INT171651

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Context Info
Confidence 0.60
First Reported 2002
Last Reported 2002
Negated 1
Speculated 0
Reported most in Body
Documents 1
Total Number 4
Disease Relevance 1.07
Pain Relevance 0.16

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peptidase activity (PRSS1) extracellular space (PRSS1) extracellular region (PRSS1)
Anatomy Link Frequency
D22 4
cleavage 2
PRSS1 (Homo sapiens)
Pain Link Frequency Relevance Heat
Chronic pancreatitis 12 87.36 High High
Disease Link Frequency Relevance Heat
Pancreatitis 92 92.84 High High
Disease 4 31.28 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
This indicates a high control of cathepsin B action on trypsinogen activation by the amino acid structure of TAP and highlights the particular functional importance of the D22 residue within the tetraaspartic group D19-D20-D21-D22.
Regulation (control) of Positive_regulation (activation) of trypsinogen in D22
1) Confidence 0.60 Published 2002 Journal BMC Gastroenterol Section Body Doc Link PMC117221 Disease Relevance 0.18 Pain Relevance 0
In contrast to the mutations N29I, N29T and R122H, which are located away from this cleavage site, trypsinogen mutations affecting the K23-I24 bond could potentially affect the cathepsin B action on trypsinogen activation.
Regulation (affect) of Positive_regulation (activation) of trypsinogen in cleavage
2) Confidence 0.60 Published 2002 Journal BMC Gastroenterol Section Body Doc Link PMC117221 Disease Relevance 0.29 Pain Relevance 0.07
This indicates a high control of cathepsin B action on trypsinogen activation by the amino acid structure of TAP and highlights the particular functional importance of the D22 residue within the tetraaspartic group D19-D20-D21-D22.
Regulation (action) of Positive_regulation (activation) of trypsinogen in D22
3) Confidence 0.26 Published 2002 Journal BMC Gastroenterol Section Body Doc Link PMC117221 Disease Relevance 0.18 Pain Relevance 0
The investigation of the wild type trypsinogen molecule and three distinct mutants (i.e., N29I, N29T and R122H) found that cathepsin B mediated trypsinogen activation was not influenced by the respective mutants [8].
Neg (not) Regulation (influenced) of Positive_regulation (activation) of trypsinogen
4) Confidence 0.26 Published 2002 Journal BMC Gastroenterol Section Body Doc Link PMC117221 Disease Relevance 0.42 Pain Relevance 0.09

General Comments

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