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(1R,2S)-2-([4-[3-(aminomethyl)anilino]quinazolin-2-yl]amino)cyclohexane-1-carboxylic acid
-
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(2-fluoro-3-trifluoromethoxyphenyl)-amide]
-
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(2-fluoro-3-trifluoromethylphenyl)-amide]
-
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(3-chlorophenyl)-amide]
-
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(3-difluoromethoxyphenyl)-amide]
-
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(3-methoxyphenyl)-amide]
-
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(3-trifluoromethoxyphenyl)-amide]
-
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 3-[(3-bromophenyl)amide] 2-[(1-carbamoyl-1H-indol-3-yl)amide]
-
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 3-[(6-bromo-pyridin-2-yl)-amide] 2-[(1-carbamoyl-1H-indol-3-yl)-amide]
-
(1R,3S,5R)-2-azabicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(6-trifluoromethyl-pyridin-2-yl)-amide]
-
(1S,2S,5R)-3-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 3-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(2S)-2-([4-[3-(aminomethyl)anilino]pyrimidin-2-yl]amino)-3-methylbutanoic acid
-
(2S)-2-([4-[3-(aminomethyl)anilino]quinazolin-2-yl]amino)-3-methylbutanoic acid
-
(2S)-N2-(diphenylmethyl)-N1-(1-methyl-1H-indol-3-yl)pyrrolidine-1,2-dicarboxamide
-
(2S,4R)-4-fluoro-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxy-phenyl)-amide]
-
(2S,4R)-4-methyl-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(2S,4S)-4-amino-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(2S,4S)-4-fluoro-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(2S,4S)-4-hydroxy-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(2S,4S)-4-methyl-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxy-phenyl)-amide
-
(R)-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(S)-4,4-difluoro-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(S)-piperidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(S)-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
(S)-pyrrolidine-1,2-dicarboxylic acid 1-[(1-methyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
-
1-(2-((1R,3S,5R)-3-((6-bromopyridin-2-yl)carbamoyl)-2-azabicyclo[3.1.0]hexan-2-yl)-2-oxoethyl)-1H-indazole-3-carboxamide
-
1-(2-[(1R,3S,5R)-3-[(6-bromopyridin-2-yl)carbamoyl]-2-azabicyclo[3.1.0]hexan-2-yl]-2-oxoethyl)-1H-indazole-3-carboxamide
-
1-[2-[(1R,3S,5R)-3-[[(1R)-1-(3-chloro-2-fluorophenyl)ethyl]carbamoyl]-2-azabicyclo[3.1.0]hexan-2-yl]-2-oxoethyl]-1H-indazole-3-carboxamide
-
1-[2-[(1R,3S,5R)-3-[[(1R)-1-(3-chloro-2-fluorophenyl)ethyl]carbamoyl]-2-azabicyclo[3.1.0]hexan-2-yl]-2-oxoethyl]-1H-pyrazolo[3,4-c]pyridine-3-carboxamide
-
3'-(aminomethyl)-5-(3-methylbutanamido)-N-(1,2,3,4-tetrahydronaphthalen-1-yl)[1,1'-biphenyl]-3-carboxamide (incorrect configuration definition!)
