INT340167

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Context Info
Confidence 0.29
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 7
Disease Relevance 0.69
Pain Relevance 0.25

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 (Oxtr) signal transducer activity (Oxtr)
Anatomy Link Frequency
P19 1
bars 1
Oxtr (Mus musculus)
Pain Link Frequency Relevance Heat
Dismenorea 7 93.28 High High
Inflammation 7 91.16 High High
antagonist 112 84.72 Quite High
imagery 14 5.00 Very Low Very Low Very Low
Potency 7 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Myocardial Infarction 7 95.60 Very High Very High Very High
Dysmenorrhea 7 93.28 High High
INFLAMMATION 7 91.16 High High
Increased Venous Pressure Under Development 7 82.56 Quite High
Apoptosis 14 69.40 Quite High
Embryonal Carcinoma 161 67.84 Quite High
Natriuresis 21 5.00 Very Low Very Low Very Low
Infarction 7 5.00 Very Low Very Low Very Low
Hyperplasia 7 5.00 Very Low Very Low Very Low
Repression 7 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Docking analysis shows OT-GKR interaction with OTR
OTR Binding (interaction) of
1) Confidence 0.29 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2964328 Disease Relevance 0.07 Pain Relevance 0
In our study, molecular docking of OT and OT-GKR showed that while both peptides are able to interact with OTR with significant binding energies, the binding pocket for OT-GKR might be slightly different from the binding pocket for OT.
OTR Binding (interact) of
2) Confidence 0.29 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2964328 Disease Relevance 0 Pain Relevance 0
Computerized molecular modeling revealed OT-GKR docking to active OTR sites and to V1a receptor of vasopressin.
OTR Binding (docking) of
3) Confidence 0.25 Published 2010 Journal PLoS ONE Section Abstract Doc Link PMC2964328 Disease Relevance 0 Pain Relevance 0.08
The clinical application of OT-GKR in this pathology could be safe because of the specific interaction with OTR and V1aR, as described in the present study.
OTR Binding (interaction) of
4) Confidence 0.24 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2964328 Disease Relevance 0.62 Pain Relevance 0.16
In the present experiments, we investigated whether OT-GKR exists in fetal and newborn rodent hearts, interacts with the OT receptors (OTR) and primes the generation of contracting cells expressing CM markers in P19 cells, a model for the study of early heart differentiation.


OTR Binding (interacts) of in P19
5) Confidence 0.24 Published 2010 Journal PLoS ONE Section Abstract Doc Link PMC2964328 Disease Relevance 0 Pain Relevance 0
Docking to OTR in positions V115, K116, Q119, M123, Q171, F185, T205, Y209 and Q295 was noted for both OT and OT-GKR models (Table 1).
OTR Binding (Docking) of
6) Confidence 0.22 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2964328 Disease Relevance 0 Pain Relevance 0
Several amino acid residues have been proposed to interact with OT and OT-GKR in the OTR model where the red bars represent docking with OT-GKR, and the black bars indicate docking with OT molecule (Fig. 2D).
OTR Binding (indicate) of in bars
7) Confidence 0.22 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2964328 Disease Relevance 0 Pain Relevance 0

General Comments

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