INT111865

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Context Info
Confidence 0.06
First Reported 2003
Last Reported 2003
Negated 0
Speculated 0
Reported most in Abstract
Documents 1
Total Number 7
Disease Relevance 0
Pain Relevance 0.09

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extracellular region (LNPEP, ANGPT4) intracellular (LNPEP) cell-cell signaling (LNPEP)
cytosol (LNPEP) peptidase activity (LNPEP) extracellular space (ANGPT4)
Anatomy Link Frequency
cleavage 6
LNPEP (Homo sapiens)
ANGPT4 (Homo sapiens)
Pain Link Frequency Relevance Heat
Enkephalin 7 62.32 Quite High
Neuropeptide 7 50.24 Quite High

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Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In this study, we demonstrate that AT4 receptor ligands, including Ang IV, Nle1-Ang IV, divalinal-Ang IV, and the structurally unrelated LVV-hemorphin-7, are all potent inhibitors of IRAP catalytic activity, as assessed by cleavage of leu-beta-naphthylamide by recombinant human IRAP.
AT4 receptor Binding (ligands) of Ang IV in cleavage
1) Confidence 0.06 Published 2003 Journal J. Neurochem. Section Abstract Doc Link 12871575 Disease Relevance 0 Pain Relevance 0
In this study, we demonstrate that AT4 receptor ligands, including Ang IV, Nle1-Ang IV, divalinal-Ang IV, and the structurally unrelated LVV-hemorphin-7, are all potent inhibitors of IRAP catalytic activity, as assessed by cleavage of leu-beta-naphthylamide by recombinant human IRAP.
AT4 receptor Binding (ligands) of Nle1-Ang IV in cleavage
2) Confidence 0.06 Published 2003 Journal J. Neurochem. Section Abstract Doc Link 12871575 Disease Relevance 0 Pain Relevance 0
In this study, we demonstrate that AT4 receptor ligands, including Ang IV, Nle1-Ang IV, divalinal-Ang IV, and the structurally unrelated LVV-hemorphin-7, are all potent inhibitors of IRAP catalytic activity, as assessed by cleavage of leu-beta-naphthylamide by recombinant human IRAP.
IRAP Binding (ligands) of Ang IV in cleavage
3) Confidence 0.06 Published 2003 Journal J. Neurochem. Section Abstract Doc Link 12871575 Disease Relevance 0 Pain Relevance 0
In this study, we demonstrate that AT4 receptor ligands, including Ang IV, Nle1-Ang IV, divalinal-Ang IV, and the structurally unrelated LVV-hemorphin-7, are all potent inhibitors of IRAP catalytic activity, as assessed by cleavage of leu-beta-naphthylamide by recombinant human IRAP.
IRAP Binding (ligands) of Nle1-Ang IV in cleavage
4) Confidence 0.06 Published 2003 Journal J. Neurochem. Section Abstract Doc Link 12871575 Disease Relevance 0 Pain Relevance 0
Both Ang IV and divalinal-Ang IV display competitive kinetics, indicating that AT4 ligands mediate their effects by binding to the catalytic site of IRAP.
IRAP Binding (binding) of Ang IV
5) Confidence 0.06 Published 2003 Journal J. Neurochem. Section Abstract Doc Link 12871575 Disease Relevance 0 Pain Relevance 0.09
In this study, we demonstrate that AT4 receptor ligands, including Ang IV, Nle1-Ang IV, divalinal-Ang IV, and the structurally unrelated LVV-hemorphin-7, are all potent inhibitors of IRAP catalytic activity, as assessed by cleavage of leu-beta-naphthylamide by recombinant human IRAP.
IRAP Binding (ligands) of divalinal-Ang IV in cleavage
6) Confidence 0.05 Published 2003 Journal J. Neurochem. Section Abstract Doc Link 12871575 Disease Relevance 0 Pain Relevance 0
In this study, we demonstrate that AT4 receptor ligands, including Ang IV, Nle1-Ang IV, divalinal-Ang IV, and the structurally unrelated LVV-hemorphin-7, are all potent inhibitors of IRAP catalytic activity, as assessed by cleavage of leu-beta-naphthylamide by recombinant human IRAP.
AT4 receptor Binding (ligands) of divalinal-Ang IV in cleavage
7) Confidence 0.05 Published 2003 Journal J. Neurochem. Section Abstract Doc Link 12871575 Disease Relevance 0 Pain Relevance 0

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