S.; Glowacka, I.; Mueller, M.A.; Lavender, H.; Gnirss, K.; Nehlmeier, I.; Niemeyer, D.; He, Y.; Simmons, G.; Drosten, C.; Soilleux, E.J.; Jahn, O.; Steffen, I.; Poehlmann, S.
Cleavage and activation of the severe acute respiratory syndrome coronavirus spike protein by human airway trypsin-like protease
J. Virol.
85
13363-13372
2011
Homo sapiens (O15393), Homo sapiens
brenda
Boettcher-Friebertshaeuser, E.; Stein, D.A.; Klenk, H.D.; Garten, W.
Inhibition of influenza virus infection in human airway cell cultures by an antisense peptide-conjugated morpholino oligomer targeting the hemagglutinin-activating protease TMPRSS2
J. Virol.
85
1554-1562
2011
Homo sapiens (O15393)
brenda
Glowacka, I.; Bertram, S.; Mueller, M.A.; Allen, P.; Soilleux, E.; Pfefferle, S.; Steffen, I.; Tsegaye, T.S.; He, Y.; Gnirss, K.; Niemeyer, D.; Schneider, H.; Drosten, C.; Poehlmann, S.
Evidence that TMPRSS2 activates the severe acute respiratory syndrome coronavirus spike protein for membrane fusion and reduces viral control by the humoral immune response
J. Virol.
85
4122-4134
2011
Homo sapiens (O15393)
brenda
Shulla, A.; Heald-Sargent, T.; Subramanya, G.; Zhao, J.; Perlman, S.; Gallagher, T.
A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry
J. Virol.
85
873-882
2011
Homo sapiens (O15393), Homo sapiens
brenda
Abe, M.; Tahara, M.; Sakai, K.; Yamaguchi, H.; Kanou, K.; Shirato, K.; Kawase, M.; Noda, M.; Kimura, H.; Matsuyama, S.; Fukuhara, H.; Mizuta, K.; Maenaka, K.; Ami, Y.; Esumi, M.; Kato, A.; Takeda, M.
TMPRSS2 is an activating protease for respiratory parainfluenza viruses
J. Virol.
87
11930-11935
2013
Homo sapiens (O15393)
brenda
Shirato, K.; Kawase, M.; Matsuyama, S.
Middle East respiratory syndrome coronavirus infection mediated by the transmembrane serine protease TMPRSS2
J. Virol.
87
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2013
Homo sapiens (O15393)
brenda
Baron, J.; Tarnow, C.; Mayoli-Nuessle, D.; Schilling, E.; Meyer, D.; Hammami, M.; Schwalm, F.; Steinmetzer, T.; Guan, Y.; Garten, W.; Klenk, H.D.; Boettcher-Friebertshaeuser, E.
Matriptase, HAT, and TMPRSS2 activate the hemagglutinin of H9N2 influenza A viruses
J. Virol.
87
1811-1820
2013
Homo sapiens (O15393)
brenda
Gierer, S.; Bertram, S.; Kaup, F.; Wrensch, F.; Heurich, A.; Kraemer-Kuehl, A.; Welsch, K.; Winkler, M.; Meyer, B.; Drosten, C.; Dittmer, U.; von Hahn, T.; Simmons, G.; Hofmann, H.; Poehlmann, S.
The spike protein of the emerging betacoronavirus EMC uses a novel coronavirus receptor for entry, can be activated by TMPRSS2, and is targeted by neutralizing antibodies
J. Virol.
87
5502-5511
2013
Homo sapiens (O15393)
brenda
Bertram, S.; Dijkman, R.; Habjan, M.; Heurich, A.; Gierer, S.; Glowacka, I.; Welsch, K.; Winkler, M.; Schneider, H.; Hofmann-Winkler, H.; Thiel, V.; Poehlmann, S.
TMPRSS2 activates the human coronavirus 229E for cathepsin-independent host cell entry and is expressed in viral target cells in the respiratory epithelium
J. Virol.
87
6150-6160
2013
Homo sapiens (O15393)
brenda
Heurich, A.; Hofmann-Winkler, H.; Gierer, S.; Liepold, T.; Jahn, O.; Poehlmann, S.
TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein
J. Virol.
88
1293-1307
2014
Homo sapiens (O15393)
brenda
Kuehn, N.; Bergmann, S.; Koesterke, N.; Lambertz, R.L.O.; Keppner, A.; van den Brand, J.M.A.; Poehlmann, S.; Weiss, S.; Hummler, E.; Hatesuer, B.; Schughart, K.
