INT107620

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Context Info
Confidence 0.48
First Reported 2002
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 25
Total Number 25
Disease Relevance 5.49
Pain Relevance 4.24

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

isomerase activity (PTGES) signal transduction (PTGES) cytoplasm (PTGES)
Anatomy Link Frequency
proximal 2
pigmentation 2
TM1 1
PTGES (Homo sapiens)
Pain Link Frequency Relevance Heat
melanocortin 1 receptor 4 99.66 Very High Very High Very High
cytokine 21 98.48 Very High Very High Very High
cINOD 93 98.28 Very High Very High Very High
Inflammation 181 97.20 Very High Very High Very High
Arthritis 40 95.52 Very High Very High Very High
Pain 38 86.08 High High
Hyperalgesia 16 82.72 Quite High
COX-2 inhibitor 9 82.32 Quite High
Potency 24 77.52 Quite High
Osteoarthritis 176 69.40 Quite High
Disease Link Frequency Relevance Heat
Cancer 9 99.76 Very High Very High Very High
INFLAMMATION 252 98.16 Very High Very High Very High
Arthritis 40 95.52 Very High Very High Very High
Toxicity 1 93.28 High High
Disease 45 91.36 High High
Colon Cancer 1 89.84 High High
Pain 46 86.08 High High
Fever 24 85.36 High High
Hyperalgesia 16 82.72 Quite High
Osteoarthritis 200 76.48 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
It is crucial for rational design of the next-generation anti-inflammatory drugs to know the three-dimensional (3D) structure of mPGES-1 trimer and to understand how mPGES-1 binds with substrates and inhibitors.
mPGES-1 Binding (binds) of associated with inflammation and cinod
1) Confidence 0.48 Published 2008 Journal J Phys Chem B Section Abstract Doc Link 18476739 Disease Relevance 0.19 Pain Relevance 0.19
Understanding microscopic binding of human microsomal prostaglandin E synthase-1 with substrates and inhibitors by molecular modeling and dynamics simulation.
prostaglandin E synthase-1 Binding (binding) of
2) Confidence 0.48 Published 2008 Journal J Phys Chem B Section Title Doc Link 18476739 Disease Relevance 0.18 Pain Relevance 0.23
The 3D structural model enables us to understand how mPGES-1 binds with its substrates/inhibitors, and the key amino acid residues for the mPGES-1 binding with ligands have been identified.
mPGES-1 Binding (binds) of
3) Confidence 0.48 Published 2008 Journal J Phys Chem B Section Abstract Doc Link 18476739 Disease Relevance 0.17 Pain Relevance 0.23
Homo-timeric structural model of human microsomal prostaglandin E synthase-1 and characterization of its substrate/inhibitor binding interactions.
prostaglandin E synthase-1 Binding (interactions) of
4) Confidence 0.48 Published 2009 Journal J. Comput. Aided Mol. Des. Section Title Doc Link 18777160 Disease Relevance 0.09 Pain Relevance 0.09
Identification of key residues determining species differences in inhibitor binding of microsomal prostaglandin E synthase-1.
microsomal prostaglandin E synthase-1 Binding (binding) of
5) Confidence 0.40 Published 2010 Journal J. Biol. Chem. Section Title Doc Link 20605783 Disease Relevance 0.37 Pain Relevance 0.36
The 3D structural model enables us to understand how mPGES-1 binds with its substrates/inhibitors, and the key amino acid residues for the mPGES-1 binding with ligands have been identified.
mPGES-1 Binding (binding) of
6) Confidence 0.36 Published 2008 Journal J Phys Chem B Section Abstract Doc Link 18476739 Disease Relevance 0.16 Pain Relevance 0.23
In cell-free assays, YS121 inhibited human mPGES-1 in a reversible and noncompetitive manner (IC(50) = 3.4 muM), and surface plasmon resonance spectroscopy studies using purified in vitro-translated human mPGES-1 indicate direct, reversible, and specific binding to mPGES-1 (K(D) = 10-14 muM).
mPGES-1 Binding (binding) of
7) Confidence 0.36 Published 2010 Journal J. Pharmacol. Exp. Ther. Section Abstract Doc Link 19934399 Disease Relevance 0.14 Pain Relevance 0.07
This review will focus on recent efforts to target the terminal synthase, mPGES-1, for cancer chemoprevention.
mPGES-1 Binding (target) of associated with cancer
8) Confidence 0.35 Published 2010 Journal Biochimie Section Abstract Doc Link 20159031 Disease Relevance 0.77 Pain Relevance 0.21
Similar to COX-2, our data indicate that the maintained mPGES-1 protein and mRNA expression might be linked to repetitive treatments with HNE.