-
3'-(aminomethyl)-N-benzyl[1,1'-biphenyl]-3-carboxamide
-
3'-(aminomethyl)-N-[(1R)-1,2,3,4-tetrahydronaphthalen-1-yl][1,1'-biphenyl]-3-carboxamide
-
3'-(aminomethyl)-N-[(1S)-1,2,3,4-tetrahydronaphthalen-1-yl][1,1'-biphenyl]-3-carboxamide
3,4-dichloroisocoumarin
-
mechanism-based inactivation
3-([3-[3-(aminomethyl)anilino]-1H-pyrazolo[3,4-d]pyrimidin-4-yl]amino)phenol
-
3-[[(2-carbamoyl-1H-indol-5-yl)oxy]methyl]benzoic acid
anti-factor D Fab fragment
-
diisopropyl fluorophosphate
-
-
methyl 2-([[(2S)-2-[[3-(trifluoromethoxy)phenyl]carbamoyl]pyrrolidine-1-carbonyl]amino]methyl)benzoate
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]-2-phenylacetamide
-
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]-3-methylbutanamide
-
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]-3-phenylpropanamide
-
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]acetamide
-
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]benzamide
-
[2-([3'-[(1S)-1-amino-2-hydroxyethyl][1,1'-biphenyl]-3-yl]methoxy)phenyl]acetic acid
selective inhibitor
3'-(aminomethyl)-N-[(1S)-1,2,3,4-tetrahydronaphthalen-1-yl][1,1'-biphenyl]-3-carboxamide
-
3'-(aminomethyl)-N-[(1S)-1,2,3,4-tetrahydronaphthalen-1-yl][1,1'-biphenyl]-3-carboxamide
-
-
3-[[(2-carbamoyl-1H-indol-5-yl)oxy]methyl]benzoic acid
-
3-[[(2-carbamoyl-1H-indol-5-yl)oxy]methyl]benzoic acid
-
-
anti-factor D Fab fragment
an Escherichia coli-expressed, humanized Fab fragment, derived from monoclonal antibody 166-32, and designed as specific enzyme inhibitor targeting the exosite. Anti-factor D Fab fragment prevents factor D-mediated proteolytic activation of its macromolecular substrate C3bB, but not proteolysis of a small synthetic substrate, indicating that the inhibitor does not block access of the substrate to the catalytic site, binding structure and inhibitory mechanism, overview. The structures show that the AFD-binding site includes surface loops of the enzyme that form part of the enzyme's exosite. Anti-factor D Fab fragment inhibits the enzyme proteolytic function by interfering with macromolecular substrate access rather than by inhibiting the enzyme catalysis
-
anti-factor D Fab fragment
-
an Escherichia coli-expressed, humanized Fab fragment, derived from monoclonal antibody 166-32, and designed as specific enzyme inhibitor targeting the exosite. Anti-factor D Fab fragment prevents factor D-mediated proteolytic activation of its macromolecular substrate C3bB, but not proteolysis of a small synthetic substrate, indicating that the inhibitor does not block access of the substrate to the catalytic site, binding structure and inhibitory mechanism, overview. The structures show that the AFD-binding site includes surface loops of the enzyme that form part of the enzyme's exosite. Anti-factor D Fab fragment inhibits the enzyme proteolytic function by interfering with macromolecular substrate access rather than by inhibiting the enzyme catalysis
-
methyl 2-([[(2S)-2-[[3-(trifluoromethoxy)phenyl]carbamoyl]pyrrolidine-1-carbonyl]amino]methyl)benzoate
-
methyl 2-([[(2S)-2-[[3-(trifluoromethoxy)phenyl]carbamoyl]pyrrolidine-1-carbonyl]amino]methyl)benzoate
-
-
additional information
human factor D is a self-inhibited thrombin-like serine proteinase. Ser199 of the self-inhibitory loop blocks the formation of the canonical active configurations
-
additional information
-
human factor D is a self-inhibited thrombin-like serine proteinase. Ser199 of the self-inhibitory loop blocks the formation of the canonical active configurations
-
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0.084
(1R,2S)-2-([4-[3-(aminomethyl)anilino]quinazolin-2-yl]amino)cyclohexane-1-carboxylic acid
Homo sapiens
at pH 7.5 and 25°C
0.000012
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(2-fluoro-3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.000023
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(2-fluoro-3-trifluoromethylphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.00015
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(3-chlorophenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.00015
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(3-difluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.00032
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(3-methoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.00005
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.000045
