Structure analysis of the receptor binding of 2019-nCoV
Chen, Y.; Guo, Y.; Pan, Y.; Zhao, Z.; Biochem. Biophys. Res. Commun. FEHLT, 0000 (2020) 
Data extracted from this reference:
Application
Application
Commentary
Organism
medicine
antibodies and small molecular inhibitors that can block the interaction of the enzyme (ACE2) with the receptor binding domain can to combat the virus SARS-CoV-2
Homo sapiens
Organism
Organism
UniProt
Commentary
Textmining
Callorhinchus milii
XP_007889845.1
-
-
Homo sapiens
Q9BYF1
-
-
Nipponia nippon
A0A091UR55
-
-
Paguma larvata
Q56NL1
-
-
Protobothrops mucrosquamatus
XP_029140508.1
-
-
Rhinolophus sinicus
E2DHI7
-
-
Xenopus laevis
XP_018104311.1
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
intestine
predominantly expressed in intestines, testis, and kidney
Homo sapiens
-
kidney
predominantly expressed in intestines, testis, and kidney
Homo sapiens
-
lung
expression level of ACE2 in the lung is minimal
Homo sapiens
-
testis
predominantly expressed in intestines, testis, and kidney
Homo sapiens
-
Synonyms
Synonyms
Commentary
Organism
ACE2
-
Callorhinchus milii
ACE2
-
Nipponia nippon
ACE2
-
Protobothrops mucrosquamatus
ACE2
-
Rhinolophus sinicus
ACE2
-
Xenopus laevis
ACE2
-
Paguma larvata
ACE2
-
Homo sapiens
Application (protein specific)
Application
Commentary
Organism
medicine
antibodies and small molecular inhibitors that can block the interaction of the enzyme (ACE2) with the receptor binding domain can to combat the virus SARS-CoV-2
Homo sapiens
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
intestine
predominantly expressed in intestines, testis, and kidney
Homo sapiens
-
kidney
predominantly expressed in intestines, testis, and kidney
Homo sapiens
-
lung
expression level of ACE2 in the lung is minimal
Homo sapiens
-
testis
predominantly expressed in intestines, testis, and kidney
Homo sapiens
-
General Information
General Information
Commentary
Organism
drug target
antibodies and small molecular inhibitors that can block the interaction of the enzyme (ACE2) with the receptor binding domain can to combat the virus SARS-CoV-2
Homo sapiens
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Callorhinchus milii
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Homo sapiens
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Nipponia nippon
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Paguma larvata
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Protobothrops mucrosquamatus
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Rhinolophus sinicus
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Xenopus laevis
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Callorhinchus milii
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Homo sapiens
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Nipponia nippon
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Paguma larvata
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Protobothrops mucrosquamatus
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Rhinolophus sinicus
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Xenopus laevis
General Information (protein specific)
General Information
Commentary
Organism
drug target
antibodies and small molecular inhibitors that can block the interaction of the enzyme (ACE2) with the receptor binding domain can to combat the virus SARS-CoV-2
Homo sapiens
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Callorhinchus milii
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Homo sapiens
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Nipponia nippon
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Paguma larvata
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Protobothrops mucrosquamatus
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Rhinolophus sinicus
evolution
ACE2 is widely expressed in the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Remarkably, its structure is highly conserved. Comparison of human ACE2 with that of a civet (Paguma larvata), a bat (Rhinolophus sinicus), a bird (Nipponia nippon), a snake (Protobothrops mucrosquamatus), a frog (Xenopus laevis), and a fish (Callorhinchus milii) reveal amino acid sequence identity of 83%, 81%, 83%, 61%, 60%, and 59%, respectively
Xenopus laevis
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Callorhinchus milii
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Homo sapiens
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Nipponia nippon
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Paguma larvata
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Protobothrops mucrosquamatus
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Rhinolophus sinicus
physiological function
the receptor binding domain (RBD) of spike glycoprotein is responsible for entry of coronaviruses (SARS-CoV-2 and SARS-CoV) into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling reveals that SARS-CoV-2 RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of SARS-CoV-2, making them all possible natural hosts for the virus
Xenopus laevis
Other publictions for EC 3.4.17.23
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
752692
Chen
Structure analysis of the rec ...
Callorhinchus milii, Homo sapiens, Nipponia nippon, Paguma larvata, Protobothrops mucrosquamatus, Rhinolophus sinicus, Xenopus laevis
Biochem. Biophys. Res. Commun.
FEHLT
0000
2020
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1
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16
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4
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7
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1
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4
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-
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15
15
-
-
-
753192
Cao
Comparative genetic analysis ...
Homo sapiens
Cell Discov.
6
11
2020
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-
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-
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1
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1
1
-
-
-
753315
Batlle
Soluble angiotensin-convertin ...