The proteolytic activation of (H3N2) influenza A virus hemagglutinin is facilitated by different type II transmembrane serine proteases
J. Virol.
90
4298-4307
2016
Mus musculus (Q9JIQ8)
brenda
Shirato, K.; Kanou, K.; Kawase, M.; Matsuyama, S.
Clinical isolates of human coronavirus 229E bypass the endosome for cell entry
J. Virol.
91
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Homo sapiens (O15393), Homo sapiens
brenda
Phillips, J.M.; Gallagher, T.; Weiss, S.R.
Neurovirulent murine coronavirus JHM.SD uses cellular zinc metalloproteases for virus entry and cell-cell fusion
J. Virol.
91
e01564
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Homo sapiens (O15393)
brenda
Limburg, H.; Harbig, A.; Bestle, D.; Stein, D.A.; Moulton, H.M.; Jaeger, J.; Janga, H.; Hardes, K.; Koepke, J.; Schulte, L.; Koczulla, A.R.; Schmeck, B.; Klenk, H.D.; Boettcher-Friebertshaeuser, E.
TMPRSS2 is the major activating protease of influenza A virus in primary human airway cells and influenza B virus in human type II pneumocytes
J. Virol.
93
e00649
2019
Homo sapiens (O15393)
brenda
Iwata-Yoshikawa, N.; Okamura, T.; Shimizu, Y.; Hasegawa, H.; Takeda, M.; Nagata, N.
TMPRSS2 contributes to virus spread and immunopathology in the airways of murine models after coronavirus infection
J. Virol.
93
e01815
2019
Mus musculus (Q9JIQ8)
brenda
Kim, T.S.; Heinlein, C.; Hackman, R.C.; Nelson, P.S.
Phenotypic analysis of mice lacking the Tmprss2-encoded protease
Mol. Cell. Biol.
26
965-975
2006
Mus musculus (Q9JIQ8)
brenda
Sun, C.; Dobi, A.; Mohamed, A.; Li, H.; Thangapazham, R.L.; Furusato, B.; Shaheduzzaman, S.; Tan, S.H.; Vaidyanathan, G.; Whitman, E.; Hawksworth, D.J.; Chen, Y.; Nau, M.; Patel, V.; Vahey, M.; Gutkind, J.S.; Sreenath, T.; Petrovics, G.; Sesterhenn, I.A.; McLeod, D.G.; Srivastava, S.
TMPRSS2-ERG fusion, a common genomic alteration in prostate cancer activates C-MYC and abrogates prostate epithelial differentiation
Oncogene
27
5348-5353
2008
Homo sapiens (O15393)
brenda
Zmora, P.; Moldenhauer, A.S.; Hofmann-Winkler, H.; Poehlmann, S.
TMPRSS2 isoform 1 activates respiratory viruses and is expressed in viral target cells
PLoS ONE
10
e0138380
2015
Homo sapiens (O15393)
brenda
Reinke, L.M.; Spiegel, M.; Plegge, T.; Hartleib, A.; Nehlmeier, I.; Gierer, S.; Hoffmann, M.; Hofmann-Winkler, H.; Winkler, M.; Poehlmann, S.
Different residues in the SARS-CoV spike protein determine cleavage and activation by the host cell protease TMPRSS2
PLoS ONE
12
e0179177
2017
Homo sapiens (O15393)
brenda
Bertram, S.; Heurich, A.; Lavender, H.; Gierer, S.; Danisch, S.; Perin, P.; Lucas, J.M.; Nelson, P.S.; Poehlmann, S.; Soilleux, E.J.
Influenza and SARS-coronavirus activating proteases TMPRSS2 and HAT are expressed at multiple sites in human respiratory and gastrointestinal tracts
PLoS ONE
7
e35876
2012
Sus scrofa, Homo sapiens (O15393), Mus musculus (Q9JIQ8)
brenda
Kleine-Weber, H.; Elzayat, M.T.; Hoffmann, M.; Poehlmann, S.
Functional analysis of potential cleavage sites in the MERS-coronavirus spike protein
Sci. Rep.
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16597
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Homo sapiens (O15393)
brenda
Boettcher, E.; Freuer, C.; Steinmetzer, T.; Klenk, H.D.; Garten, W.
MDCK cells that express proteases TMPRSS2 and HAT provide a cell system to propagate influenza viruses in the absence of trypsin and to study cleavage of HA and its inhibition
Vaccine
27
6324-6329
2009
Homo sapiens (O15393)
brenda
Shirato, K.; Kawase, M.; Matsuyama, S
Wild-type human coronaviruses prefer cell-surface TMPRSS2 to endosomal cathepsins for cell entry
Virology
517
9-15
2018
Homo sapiens (O15393), Homo sapiens
brenda
Mettelman, R.C.; OBrien, A.; Whittaker, G.R.; Baker, S.C.