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 3-[(3-bromophenyl)amide] 2-[(1-carbamoyl-1H-indol-3-yl)amide]
Homo sapiens
at pH 7.5 and 25°C
0.000006
(1R,3S,5R)-2-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 3-[(6-bromo-pyridin-2-yl)-amide] 2-[(1-carbamoyl-1H-indol-3-yl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.000014
(1R,3S,5R)-2-azabicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(6-trifluoromethyl-pyridin-2-yl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.00065
(1S,2S,5R)-3-aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 3-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.044
(2S)-2-([4-[3-(aminomethyl)anilino]pyrimidin-2-yl]amino)-3-methylbutanoic acid
Homo sapiens
at pH 7.5 and 25°C
0.075
(2S)-2-([4-[3-(aminomethyl)anilino]quinazolin-2-yl]amino)-3-methylbutanoic acid
Homo sapiens
at pH 7.5 and 25°C
0.0058
(2S)-N2-(diphenylmethyl)-N1-(1-methyl-1H-indol-3-yl)pyrrolidine-1,2-dicarboxamide
Homo sapiens
at pH 7.5 and 25°C
0.00005
(2S,4R)-4-fluoro-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxy-phenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.00085
(2S,4R)-4-methyl-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.0005
(2S,4S)-4-amino-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.0007
(2S,4S)-4-fluoro-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.0014
(2S,4S)-4-hydroxy-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.0003
(2S,4S)-4-methyl-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxy-phenyl)-amide
Homo sapiens
at pH 7.5 and 25°C
0.03
(R)-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.00045
(S)-4,4-difluoro-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.022
(S)-piperidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.0005
(S)-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.02
(S)-pyrrolidine-1,2-dicarboxylic acid 1-[(1-methyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxyphenyl)-amide]
Homo sapiens
at pH 7.5 and 25°C
0.000006
1-(2-[(1R,3S,5R)-3-[(6-bromopyridin-2-yl)carbamoyl]-2-azabicyclo[3.1.0]hexan-2-yl]-2-oxoethyl)-1H-indazole-3-carboxamide
Homo sapiens
at pH 7.5 and 25°C
0.000017
1-[2-[(1R,3S,5R)-3-[[(1R)-1-(3-chloro-2-fluorophenyl)ethyl]carbamoyl]-2-azabicyclo[3.1.0]hexan-2-yl]-2-oxoethyl]-1H-pyrazolo[3,4-c]pyridine-3-carboxamide
Homo sapiens
at pH 7.5 and 25°C
0.0034
3'-(aminomethyl)-5-(3-methylbutanamido)-N-(1,2,3,4-tetrahydronaphthalen-1-yl)[1,1'-biphenyl]-3-carboxamide (incorrect configuration definition!)
Homo sapiens
at pH 7.5 and 25°C
0.31
3'-(aminomethyl)-N-benzyl[1,1'-biphenyl]-3-carboxamide
Homo sapiens
at pH 7.5 and 25°C
0.098
3'-(aminomethyl)-N-[(1R)-1,2,3,4-tetrahydronaphthalen-1-yl][1,1'-biphenyl]-3-carboxamide
Homo sapiens
at pH 7.5 and 25°C
0.037 - 0.054
3'-(aminomethyl)-N-[(1S)-1,2,3,4-tetrahydronaphthalen-1-yl][1,1'-biphenyl]-3-carboxamide
0.02
3-([3-[3-(aminomethyl)anilino]-1H-pyrazolo[3,4-d]pyrimidin-4-yl]amino)phenol
Homo sapiens
at pH 7.5 and 25°C
0.014
methyl 2-([[(2S)-2-[[3-(trifluoromethoxy)phenyl]carbamoyl]pyrrolidine-1-carbonyl]amino]methyl)benzoate
0.043
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]-2-phenylacetamide
Homo sapiens
at pH 7.5 and 25°C
0.12
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]-3-methylbutanamide
Homo sapiens
at pH 7.5 and 25°C
0.14
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]-3-phenylpropanamide
Homo sapiens
at pH 7.5 and 25°C
0.69
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]acetamide
Homo sapiens
at pH 7.5 and 25°C
0.257
N-[3'-(aminomethyl)[1,1'-biphenyl]-3-yl]benzamide
Homo sapiens
at pH 7.5 and 25°C
0.000012
[2-([3'-[(1S)-1-amino-2-hydroxyethyl][1,1'-biphenyl]-3-yl]methoxy)phenyl]acetic acid
Homo sapiens
pH and temperature not specified in the publication
0.037
3'-(aminomethyl)-N-[(1S)-1,2,3,4-tetrahydronaphthalen-1-yl][1,1'-biphenyl]-3-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.054
3'-(aminomethyl)-N-[(1S)-1,2,3,4-tetrahydronaphthalen-1-yl][1,1'-biphenyl]-3-carboxamide
Homo sapiens
at pH 7.5 and 25°C
0.014
methyl 2-([[(2S)-2-[[3-(trifluoromethoxy)phenyl]carbamoyl]pyrrolidine-1-carbonyl]amino]methyl)benzoate
Homo sapiens
at pH 7.5 and 25°C
0.014
methyl 2-([[(2S)-2-[[3-(trifluoromethoxy)phenyl]carbamoyl]pyrrolidine-1-carbonyl]amino]methyl)benzoate
Homo sapiens
-
at pH 7.5 and 25°C
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Harper, J.W.; Hemmi, K.; Powers, J.C.