mPGES-1 protein Binding (maintained) of
9) Confidence 0.33 Published 2010 Journal Arthritis Res Ther Section Body Doc Link PMC2875653 Disease Relevance 0.07 Pain Relevance 0.03
Emerging evidence has disclosed that the transcriptional induction of mPGES-1 is primarily controlled by Egr-1 through two Egr-1 binding motifs identified in the proximal promoter region of mPGES-1 [36,37].
mPGES-1 Binding (binding) of in proximal
10) Confidence 0.33 Published 2010 Journal Arthritis Res Ther Section Body Doc Link PMC2875653 Disease Relevance 0.21 Pain Relevance 0.18
Transient transfection was performed to determine promoter activities of mPGES-1 and 5-LOX.


mPGES-1 Binding (activities) of
11) Confidence 0.31 Published 2010 Journal Arthritis Res Ther Section Abstract Doc Link PMC2875653 Disease Relevance 0.14 Pain Relevance 0.04
The detailed 3D structures and calculated binding free energies for mPGES-1's binding with substrates and inhibitors are all consistent with available experimental data, suggesting that the 3D model of the mPGES-1 trimer and the enzyme-ligand binding modes are reasonable.
mPGES-1 Binding (binding) of
12) Confidence 0.31 Published 2008 Journal J Phys Chem B Section Abstract Doc Link 18476739 Disease Relevance 0.15 Pain Relevance 0.23
Emerging evidence has disclosed that the transcriptional induction of mPGES-1 is primarily controlled by Egr-1 through two Egr-1 binding motifs identified in the proximal promoter region of mPGES-1 [36,37].
mPGES-1 Binding (binding) of in proximal
13) Confidence 0.28 Published 2010 Journal Arthritis Res Ther Section Body Doc Link PMC2875653 Disease Relevance 0.20 Pain Relevance 0.17
Although guinea pigs and humans share the same amino acid residues in positions 131, 135, and 138 of MPGES1, allowing for species discriminating MPGES1 inhibitors to bind, the overall identity of the two enzymes is only 79%.
MPGES1 Binding (bind) of
14) Confidence 0.25 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2937957 Disease Relevance 0.89 Pain Relevance 0.48
This can be explained based on a more recently solved structure in which PGES (PDBID: 2pbj[31]) is found to contain glutathione (GSH) and heme bound to it and it is involved in degradation reactions similar to that of cytochrome P450.
PGES Binding (bound) of
15) Confidence 0.20 Published 2010 Journal BMC Bioinformatics Section Body Doc Link PMC3009524 Disease Relevance 0 Pain Relevance 0
Hence, the amino acid differences between rat and human in TM1 do not play a crucial role for inhibitor binding of MPGES1.



MPGES1 Binding (binding) of in TM1
16) Confidence 0.19 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2937957 Disease Relevance 0.35 Pain Relevance 0.28
Second, compound I acts as a competitive inhibitor toward the natural substrate PGH2 and thus binds to the corresponding location of the active site of MPGES1.
MPGES1 Binding (binds) of
17) Confidence 0.19 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2937957 Disease Relevance 0.23 Pain Relevance 0.06
We went on to locate individual residues that are important for inhibitor binding by exchanging single amino acid residues in rat MPGES1 toward the corresponding residue in the human enzyme and tested their ability to be inhibited by compound I.
MPGES1 Binding (binding) of
18) Confidence 0.17 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2937957 Disease Relevance 0 Pain Relevance 0
Exchange of the same residues 115–140 in human WT MPGES1 abrogated inhibitor binding.
MPGES1 Binding (binding) of
19) Confidence 0.17 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2937957 Disease Relevance 0 Pain Relevance 0
Although evidence for the substrate and/or inhibitor-binding site in the protein structures of other MAPEG members fit very well with the findings in this work, there is no direct structural data on inhibitor binding in MPGES1 to date.
MPGES1 Binding (binding) of
20) Confidence 0.17 Published 2010 Journal The Journal of Biological Chemistry Section Body Doc Link PMC2937957 Disease Relevance 0 Pain Relevance 0

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