INT273358

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Context Info
Confidence 0.17
First Reported 2009
Last Reported 2010
Negated 2
Speculated 1
Reported most in Body
Documents 4
Total Number 6
Disease Relevance 0.88
Pain Relevance 0.27

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

lipid binding (LTC4S) nuclear envelope (LTC4S) small molecule metabolic process (LTC4S)
lyase activity (LTC4S) endoplasmic reticulum (LTC4S) nucleus (LTC4S)
Anatomy Link Frequency
TM1 1
TM4 1
LTC4S (Homo sapiens)
Pain Link Frequency Relevance Heat
Spinal cord 4 86.16 High High
agonist 16 76.80 Quite High
Inflammation 50 69.80 Quite High
Inflammatory mediators 2 47.44 Quite Low
Arthritis 12 43.20 Quite Low
Hyperalgesia 6 30.40 Quite Low
Pain 12 24.36 Low Low
antagonist 13 17.48 Low Low
Potency 9 15.84 Low Low
cINOD 25 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Targeted Disruption 12 98.12 Very High Very High Very High
Frailty 4 86.44 High High
Cv Unclassified Under Development 4 84.12 Quite High
INFLAMMATION 64 69.80 Quite High
Arthritis 12 43.20 Quite Low
Disease 12 39.04 Quite Low
Hyperalgesia 6 30.40 Quite Low
Occupational Lung Diseases 1 25.36 Quite Low
Pain 15 24.36 Low Low
Osteoarthritis 3 24.16 Low Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Furthermore, the corresponding residues in FLAP and LTC4S have been determined to bind to an inhibitor that was cocrystallized, or to a substrate surrogate, respectively, and hence support a high degree of conservation of the substrate/inhibitor-binding site within the MAPEG superfamily.


LTC4S Spec (determined) Binding (bind) of
1) Confidence 0.17 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2937957 Disease Relevance 0 Pain Relevance 0
The observation of a detergent molecule, bound between TM1 and TM4 of neighboring subunits in LTC4S, led to the suggestion that it mimics LTA4, the substrate of this enzyme, and thus indicates the active site region of LTC4S (22).
LTC4S Binding (bound) of in TM4
2) Confidence 0.14 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2937957 Disease Relevance 0.14 Pain Relevance 0.03
The observation of a detergent molecule, bound between TM1 and TM4 of neighboring subunits in LTC4S, led to the suggestion that it mimics LTA4, the substrate of this enzyme, and thus indicates the active site region of LTC4S (22).
LTC4S Binding (bound) of in TM1
3) Confidence 0.05 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2937957 Disease Relevance 0.14 Pain Relevance 0.03
Of note, no binding of LTC4 and LTD4 to GPR17 was seen in this study (Maekawa et al., 2009)
LTC4 Neg (no) Binding (binding) of
4) Confidence 0.03 Published 2010 Journal British Journal of Pharmacology Section Body Doc Link PMC2839267 Disease Relevance 0.42 Pain Relevance 0.07
A possible explanation of the inhibitory effects of NCX2057 in the present study, is therefore that this lipophilic NO donor has the potential to inhibit de novo synthesis of leukotrienes and prostanoids via interaction with iron centre in 5-lipoxygenase and cyclooxygenase enzymes [34,35], and via interaction with thiol groups on LTC4 synthase [34].
LTC4 synthase Binding (interaction) of
5) Confidence 0.03 Published 2009 Journal Respir Res Section Body Doc Link PMC2696438 Disease Relevance 0.19 Pain Relevance 0.09
As shown in Figure S3, LTC4 did not activate or bind to hGPR17-L, -S or mGPR17, whereas this was readily observed for CysLT2.
LTC4 Neg (not) Binding (bind) of
6) Confidence 0.03 Published 2010 Journal British Journal of Pharmacology Section Body Doc Link PMC2839267 Disease Relevance 0 Pain Relevance 0.04

General Comments

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