Reaction of serine proteases with substituted isocoumarins: discovery of 3,4-dichloroisocoumarin, a new general mechanism based serine protease inhibitor
Biochemistry
24
1831-1841
1985
Homo sapiens
brenda
Davis III, A.E.; Alper, C.A.
Factor D of the alternative complement pathway
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
5
549-553
1984
Homo sapiens
-
brenda
Reid, K.B.M.; Johnson, D.M.A.; Gagnon, J.; Prohaska, R.
Preparation of human factor D of the alternative pathway of complement
Methods Enzymol.
80
134-143
1981
Homo sapiens
brenda
Davies, A.E.; Zalut, C.; Rosen, F.S.; Alper, C.A.
Human factor D of the alternative complement pathway. Physicochemical characteristics and N-terminal amino acid sequence
Biochemistry
18
5082-5087
1979
Homo sapiens
brenda
Lesavre, P.H.; Hugli, T.E.; Esser, A.F.; Mller-Eberhard, H.J.
The alternative pathway C3/C5 convertase: chemical basis of factor B activation
J. Immunol.
123
529-534
1979
Homo sapiens
brenda
Volanakis, J.E.; Schrohenloher, R.E.; Stroud, R.M.
Human factor D of the alternative complement pathway: purification and characterization
J. Immunol.
119
337-342
1977
Homo sapiens
brenda
Jing, H.; Macon, K.J.; Moore, D.; DeLucas, L.J.; Volanakis, J.E.; Narayana, S.V.L.
Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D
EMBO J.
18
804-814
1999
Homo sapiens (P00746)
brenda
Balke, N.; Holtkamp, U.; Hrl, W.H.; Tschesche, H.
Inhibition of degranulation of human polymorphonuclear leukocytes by complement factor D
FEBS Lett.
371
300-302
1995
Homo sapiens
brenda
Kim, S.; Narayana, S.V.L.; Volanakis, J.E.
Crystal structure of a complement factor D mutant expressing enhanced catalytic activity [published erratum appears in J Biol Chem 1995 Dec 29;270(52):31414
J. Biol. Chem.
270
24399-24405
1995
Homo sapiens
brenda
Cole, L.B.; Chu, N.; Kilpatrick, J.M.; Volanakis, J.E.; Narayana, S.V.L.; Babu, Y.S.
Structure of diisopropyl fluorophosphate-inhibited factor D
Acta Crystallogr. Sect. D
53
143-150
1997
Homo sapiens
brenda
Jing, H.; Babu, Y.S.; Moore, D.; Kilpatrick, J.M.; Liu, X.Y.; Volanakis, J.E.; Narayana, S.V.L.
Structures of native and complexed complement factor D: implications of the atypical His57 conformation and self-inhibitory loop in the regulation of specific serine protease activity
J. Mol. Biol.
282
1061-1081
1998
Homo sapiens (P00746)
brenda
Catana, E.; Schifferli, J.A.
Purification of human complement factor D from the peritoneal fluid of patients on chronic ambulatory peritoneal dialysis
J. Immunol. Methods
138
265-271
1991
Homo sapiens
brenda
Miyata, T.; Oda, O.; Inagi, R.; Sugiyama, S.; Miyama, A.; Maeda, K.; Nakashima, I.; Yamanaka, N.
Molecular and functional identification and purification of complement component factor D from urine of patients with chronic renal failure
Mol. Immunol.
27
637-644
1990
Homo sapiens
brenda
Volanakis, J.E.; Barnum, S.R.; Kilpatrick, J.M.
Purification and properties of human factor D
Methods Enzymol.
223
82-97
1993
Homo sapiens
brenda
Kitano, E.; Kitamura, H.
Synthesis of factor D by normal human hepatocytes
Int. Arch. Allergy Immunol.
122
299-302
2000
Homo sapiens
brenda
Sprong, T.; Roos, D.; Weemaes, C.; Neeleman, C.; Geesing, C.L.; Mollnes, T.E.; van Deuren, M.
