3.4.22.66: calicivirin
This is an abbreviated version!
For detailed information about calicivirin, go to the full flat file.
Word Map on EC 3.4.22.66
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3.4.22.66
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coronavirus
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sars-cov-2
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covid-19
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polyproteins
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pandemic
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repurposing
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outbreak
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plpro
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3-chymotrypsin-like
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papain-like
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rna-dependent
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remdesivir
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ace2
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mers-cov
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ramaswamy
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replicase
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nonstructural
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sarma
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wuhan
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lopinavir
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admet
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anti-sars-cov-2
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mhv-a59
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genogroups
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picornavirus
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caliciviruses
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medicine
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anti-sars
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norwalk
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anti-covid-19
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betacoronavirus
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sars-coronavirus
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anti-coronavirus
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trans-cleavage
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drug development
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pp1ab
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caliciviridae
- 3.4.22.66
- coronavirus
- sars-cov-2
- covid-19
- polyproteins
- pandemic
-
repurposing
-
outbreak
- plpro
-
3-chymotrypsin-like
-
papain-like
-
rna-dependent
- remdesivir
- ace2
- mers-cov
-
ramaswamy
-
replicase
-
nonstructural
-
sarma
-
wuhan
- lopinavir
-
admet
-
anti-sars-cov-2
-
mhv-a59
-
genogroups
- picornavirus
- caliciviruses
- medicine
-
anti-sars
-
norwalk
-
anti-covid-19
- betacoronavirus
-
sars-coronavirus
-
anti-coronavirus
-
trans-cleavage
- drug development
- pp1ab
- caliciviridae
Reaction
endopeptidase with a preference for cleavage when the P1 position is occupied by Glu-/- and the P1' position is occupied by Gly-/- =
Synonyms
3C protease, 3C-like cysteine protease, 3C-like protease, 3C-like proteinase, 3C-like viral protease, 3CL Pro, 3cLpro, 3CP, 3Cpro, C37.001, calicivirus protease, CVP, FCV 3CLpro, NoV 3CLpro, NV 3CLpro, NV protease, NVPro, Pro, PV 3Cpro, Southampton virus 3C-like protease, viral cysteine protease, virus-encoded 3C-like proteinase
ECTree
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Application
Application on EC 3.4.22.66 - calicivirin
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drug development
medicine
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the conserved key site of the enzyme may serve as attractive target for the design of broad-spectrum antivirals for multiple viruses in the supercluster
drug development
the conserved key site of the enzyme may serve as attractive target for the design of broad-spectrum antivirals for multiple viruses in the supercluster
drug development
-
the conserved key site of the enzyme may serve as attractive target for the design of broad-spectrum antivirals for multiple viruses in the supercluster
drug development
-
the conserved key site of the enzyme may serve as attractive target for the design of broad-spectrum antivirals for multiple viruses in the supercluster
drug development
the conserved key site of the enzyme may serve as attractive target for the design of broad-spectrum antivirals for multiple viruses in the supercluster
drug development
-
the conserved key site of the enzyme may serve as attractive target for the design of broad-spectrum antivirals for multiple viruses in the supercluster
drug development
-
the conserved key site of the enzyme may serve as attractive target for the design of broad-spectrum antivirals for multiple viruses in the supercluster
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calicivirus 3CLpro mediates the cleavage of poly(A)-binding protein as part of its strategy to inhibit cellular translation
medicine
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establishment of a mammalian cell-based system for analysis of human norovirus replication and, thus makes it feasible to investigate antiviral agents in mammalian cells
medicine
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nonbacterial acute gastroenteritis and other diseases associated with viruses expressing 3Cpro, knowledge of the structure and previous mutagenesis study allows to correlate proteolysis and structure
medicine
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norovirus precursor comprised of both the proteinase and polymerase (released from 3C-like proteinase) is a bifunctional enzyme during virus replication, which might be useful in the development of antiviral drugs of the noroviruses associated with acute gastroenteritis
medicine
Norwalk virus is the major cause of acute, epidemic, viral gastroenteritis
medicine
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poliovirus 3Cpro mediates the cleavage of poly(A)-binding protein as part of its strategy to inhibit cellular translation
medicine
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calicivirus 3CLpro mediates the cleavage of poly(A)-binding protein as part of its strategy to inhibit cellular translation
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medicine
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norovirus precursor comprised of both the proteinase and polymerase (released from 3C-like proteinase) is a bifunctional enzyme during virus replication, which might be useful in the development of antiviral drugs of the noroviruses associated with acute gastroenteritis
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