INT170517

From wiki-pain
Jump to: navigation, search
Context Info
Confidence 0.15
First Reported 2001
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 2
Total Number 4
Disease Relevance 0.36
Pain Relevance 0.05

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

cytoplasm (Ryr1, Qdpr) cytosol (Qdpr) mitochondrion (Qdpr)
transport (Ryr1) oxidoreductase activity (Qdpr) plasma membrane (Ryr1)
Anatomy Link Frequency
myotubes 1
Ryr1 (Mus musculus)
Qdpr (Mus musculus)
Ryr1 - R163C (1)
Pain Link Frequency Relevance Heat
agonist 15 93.52 High High
halothane 6 25.68 Quite Low
addiction 50 5.00 Very Low Very Low Very Low
tetrodotoxin 4 5.00 Very Low Very Low Very Low
withdrawal 3 5.00 Very Low Very Low Very Low
Glutamate 1 5.00 Very Low Very Low Very Low
imagery 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Malignant Hyperthermia 45 98.44 Very High Very High Very High
Disease 3 34.52 Quite Low
Contracture 6 27.16 Quite Low
Myelodysplastic Syndromes 3 5.00 Very Low Very Low Very Low
Congenital Anomalies 3 5.00 Very Low Very Low Very Low
Targeted Disruption 2 5.00 Very Low Very Low Very Low
Cold Sores 1 5.00 Very Low Very Low Very Low
Herpes Simplex Virus 1 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Because the DHPR and RYR1 are functionally coupled, mutations in RYR1 that are linked to malignant hyperthermia (MH) may affect DHPR activity.
RYR1 Binding (coupled) of DHPR associated with malignant hyperthermia
1) Confidence 0.15 Published 2010 Journal The Journal of General Physiology Section Abstract Doc Link PMC2888063 Disease Relevance 0.36 Pain Relevance 0
If this idea is correct, then just as the transition of the DHPR from resting to ECC activated would promote the corresponding transition of RYR1, alterations of RYR1 that promoted its entry into the ECC-activated conformation would facilitate the corresponding transition of the DHPR.
RYR1 Binding (alterations) of DHPR
2) Confidence 0.14 Published 2010 Journal The Journal of General Physiology Section Body Doc Link PMC2888063 Disease Relevance 0 Pain Relevance 0.05
Collectively, the results with whole cell voltage clamp measurements in this paper, and the results on myoplasmic Ca2+ transients evoked by application of elevated K+ to intact myotubes, which are described by Estève et al. in this issue, indicate that the R163C mutation in RYR1 alters the gating of the DHPR with respect both to membrane currents and ECC.
RYR1 (R163C) Binding (gating) of DHPR in myotubes
3) Confidence 0.14 Published 2010 Journal The Journal of General Physiology Section Body Doc Link PMC2888063 Disease Relevance 0 Pain Relevance 0
Further, the interactions between DHPR subunits and RyR1 also are incompletely understood.
RyR1 Binding (interactions) of DHPR
4) Confidence 0.13 Published 2001 Journal BMC Physiol Section Body Doc Link PMC37314 Disease Relevance 0 Pain Relevance 0

General Comments

This test has worked.

Personal tools
Namespaces

Variants
Actions
Navigation
Toolbox