Deficient alternative complement pathway activation due to factor D deficiency by 2 novel mutations in the complement factor D gene in a family with meningococcal infections
Blood
107
4865-4870
2006
Homo sapiens
brenda
Oda, O.; Nagaya, T.; Ogawa, H.
Analysis of protein absorbed by LDL column (Liposorber) with special reference to complement component factor D
Clin. Chim. Acta
342
155-160
2004
Homo sapiens
brenda
Harris, C.L.; Abbott, R.J.; Smith, R.A.; Morgan, B.P.; Lea, S.M.
Molecular dissection of interactions between components of the alternative pathway of complement and decay accelerating factor (CD55)
J. Biol. Chem.
280
2569-2578
2005
Homo sapiens
brenda
Elliott, M.K.; Jarmi, T.; Ruiz, P.; Xu, Y.; Holers, V.M.; Gilkeson, G.S.
Effects of complement factor D deficiency on the renal disease of MRL/lpr mice
Kidney Int.
65
129-138
2004
Mus musculus
brenda
Recinos, A.; Carr, B.K.; Bartos, D.B.; Boldogh, I.; Carmical, J.R.; Belalcazar, L.M.; Brasier, A.R.
Liver gene expression associated with diet and lesion development in atherosclerosis-prone mice: induction of components of alternative complement pathway
Physiol. Genomics
19
131-142
2004
Mus musculus (P03953), Mus musculus
brenda
Lovoll, M.; Kilvik, T.; Boshra, H.; Bogwald, J.; Sunyer, J.O.; Dalmo, R.A.
Maternal transfer of complement components C3-1, C3-3, C3-4, C4, C5, C7, Bf, and Df to offspring in rainbow trout (Oncorhynchus mykiss)
Immunogenetics
58
168-179
2006
Oncorhynchus mykiss
brenda
Luginbuehl, A.; Nikolic, M.; Beck, H.P.; Wahlgren, M.; Lutz, H.U.
Complement factor D, albumin, and immunoglobulin G anti-band 3 protein antibodies mimic serum in promoting rosetting of malaria-infected red blood cells
Infect. Immun.
75
1771-1777
2007
Homo sapiens (P00746)
brenda
Li, L.; Liu, B.; Li, X.; Yang, S.; Xiao, J.; Chen, M.; Zhang, Y.; Ma, J.
Vascular endothelial growth factor D and intratumoral lymphatics as independent prognostic factors in epithelial ovarian carcinoma
Anat. Rec. (Hoboken)
292
562-569
2009
Homo sapiens (O43915), Homo sapiens
brenda
Schaefer, G.; Wissmann, C.; Hertel, J.; Lunyak, V.; Hoecker, M.
Regulation of vascular endothelial growth factor D by orphan receptors hepatocyte nuclear factor-4 alpha and chicken ovalbumin upstream promoter transcription factors 1 and 2
Cancer Res.
68
457-466
2008
Homo sapiens
brenda
Liu, G.; Changsirikulchai, S.; Hudkins, K.L.; Banas, M.C.; Kowalewska, J.; Yang, X.; Wietecha, T.A.; Volpone, J.; Gilbertson, D.G.; Alpers, C.E.
Identification of platelet-derived growth factor D in human chronic allograft nephropathy
Hum. Pathol.
39
393-402
2008
Homo sapiens
brenda
Toivanen, P.I.; Nieminen, T.; Viitanen, L.; Alitalo, A.; Roschier, M.; Jauhiainen, S.; Markkanen, J.E.; Laitinen, O.H.; Airenne, T.T.; Salminen, T.A.; Johnson, M.S.; Airenne, K.J.; Ylae-Herttuala, S.
Novel vascular endothelial growth factor D (VEGF-D) variants with increased biological activity
J. Biol. Chem.
284
16037-1648
2009
Homo sapiens (O43915)
brenda
Kinnunen, K.; Kalesnykas, G.; Maehoenen, A.J.; Laidinen, S.; Holma, L.; Heikura, T.; Airenne, K.; Uusitalo, H.; Ylae-Herttuala, S.