Generating and evaluating type I interferon receptor-deficient and feline TMPRSS2-expressing cells for propagating serotype I feline infectious peritonitis virus
Virology
537
226-236
2019
Felis catus (M3W8X2)
brenda
Bilinska, K.; Jakubowska, P.; Von Bartheld, C.S.; Butowt, R.
Expression of the SARS-CoV-2 entry proteins, ACE2 and TMPRSS2, in cells of the olfactory epithelium identification of cell types and trends with age
ACS Chem. Neurosci.
11
1555-1562
2020
Mus musculus
brenda
Kawasumi, T.; Takeno, S.; Ishino, T.; Ueda, T.; Hamamoto, T.; Takemoto, K.; Horibe, Y.; Takashi, O.
Co-expression and localization of angiotensin-converting enzyme-2 (ACE2) and the transmembrane serine protease 2 (TMPRSS2) in paranasal ciliated epithelium of patients with chronic rhinosinusitis
Am. J. Rhinol. Allergy
36
313-322
2022
Homo sapiens (O15393)
brenda
Afar, D.E.; Vivanco, I.; Hubert, R.S.; Kuo, J.; Chen, E.; Saffran, D.C.; Raitano, A.B.; Jakobovits, A.
Catalytic cleavage of the androgen-regulated TMPRSS2 protease results in its secretion by prostate and prostate cancer epithelia
Cancer Res.
61
1686-1692
2001
Homo sapiens (O15393)
brenda
Yu, Y.; Herrmann, A.; Thonn, V.; Cordsmeier, A.; Neurath, M.; Ensser, A.; Becker, C.
SMYD2 inhibition downregulates TMPRSS2 and decreases SARS-CoV-2 infection in human intestinal and airway epithelial cells
Cells
11
1262
2022
Homo sapiens (O15393)
brenda
Rajput, S.K.; Logsdon, D.M.; Kile, B.; Engelhorn, H.J.; Goheen, B.; Khan, S.; Swain, J.; McCormick, S.; Schoolcraft, W.B.; Yuan, Y.; Krisher, R.L.
Human eggs, zygotes, and embryos express the receptor angiotensin 1-converting enzyme 2 and transmembrane serine protease 2 protein necessary for severe acute respiratory syndrome coronavirus 2 infection
F S Sci.
2
33-42
2021
Homo sapiens (C9JKZ3), Homo sapiens
brenda
Jacquinet, E.; Rao, N.V.; Rao, G.V.; Hoidal, J.R.
Cloning, genomic organization, chromosomal assignment and expression of a novel mosaic serine proteinase epitheliasin
FEBS Lett.
468
93-100
2000
Mus musculus (Q9JIQ8), Mus musculus
brenda
Sure, F.; Bertog, M.; Afonso, S.; Diakov, A.; Rinke, R.; Madej, M.G.; Wittmann, S.; Gramberg, T.; Korbmacher, C.; Ilyaskin, A.V.
Transmembrane serine protease 2 (TMPRSS2) proteolytically activates the epithelial sodium channel (ENaC) by cleaving the channels gamma-subunit
J. Biol. Chem.
298
102004
2022
Homo sapiens (C9JKZ3)
brenda
Schuler, B.A.; Habermann, A.C.; Plosa, E.J.; Taylor, C.J.; Jetter, C.; Negretti, N.M.; Kapp, M.E.; Benjamin, J.T.; Gulleman, P.; Nichols, D.S.; Braunstein, L.Z.; Hackett, A.; Koval, M.; Guttentag, S.H.; Blackwell, T.S.; Webber, S.A.; Banovich, N.E.; Banovich, N.E.; Banovich, N.E.; Kropski, J.A.; Sucre, J.M.
Age-determined expression of priming protease TMPRSS2 and localization of SARS-CoV-2 in lung epithelium
J. Clin. Invest.
131
e140766
2021
Homo sapiens (C9JKZ3), Mus musculus
brenda
Ohnishi, T.; Nakamura, T.; Shima, K.; Noguchi, K.; Chiba, N.; Matsuguchi, T.
Periodontitis promotes the expression of gingival transmembrane serine protease 2 (TMPRSS2), a priming protease for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)
J. Oral Biosci.
64
229-236
2022
Homo sapiens (C9JKZ3)
brenda