INT272348

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Context Info
Confidence 0.38
First Reported 2006
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 8
Total Number 8
Disease Relevance 1.01
Pain Relevance 0.36

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mRNA processing (Adar) nucleolus (Adar) RNA binding (Adar)
nucleus (Adar) intracellular (Adar) DNA binding (Adar)
Anatomy Link Frequency
ADAR 5
Adar (Mus musculus)
Pain Link Frequency Relevance Heat
Serotonin 99 91.36 High High
fluoxetine 39 84.88 Quite High
antidepressant 3 72.68 Quite High
depression 19 70.96 Quite High
adenocard 70 14.60 Low Low
Neuronal excitability 6 9.56 Low Low
Rsd 6 6.20 Low Low
Glutamate 60 5.00 Very Low Very Low Very Low
ischemia 30 5.00 Very Low Very Low Very Low
Action potential 30 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Targeted Disruption 53 93.88 High High
Anaplastic Astrocytoma 18 80.68 Quite High
Schizophrenia 31 79.60 Quite High
Urological Neuroanatomy 1 78.92 Quite High
Depression 19 70.96 Quite High
Suicidal Behaviour 7 69.24 Quite High
Congenital Anomalies 2 67.48 Quite High
Epilepsy 54 63.20 Quite High
Shock 1 44.20 Quite Low
Helminth Infection 8 19.04 Low Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Local accumulation of small nucleolar RNAs (snoRNAs) in the nucleolus may be responsible for the tethering of ADAR1 and ADAR2, due to interaction between these dsRNA structures with the dsRBD of ADAR.
ADAR1 Binding (interaction) of in ADAR
1) Confidence 0.38 Published 2009 Journal Mol Brain Section Body Doc Link PMC2694175 Disease Relevance 0 Pain Relevance 0
In addition, multiple copies of dsRBMs and subtle amino acid changes among the different dsRBMs could allow preferential binding of ADAR family members to RNA substrates with different secondary structures.
ADAR Binding (binding) of in ADAR
2) Confidence 0.38 Published 2009 Journal Mol Brain Section Body Doc Link PMC2694175 Disease Relevance 0 Pain Relevance 0
Such a model would therefore suggest that the editing substrates and snoRNAs compete for binding to the ADAR proteins.
ADAR Binding (binding) of in ADAR
3) Confidence 0.38 Published 2009 Journal Mol Brain Section Body Doc Link PMC2694175 Disease Relevance 0.26 Pain Relevance 0
Therefore, recognition and binding of ADAR substrates by dsRBMs is structurally-dependent and length sensitive.
ADAR Binding (binding) of in ADAR
4) Confidence 0.38 Published 2009 Journal Mol Brain Section Body Doc Link PMC2694175 Disease Relevance 0 Pain Relevance 0
Although the structural details of interaction between two ADAR monomers are still unknown, the crystal structure of structurally similar cytidine deaminase APOBEC-1 homodimer has indicated that the active site in each monomer is completed only with contribution from the other partner [36].
ADAR Binding (interaction) of in ADAR
5) Confidence 0.33 Published 2009 Journal Mol Brain Section Body Doc Link PMC2694175 Disease Relevance 0.17 Pain Relevance 0
Therefore, it is possible that a heterodimer of ADAR1 and ADAR2 may result in a non-functional enzyme that could neither edit ADAR1 nor ADAR2 substrates.
ADAR1 Binding (heterodimer) of
6) Confidence 0.29 Published 2009 Journal Mol Brain Section Body Doc Link PMC2694175 Disease Relevance 0.15 Pain Relevance 0
Furthermore, it is difficult to reconcile any mechanistic hypothesis with the observed changes, given the known activities and specificities of ADAR1 and ADAR2.
ADAR1 Binding (specificities) of
7) Confidence 0.29 Published 2010 Journal Nucleic Acids Research Section Body Doc Link PMC2879535 Disease Relevance 0.43 Pain Relevance 0.36
It has recently been found that ADAR1p150 binds siRNA containing 3?
ADAR1p150 Binding (binds) of
8) Confidence 0.27 Published 2006 Journal Journal of RNAi and Gene Silencing : An International Journal of RNA and Gene Targeting Research Section Body Doc Link PMC2737212 Disease Relevance 0 Pain Relevance 0

General Comments

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