Baculovirus is an efficient vector for the transduction of the eye: comparison of baculovirus- and adenovirus-mediated intravitreal vascular endothelial growth factor D gene transfer in the rabbit eye
J. Gene Med.
11
382-389
2009
Homo sapiens
brenda
Ahmad, A.; Wang, Z.; Kong, D.; Ali, R.; Ali, S.; Banerjee, S.; Sarkar, F.H.
Platelet-derived growth factor-D contributes to aggressiveness of breast cancer cells by up-regulating Notch and NF-kappaB signaling pathways
Breast Cancer Res. Treat.
126
15-25
2011
Homo sapiens
brenda
Glasgow, C.G.; Avila, N.A.; Lin, J.P.; Stylianou, M.P.; Moss, J.
Serum vascular endothelial growth factor-D levels in patients with lymphangioleiomyomatosis reflect lymphatic involvement
Chest
135
1293-1300
2009
Homo sapiens
brenda
Ming, J.; Zhang, Q.; Qiu, X.; Wang, E.
Interleukin 7/interleukin 7 receptor induce c-Fos/c-Jun-dependent vascular endothelial growth factor-D up-regulation: a mechanism of lymphangiogenesis in lung cancer
Eur. J. Cancer
45
866-873
2009
Homo sapiens
brenda
Kong, H.J.; Hong, G.E.; Nam, B.H.; Kim, Y.O.; Kim, W.J.; Lee, S.J.; Lee, N.S.; Do, J.W.; Cho, H.K.; Cheong, J.; Lee, C.H.; Kim, K.K.
An immune responsive complement factor D/adipsin and kallikrein-like serine protease (PoDAK) from the olive flounder Paralichthys olivaceus
Fish Shellfish Immunol.
27
486-492
2009
Paralichthys olivaceus (C9D6Z6), Paralichthys olivaceus
brenda
Hu, J.; Ye, H.; Fu, A; Chen, X.; Wang, Y.; Chen, X.; Ye, X.; Xiao, W.; Duan, X.; Wei, Y.; Chen, L.
Deguelin-an inhibitor to tumor lymphangiogenesis and lymphatic metastasis by down-regulation of vascular endothelial cell growth factor-D in lung tumor model
Int. J. Cancer
127
2455-2466
2010
Homo sapiens
brenda
Takahashi, M.; Ishida, Y.; Iwaki, D.; Kanno, K.; Suzuki, T.; Endo, Y.; Homma, Y.; Fujita, T.
Essential role of mannose-binding lectin-associated serine protease-1 in activation of the complement factor D
J. Exp. Med.
207
29-37
2010
Mus musculus
brenda
Deng, J.; Liang, H.; Sun, D.; Pan, Y.; Wang, B.; Guo, Y.
Vascular endothelial growth factor-D is correlated with hepatic metastasis from gastric cancer after radical gastrectomy
Surgery
146
896-905
2009
Homo sapiens
brenda
Forneris, F.; Ricklin, D.; Wu, J.; Tzekou, A.; Wallace, R.; Lambris, J.; Gros, P.
Structures of C3b in complex with factors B and D give insight into complement convertase formation
Science
330
1816-1820
2010
Homo sapiens
brenda
Forneris, F.; Burnley, B.T.; Gros, P.
Ensemble refinement shows conformational flexibility in crystal structures of human complement factor D
Acta Crystallogr. Sect. D
70
733-743
2014
Homo sapiens (P00746), Homo sapiens
brenda
Katschke, K.J.; Wu, P.; Ganesan, R.; Kelley, R.F.; Mathieu, M.A.; Hass, P.E.; Murray, J.; Kirchhofer, D.; Wiesmann, C.; van Lookeren Campagne, M.
Inhibiting alternative pathway complement activation by targeting the factor D exosite
J. Biol. Chem.
287
12886-12892
2012
Macaca fascicularis, Homo sapiens (P00746), Homo sapiens
brenda
Degn, SE.; Jensenius, J.C.; Thiel, S.
The pro-Factor D cleaving activity of MASP-1/-3 is not required for alternative pathway function
J. Immunol.
192
5448-5449
2014
Mus musculus
brenda
Cresci, G.A.; Allende, D.; McMullen, M.R.; Nagy, L.E.
Alternative complement pathway component Factor D contributes to efficient clearance of tissue debris following acute CCl4-induced injury
Mol. Immunol.