Homo sapiens
Clin. Sci.
134
543-545
2020
-
1
-
-
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2
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3
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5
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1
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1
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5
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2
2
-
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753431
Tian
Potent binding of 2019 novel ...
Mus musculus
Emerg. Microbes Infect.
9
382-385
2020
-
-
-
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-
-
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-
-
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1
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1
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1
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1
-
-
753944
Zhang
Angiotensin-converting enzyme ...
Homo sapiens
Intensive Care Med.
FEHLT
0000
2020
-
1
-
-
-
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-
-
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2
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1
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1
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1
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1
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2
2
-
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754646
Qiu
Predicting the angiotensin co ...
Bos taurus, Bubalus bubalis, Capra hircus, Columba livia, Felis catus, Homo sapiens, Manis javanica, Mus musculus, Ovis aries, Paguma larvata, Rhinolophus sinicus, Sus scrofa
Microbes Infect.
FEHLT
0000
2020
-
12
-
-
-
-
-
-
-
-
-
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12
-
-
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3
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12
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709990
Fraga-Silva
ACE2 activation promotes antit ...
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Mol. Med.
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2010
2
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6
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6
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10
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2
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710171
Feng
The angiotensin-converting enz ...
Homo sapiens
Oncol. Rep.
23
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2010
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1
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2
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-
-
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1
1
1
1
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710214
Lin
Regulation of angiotensin conv ...
Homo sapiens
Peptides
31
1334-1340
2010
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1
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2
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2
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1
1
1
1
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710532
Coelho
High sucrose intake in rats is ...
Rattus norvegicus
Regul. Pept.
162
61-67
2010
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1
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Losartan attenuates chronic ci ...
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Toxicol. Appl. Pharmacol.
245
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2010
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2
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-
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690356
Herath. C.B.; Lubel
Portal pressure responses and ...
Rattus norvegicus
Am. J. Physiol. Gastrointest. Liver Physiol.
297
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2009
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1
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2
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-
-
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692094
Lai
The identification of a calmod ...
Homo sapiens
Endocrinology
150
2376-2381
2009
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1
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1
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1
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692679
Huang
Expression of angiotensin-conv ...
Rattus norvegicus
Int. J. Mol. Med.
23
717-723
2009
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-
-
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2
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2
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1
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-
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693796
Luhtala
Activities of angiotensin-conv ...
Sus scrofa
J. Ocul. Pharmacol. Ther.
25
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2009
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3
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-
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-
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-
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694170
Bindom
The sweeter side of ACE2: phys ...
Homo sapiens, Rattus norvegicus
Mol. Cell. Endocrinol.
302
193-202
2009
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-
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14
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2
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2
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14
-
-
-
-
-
-
-
-
-
-
-
-
-
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694351
Oudit
The role of ACE2 in pulmonary ...
Homo sapiens
Nephrol. Dial. Transplant.
24
1362-1365
2009
-
1
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-
-
-
-
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1
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1
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2
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4
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2
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1
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1
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2
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4
-
-
-
-
-
-
-
-
-
-
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-
-
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695087
Vaz-Silva
The vasoactive peptide angiote ...
Homo sapiens
Reprod. Sci.
16
247-256
2009
-
-
-
-
-
-
-
-
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-
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2
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2
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2
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2
-
-
-
-
-
-
-
-
-
-
-
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695187
Zhou
Decreased expression of Angiot ...
Homo sapiens
Tohoku J. Exp. Med.
217
123-131
2009
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1
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2
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1
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1
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2
-
-
-
-
-
-
-
-
-
-
-
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695418
Clayton
The active site specificity of ...
Homo sapiens
Adv. Exp. Med. Biol.
611
559-560
2009
-
-
-
-
-
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1
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1
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1
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2
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2
-
2
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-
-
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1
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1
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1
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-
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2
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2
-
-
-
-
-
-
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-
-
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707055
Iwata
Selective and specific regulat ...
Cricetulus griseus, Mus musculus
Am. J. Physiol. Cell Physiol.
297
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2009
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2
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2
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2
2
1
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1
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-
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-
-
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2
-
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1
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1
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3
-
-
-
-
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1
-
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2
-
-
-
2
1
-
-
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1
-
-
-
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2
2
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707074
Jia
Ectodomain shedding of angiote ...
Homo sapiens
Am. J. Physiol. Lung Cell Mol. Physiol.
297
L84-L96
2009
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1
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7
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3
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1
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5
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1
1
2
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-
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1
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7
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3
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1
-
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1
-
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5
-
-
1
1
-
-
-
-
-
-
-
-
-
2
2
-
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708141
Kassiri
Loss of angiotensin-converting ...
