INT211782

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Context Info
Confidence 0.26
First Reported 2007
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 2
Total Number 3
Disease Relevance 2.12
Pain Relevance 0.64

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

transport (Ambp) extracellular region (Ambp) plasma membrane (Ambp)
protein maturation (Ambp)
Anatomy Link Frequency
plasma 1
cleavage 1
urine 1
Ambp (Mus musculus)
Pain Link Frequency Relevance Heat
Inflammation 27 88.88 High High
anesthesia 26 83.24 Quite High
cytokine 14 79.72 Quite High
Inflammatory response 4 78.60 Quite High
cva 10 73.92 Quite High
Central nervous system 17 5.00 Very Low Very Low Very Low
Spinal cord 6 5.00 Very Low Very Low Very Low
aspirin 2 5.00 Very Low Very Low Very Low
Versed 2 5.00 Very Low Very Low Very Low
iatrogenic 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Injury 11 98.04 Very High Very High Very High
Postoperative Hemorrhage 12 93.40 High High
INFLAMMATION 31 88.88 High High
Pancreatitis 2 86.16 High High
Syndrome 5 82.08 Quite High
Disseminated Intravascular Coagulation 6 79.12 Quite High
Multiple Organ Failure 2 75.12 Quite High
Contagious Ecthyma 3 71.40 Quite High
Pressure Volume 2 Under Development 46 63.20 Quite High
Cancer 2 60.80 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In humans, ulinastatin is excreted by the kidneys and its main function is probably in plasma [25].
Localization (excreted) of ulinastatin in plasma
1) Confidence 0.26 Published 2010 Journal Korean Journal of Anesthesiology Section Body Doc Link PMC2872884 Disease Relevance 1.10 Pain Relevance 0.36
Ulinastatin (UlistinĀ®, Han Lim Pharmaceutical, Seoul, Korea), a urinary trypsin inhibitor, is a glycoprotein derived from human urine [12].
Localization (derived) of Ulinastatin in urine
2) Confidence 0.24 Published 2010 Journal Korean Journal of Anesthesiology Section Body Doc Link PMC2872884 Disease Relevance 0.95 Pain Relevance 0.28
Processing of the polyprotein is thought to proceed in accordance to a pathway established by protein folding resulting in masking of certain cleavage sites and by amino acid sequences adjoining the scissile bond [78] The first cleavage of the genomic polyprotein at a tyrosine-glycine dipeptide is catalyzed by the 2A proteinase and results in release of a 97-kDa polyprotein consisting of the P1 structural segment of the genome [190].
Localization (release) of polyprotein in cleavage
3) Confidence 0.01 Published 2007 Journal Virol J Section Body Doc Link PMC1947962 Disease Relevance 0.07 Pain Relevance 0

General Comments

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