64
9-17
2015
Mus musculus, Mus musculus C57BL/6
brenda
Vulpetti, A.; Ostermann, N.; Randl, S.; Yoon, T.; Mac Sweeney, A.; Cumin, F.; Lorthiois, E.; Ruedisser, S.; Erbel, P.; Maibaum, J.
Discovery and design of first benzylamine-based ligands binding to an unlocked conformation of the complement factor D
ACS Med. Chem. Lett.
9
490-495
2018
Homo sapiens (P00746)
brenda
McCullough, R.L.; McMullen, M.R.; Sheehan, M.M.; Poulsen, K.L.; Roychowdhury, S.; Chiang, D.J.; Pritchard, M.T.; Caballeria, J.; Nagy, L.E.
Complement factor D protects mice from ethanol-induced inflammation and liver injury
Am. J. Physiol. Gastrointest. Liver Physiol.
315
G66-G79
2018
Mus musculus
brenda
Ezure, T.; Sugahara, M.; Amano, S.
Senescent dermal fibroblasts negatively influence fibroblast extracellular matrix-related gene expression partly via secretion of complement factor D
Biofactors
45
556-562
2019
Homo sapiens (P00746)
brenda
Godahewa, G.I.; Perera, N.C.; Bathige, S.D.; Nam, B.H.; Noh, J.K.; Lee, J.
Complement factor D homolog involved in the alternative complement pathway of rock bream (Oplegnathus fasciatus) Molecular and functional characterization and immune responsive mRNA expression analysis
Fish Shellfish Immunol.
55
423-433
2016
Oplegnathus fasciatus
brenda
Ding, M.; Fan, J.; Wang, W.; Wang, H.; Liu, H.
Molecular characterization, expression and antimicrobial activity of complement factor D in Megalobrama amblycephala
Fish Shellfish Immunol.
89
43-51
2019
Megalobrama amblycephala
brenda
Huang, W.; Kim, H.R.
Dynamic regulation of platelet-derived growth factor D (PDGF-D) activity and extracellular spatial distribution by matriptase-mediated proteolysis
J. Biol. Chem.
290
9162-9170
2015
Homo sapiens
brenda
Lorthiois, E.; Anderson, K.; Vulpetti, A.; Rogel, O.; Cumin, F.; Ostermann, N.; Steinbacher, S.; Mac Sweeney, A.; Delgado, O.; Liao, S.M.; Randl, S.; Ruedisser, S.; Dussauge, S.; Fettis, K.; Kieffer, L.; de Erkenez, A.; Yang, L.; Hartwieg, C.; Argikar, U.A.; La Bonte, L.R.; Newton, R.; Kansara, V.; Flohr, S.; Hommel, U.; Jaffee, B.; Maibaum, J.
Discovery of highly potent and selective small-molecule reversible factor D inhibitors demonstrating alternative complement pathway inhibition in vivo
J. Med. Chem.
60
5717-5735
2017
Homo sapiens (P00746), Homo sapiens
brenda
Karki, R.G.; Powers, J.; Mainolfi, N.; Anderson, K.; Belanger, D.B.; Liu, D.; Ji, N.; Jendza, K.; Gelin, C.F.; Mac Sweeney, A.; Solovay, C.; Delgado, O.; Crowley, M.; Liao, S.M.; Argikar, U.A.; Flohr, S.; La Bonte, L.R.; Lorthiois, E.L.; Vulpetti, A.; Brown, A.; Long, D.; Prentiss, M.; Gradoux, N.; de Erkenez, A.; Cumin, F.; Adams, C.; Jaffe, B.; Mogi, M.
Design, synthesis, and preclinical characterization of selective factor D inhibitors targeting the alternative complement pathway
J. Med. Chem.
62
4656-4668
2019
Homo sapiens (P00746), Homo sapiens
brenda
Song, N.J.; Kim, S.; Jang, B.H.; Chang, S.H.; Yun, U.J.; Park, K.M.; Waki, H.; Li, D.Y.; Tontonoz, P.; Park, K.W.
Small molecule-induced complement factor D (adipsin) promotes lipid accumulation and adipocyte differentiation
PLoS ONE
11
e0162228
2016
Mus musculus (Q3UP47)
brenda