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Context Info
Confidence 0.99
First Reported 1995
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 5
Total Number 5
Disease Relevance 2.66
Pain Relevance 0.95

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

extracellular space (EDN1) extracellular region (EDN1) cell-cell signaling (EDN1)
cytoplasm (EDN1)
EDN1 (Homo sapiens)
Pain Link Frequency Relevance Heat
bradykinin 5 100.00 Very High Very High Very High
Enkephalin 4 100.00 Very High Very High Very High
Neuropeptide 1 100.00 Very High Very High Very High
cytokine 13 94.44 High High
Inflammation 33 93.28 High High
substance P 16 90.40 High High
Opioid 4 84.96 Quite High
antagonist 49 80.24 Quite High
Central nervous system 1 56.04 Quite High
Potency 1 45.52 Quite Low
Disease Link Frequency Relevance Heat
Natriuresis 3 100.00 Very High Very High Very High
Injury 5 98.96 Very High Very High Very High
Increased Venous Pressure Under Development 85 96.08 Very High Very High Very High
INFLAMMATION 40 93.28 High High
Diabetes Mellitus 17 90.72 High High
Sperm Disorder 15 88.56 High High
Adhesions 14 88.52 High High
Hyperlipidemia 5 84.56 Quite High
Hyperglycemia 3 83.04 Quite High
Cancer 66 73.88 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The former effect appears to be based on the inhibition of ET-1 degradation by neutral endopeptidase 24.11 (NEP), since kelatorphan, a specific NEP inhibitor, produced a similar increasing effect on ET-1 release.
Protein_catabolism (degradation) of ET-1
1) Confidence 0.99 Published 1995 Journal Biol. Pharm. Bull. Section Abstract Doc Link 7550091 Disease Relevance 0 Pain Relevance 0
The primary translation product of the ET-1 gene is the 212-aa prepro-ET-1, which is cleaved by an endopeptidase to form the 38-aa big-ET-1.
Protein_catabolism (cleaved) of ET-1
2) Confidence 0.30 Published 2004 Journal J Transl Med Section Body Doc Link PMC436068 Disease Relevance 0.84 Pain Relevance 0.10
NEP also degrades other bioactive peptides such as enkephalins, angiotensins, endothelin-1, cholecystokinins and bradykinin [24-28].
Protein_catabolism (NEP also) of endothelin-1 associated with enkephalin and bradykinin
3) Confidence 0.04 Published 2010 Journal Reprod Biol Endocrinol Section Body Doc Link PMC2936315 Disease Relevance 0.09 Pain Relevance 0.38
Neutral endopeptidase (NEP), a membrane-bound metallopeptidase enzyme that degrades neuropeptides, bradykinin, atrial natriuretic factor, enkephalins, and endothelin may regulate response to injury.
Protein_catabolism (degrades) of endothelin associated with natriuresis, injury, neuropeptide, enkephalin and bradykinin
4) Confidence 0.04 Published 2003 Journal Shock Section Abstract Doc Link 12785004 Disease Relevance 0.70 Pain Relevance 0.20
Also AII stimulates endothelin converting enzyme that degrades big-endothelin releasing endothelin-I, the most powerful vasoconstrictor on vessel walls [23-25].
Protein_catabolism (degrades) of endothelin-I
5) Confidence 0.01 Published 2006 Journal Cardiovasc Diabetol Section Body Doc Link PMC1434727 Disease Relevance 1.03 Pain Relevance 0.27

General Comments

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