Mus musculus
Circ. Heart Fail.
2
446-455
2009
-
-
-
-
-
-
-
-
-
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1
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2
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1
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1
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1
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-
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-
-
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1
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-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
708683
Xia
Angiotensin II type 1 receptor ...
Mus musculus
Hypertension
53
210-216
2009
2
-
-
-
1
-
1
-
-
-
-
1
-
2
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3
-
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2
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1
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2
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1
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1
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1
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-
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3
-
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2
-
-
-
-
-
-
-
-
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1
2
2
1
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-
708684
Masson
Onset of experimental severe c ...
Oryctolagus cuniculus, Rattus norvegicus
Hypertension
53
694-700
2009
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1
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2
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-
-
-
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2
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5
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5
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2
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1
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1
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2
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-
-
-
-
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2
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-
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-
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5
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
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708685
Stewart
Defects in cutaneous angiotens ...
Homo sapiens
Hypertension
53
767-774
2009
-
-
-
-
-
-
1
-
-
-
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1
-
1
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-
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1
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1
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1
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-
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-
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-
-
-
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1
-
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-
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1
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-
-
-
-
1
-
-
1
-
-
-
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-
-
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2
2
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709743
Yoshikawa
Differential virological and i ...
Homo sapiens
J. Virol.
83
5451-5465
2009
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3
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-
1
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3
-
-
-
-
-
-
-
-
-
-
-
-
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1
1
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-
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677486
Li
Angiotensin converting enzyme- ...
Homo sapiens, Mus musculus, Rattus norvegicus
Am. J. Physiol. Lung Cell Mol. Physiol.
295
L178-185
2008
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3
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6
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6
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3
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6
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6
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678102
Lambert
Angiotensin-converting enzyme ...
Homo sapiens, Mus musculus
Biochem. Pharmacol.
75
781-786
2008
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1
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1
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6
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1
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1
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1
1
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6
-
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4
-
-
-
-
-
-
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-
-
-
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-
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678710
Deaton
Thiol-based angiotensin-conver ...
Homo sapiens
Bioorg. Med. Chem. Lett.
18
732-737
2008
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-
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19
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19
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19
19
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678973
Zhong
Enhanced angiotensin convertin ...
Homo sapiens
Br. J. Pharmacol.
153
66-74
2008
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679300
Koitka
Angiotensin converting enzyme ...
Rattus norvegicus
Clin. Exp. Pharmacol. Physiol.
35
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2008
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10
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679703
Imai
The discovery of angiotensin-c ...
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Zulli
Co-localization of angiotensin ...
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679705
Guy
Functional angiotensin-convert ...
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93
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679706
Garabelli
Distinct roles for angiotensin ...
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-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
679707
Elased
Brain angiotensin-converting e ...
Mus musculus
Exp. Physiol.
93
665-675
2008
-
-
-
-
-
-
3
-
-
-
-
-
-
2
-
-
-
-
-
9
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
9
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
679708
Lew
Angiotensin-converting enzyme ...
Homo sapiens
Exp. Physiol.
93
685-693
2008
-
-
1
-
-
-
3
-
1
-
-
-
-
2
-
-
1
-
-
2
-
-
2
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
1
3
-
-
1
-
-
-
-
-
-
1
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
679876
Lambert
Calmodulin interacts with angi ...
Homo sapiens
FEBS Lett.
582
385-390
2008
-
-
1
-
-
-
1
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
4
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
680103
Der Sarkissian
Cardiac overexpression of angi ...
Rattus norvegicus
Hypertension
51
712-718
2008
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
1
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
681323
Mores
Development of potent and sele ...
Homo sapiens
J. Med. Chem.
51
2216-2226
2008
-
-
-
-
-
-
23
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
23
-
-
-
-
-
-
-
-
-
-
23
23
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
682824
Guo
Expression of feline angiotens ...
Felis silvestris, Homo sapiens, Mus musculus, Rattus norvegicus
Res. Vet. Sci.
84
494-496
2008
-
-
1
-
-
-
-
-
-
-
1
-
-
7
-
-
1
-
-
2
-
-
4
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
2
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
690333
Koka
Angiotensin II up-regulates an ...
Homo sapiens
Am. J. Pathol.
172
1174-1183
2008
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
690375
Levy
ACE2 expression and activity a ...
Rattus norvegicus
Am. J. Physiol. Regul. Integr. Comp. Physiol.
295
R1953-R1961
2008
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
3
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
691838
Feng
Angiotensin-converting enzyme ...
Mus musculus
Circ. Res.
102
729-736
2008
-
1
-
-
-
-
-
-
-
-
-
1
-
4
-
-
-
-
-
1
-
-
1
-
3
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
692319
Rushworth
Residues affecting the chlorid ...
