INT255030

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Context Info
Confidence 0.84
First Reported 2008
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 5
Total Number 6
Disease Relevance 2.39
Pain Relevance 0.14

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

small molecule metabolic process (GLP1R) plasma membrane (GLP1R) signal transducer activity (GLP1R)
Anatomy Link Frequency
cleavage 1
central nervous system 1
GLP1R (Homo sapiens)
Pain Link Frequency Relevance Heat
Central nervous system 3 96.52 Very High Very High Very High
agonist 47 90.96 High High
Neuropeptide 4 11.20 Low Low
cytokine 1 10.00 Low Low
chemokine 2 8.80 Low Low
headache 10 5.00 Very Low Very Low Very Low
adenocard 5 5.00 Very Low Very Low Very Low
tolerance 3 5.00 Very Low Very Low Very Low
potassium channel 2 5.00 Very Low Very Low Very Low
nud 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Myocardial Infarction 5 99.56 Very High Very High Very High
Coronary Artery Disease 2 96.32 Very High Very High Very High
Apoptosis 3 94.80 High High
Diabetes Mellitus 228 92.48 High High
Body Weight 27 87.80 High High
Weight Loss 19 87.40 High High
Hypoglycemia 42 86.12 High High
Disease Progression 12 70.80 Quite High
Sprains And Strains 2 52.08 Quite High
Hyperglycemia 11 35.12 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
GLP-1 is degraded rapidly by the ubiquitous enzyme dipeptidyl-peptidase IV (DPP-4).
Protein_catabolism (degraded) of GLP-1
1) Confidence 0.84 Published 2010 Journal Pediatr Nephrol Section Body Doc Link PMC2874027 Disease Relevance 0.67 Pain Relevance 0.09
GLP-1 is a product of the glucagon gene and is post-translationally cleaved from preproglucagon in the neuroendocrine L-cells of the intestinal mucosa and in the central nervous system.
Protein_catabolism (cleaved) of GLP-1 in central nervous system associated with central nervous system
2) Confidence 0.48 Published 2010 Journal Pediatr Nephrol Section Body Doc Link PMC2874027 Disease Relevance 0.40 Pain Relevance 0.05
As noted above, native GLP-1 is rapidly metabolized by DPP-IV, which is widely expressed and can be found in multiple tissues and cell types, as well as in the circulation [5].
Protein_catabolism (rapidly) of GLP-1
3) Confidence 0.47 Published 2010 Journal British Journal of Clinical Pharmacology Section Body Doc Link PMC2997321 Disease Relevance 0.50 Pain Relevance 0
As noted above, native GLP-1 is rapidly metabolized by DPP-IV, which is widely expressed and can be found in multiple tissues and cell types, as well as in the circulation [5].
Protein_catabolism (metabolized) of GLP-1
4) Confidence 0.47 Published 2010 Journal British Journal of Clinical Pharmacology Section Body Doc Link PMC2997321 Disease Relevance 0.50 Pain Relevance 0
Since the second N-terminal amino acid in GLP-1 is alanine, GLP-1 is cleaved to a truncated form (Deacon 2004) which is largely inactive; therefore the cleavage of GLP-1 by DPP-4 is an inactivation process.
Protein_catabolism (cleaved) of GLP-1 in cleavage
5) Confidence 0.41 Published 2008 Journal Vascular Health and Risk Management Section Body Doc Link PMC2597770 Disease Relevance 0 Pain Relevance 0
Both GLP-1 and GIP are rapidly degraded to largely inactive metabolites by the enzyme dipeptidyl peptidase-4 (DPP-4) (Drucker 2003).
Protein_catabolism (degraded) of GLP-1
6) Confidence 0.37 Published 2008 Journal Vascular Health and Risk Management Section Body Doc Link PMC2597758 Disease Relevance 0.32 Pain Relevance 0

General Comments

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