INT247760

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Context Info
Confidence 0.05
First Reported 2008
Last Reported 2008
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 8
Disease Relevance 0.75
Pain Relevance 0.41

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

signal transduction (Cmklr1) extracellular region (Rarres2) plasma membrane (Cmklr1)
signal transducer activity (Cmklr1)
Anatomy Link Frequency
macrophages 1
Cmklr1 (Mus musculus)
Rarres2 (Mus musculus)
Pain Link Frequency Relevance Heat
Potency 16 94.24 High High
cytokine 48 78.36 Quite High
Bioavailability 8 50.08 Quite High
Inflammation 64 43.68 Quite Low
chemokine 264 30.40 Quite Low
Inflammatory response 24 5.00 Very Low Very Low Very Low
ketamine 8 5.00 Very Low Very Low Very Low
anesthesia 8 5.00 Very Low Very Low Very Low
Multiple sclerosis 8 5.00 Very Low Very Low Very Low
agonist 8 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Anaphylaxis 232 89.60 High High
Edema 152 86.88 High High
Contact Dermatitis 56 82.20 Quite High
INFLAMMATION 88 43.68 Quite Low
Hypersensitivity 16 37.16 Quite Low
Disease 16 5.00 Very Low Very Low Very Low
Demyelinating Disease 8 5.00 Very Low Very Low Very Low
Overdose 8 5.00 Very Low Very Low Very Low
Lymphatic System Cancer 8 5.00 Very Low Very Low Very Low
Cancer 8 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The bioactive 9-mer carboxyl-terminal chemerin peptide (residues 149–157, YFPGQFAFS) was 10-fold less potent (EC50 = 26.2 nM; see Fig. 8 A) than chemerin protein in binding to CMKLR1.
CMKLR1 Binding (binding) of chemerin
1) Confidence 0.05 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.09
This may reflect inhibition of binding by the C-terminal His8 tag (which would be analogous to the inhibitory activity of the carboxyl-terminal residues in the chemerin proform) or, potentially, inaccessibility of the His8 epitope to the detection mAbs when His8-tagged chemerin is bound to CMKLR1.
CMKLR1 Binding (bound) of chemerin
2) Confidence 0.05 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.09
S8 shows the displacement of iodinated chemerin (residues 21–148) binding to CCRL2 and CMKLR1 by His8-chemerin and bioactive chemerin peptide (YFPGQFAFS).
CMKLR1 Binding (binding) of chemerin
3) Confidence 0.05 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0.26 Pain Relevance 0.04
The bioactive 9-mer carboxyl-terminal chemerin peptide (residues 149–157, YFPGQFAFS) was 10-fold less potent (EC50 = 26.2 nM; see Fig. 8 A) than chemerin protein in binding to CMKLR1.
CMKLR1 Binding (binding) of chemerin
4) Confidence 0.05 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.09
The binding affinity of chemerin for CCRL2 was similar to, if not slightly better than, chemerin binding to the first identified chemerin receptor, mCMKLR1 (EC50 = 3.1 nM; Fig. 6 B).
mCMKLR1 Binding (binding) of chemerin
5) Confidence 0.05 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0
The carboxyl-terminal domain of chemerin that is critical for binding to CMKLR1 is relatively uninvolved and unencumbered when chemerin is bound to CCRL2.
CMKLR1 Binding (binding) of chemerin
6) Confidence 0.05 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.08
Thus, CCRL2 can concentrate bioactive chemerin, which then is available for interaction with CMKLR1 on adjacent cells.


CMKLR1 Binding (interaction) of chemerin
7) Confidence 0.04 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0 Pain Relevance 0.03
Perhaps mast cell–bound and then activated chemerin interacts with CMKLR1+ macrophages or other mononuclear cells that might be present in normal skin, and such cells in turn have effects that can enhance local vascular permeability.
CMKLR1 Binding (interacts) of chemerin in macrophages
8) Confidence 0.04 Published 2008 Journal The Journal of Experimental Medicine Section Body Doc Link PMC2556791 Disease Relevance 0.49 Pain Relevance 0

General Comments

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