Homo sapiens
FEBS J.
275
6033-6042
2008
-
-
1
-
5
-
2
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
5
-
-
2
-
2
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
692586
Hernandez Prada
Structure-based identification ...
Rattus norvegicus
Hypertension
51
1312-1317
2008
2
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
693702
Ferreira. A.J.; Raizada
Are we poised to target ACE2 f ...
Homo sapiens
J. Mol. Med.
86
685-690
2008
-
1
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
693733
Xia
Angiotensin-converting enzyme ...
Homo sapiens, Mus musculus, Rattus norvegicus
J. Neurochem.
107
1482-1494
2008
-
-
1
-
-
-
-
-
-
3
-
2
-
4
-
-
-
-
-
4
-
-
7
-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
2
-
-
-
-
-
4
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
693806
Sluimer
Angiotensin-converting enzyme ...
Homo sapiens
J. Pathol.
215
273-279
2008
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
3
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
677475
Trask
Primary role of angiotensin-co ...
Rattus norvegicus
Am. J. Physiol. Heart Circ. Physiol.
292
H3019-H3024
2007
-
-
-
-
-
-
1
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
677488
Joyner
Temporal-spatial expression of ...
Rattus norvegicus
Am. J. Physiol. Regul. Integr. Comp. Physiol.
293
R169-R177
2007
-
-
-
-
-
-
1
-
-
-
-
-
-
3
-
-
-
-
-
5
-
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
5
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
677603
Ho
Emodin blocks the SARS coronav ...
Homo sapiens
Antiviral Res.
74
92-101
2007
-
-
-
-
-
-
5
-
-
-
-
-
-
10
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
5
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
679072
Keidar
ACE2 of the heart: From angiot ...
Mus musculus, Rattus norvegicus
Cardiovasc. Res.
73
463-469
2007
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
20
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
2
-
-
20
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
679135
Imai
Angiotensin-converting enzyme ...
Mus musculus
Cell. Mol. Life Sci.
64
2006-2012
2007
-
1
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
1
-
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
680099
Yamazato
Overexpression of angiotensin- ...
Rattus norvegicus
Hypertension
49
926-931
2007
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
4
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
4
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
681022
Wiener
Angiotensin converting enzyme ...
Mus musculus
J. Cell. Biochem.
101
1278-1291
2007
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
4
-
-
2
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
681178
Herath
Upregulation of hepatic angiot ...
Rattus norvegicus
J. Hepatol.
47
387-395
2007
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
-
-
-
5
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
5
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
681678
Fukushi
Amino acid substitutions in th ...
Rattus norvegicus
J. Virol.
81
10831-10834
2007
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
667146
Gallagher
Distinct roles for ANG II and ...
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Am. J. Physiol.
290
C420-C426
2006
-
-
-
-
-
-
-
-
-
-
-
-
-
164
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
668354
Kuba
Angiotensin-converting enzyme ...
Homo sapiens
Curr. Opin. Pharmacol.
6
271-276
2006
-
1
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
668895
Elased
New mass spectrometric assay f ...
Homo sapiens, Mus musculus
Hypertension
47
1010-1017
2006
-
2
-
-
-
-
2
-
-
-
-
-
-
5
-
-
-
-
-
2
-
-
3
-
2
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
2
2
-
-
-
-
-
-
-
-
-
-
-
2
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
668896
Ferrario
Angiotensin-converting enzyme ...
Rattus norvegicus
Hypertension
47
515-521
2006
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
5
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
5
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
668897
Rice
Circulating activities of angi ...
Homo sapiens
Hypertension
48
914-920
2006
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
669004
Lew
-
Characterization of angiotensi ...
Homo sapiens
Int. J. Pept. Res. Ther.
12
283-289
2006
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
670526
Valdes
Distribution of angiotensin-(1 ...
Homo sapiens
Placenta
27
200-207
2006
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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Imai
Angiotensin-converting enzyme ...
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755534
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Rice
Evaluation of angiotensin-conv ...
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Warner
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Danilczyk
Physiological roles of angiote ...
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2004
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Kuhn
Angiotensin-converting enzyme ...
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2004
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Tikellis
Identification of angiotensin ...
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Douglas
The novel angiotensin-converti ...
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2004
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Huentelman
Cloning and characterization o ...
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Guy
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Zisman
Increased angiotensin-(1-7)-fo ...
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Tikellis
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Rattus norvegicus
Hypertension
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Stoesser
The EMBL Nucleotide Sequence D ...
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Substrate-based design of the ...
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2002
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659172
Vickers
Hydrolysis of biological pepti ...
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2002
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658455
Donoghue
A novel angiotensin-converting ...
Homo sapiens
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2000
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Tipnis
A humen homolog of angiotensin ...
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