INT177338

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Context Info
Confidence 0.44
First Reported 2004
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 21
Total Number 21
Disease Relevance 1.14
Pain Relevance 0.42

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

transmembrane transporter activity (SV2A) endoplasmic reticulum (SV2A) cytoplasm (SV2A)
Anatomy Link Frequency
CAR 12
muscle 1
SV2A (Homo sapiens)
Pain Link Frequency Relevance Heat
Neurotransmitter 9 93.56 High High
Kinase C 12 89.76 High High
Neuropathic pain 8 77.36 Quite High
Action potential 1 48.16 Quite Low
gABA 1 36.72 Quite Low
GABA receptor 1 34.72 Quite Low
Spinal cord 6 34.52 Quite Low
agonist 25 14.00 Low Low
Central nervous system 2 9.68 Low Low
Paracetamol 12 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Spasticity 31 96.28 Very High Very High Very High
Epilepsy 8 81.44 Quite High
Neuropathic Pain 8 77.36 Quite High
Dyskinesias 8 74.80 Quite High
Cerebral Palsy 1 72.32 Quite High
Muscle Hypertonia 1 70.20 Quite High
Contracture 1 66.16 Quite High
Hypersensitivity 1 49.12 Quite Low
Shock 1 21.88 Low Low
Colon Cancer 24 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Indirect evidence for this assumption is provided by the observation that among all variants human CAR-specific ligand CITCO solely induced the interaction of CAR(SV2) with coactivators.
SV2 Binding (interaction) of in CAR
1) Confidence 0.44 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0
The missing DNA binding activity of CAR(SV5) is in agreement with the observation that the structural similar mouse CAR2 also did not bind to DNA [15].
SV5 Binding (binding) of in CAR
2) Confidence 0.44 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0.04
causes the loss of constitutive coactivator interaction of CAR(SV2) and of the other isoforms, as they all are compromised in heterodimerization with RXR?.
SV2 Binding (interaction) of in CAR
3) Confidence 0.44 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0
In contrast, interaction of CAR(SV2) with coactivators was strongly induced.
SV2 Binding (interaction) of in CAR
4) Confidence 0.44 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0
The recent finding that SV2 binds adenine nucleotides suggests that its action may regulate or be regulated by synaptic energy levels [18].
SV2 Binding (binds) of
5) Confidence 0.41 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2669215 Disease Relevance 0.23 Pain Relevance 0.08
Likewise CAR(SV5) is probably impaired in ligand binding, as homology modeling of the CAR LBD has shown that residues of helices H10/11 and H12 should participate in the ligand binding cavity [20].
SV5 Binding (binding) of in CAR
6) Confidence 0.39 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0
Thus we assume that CAR(SV2) is the only variant capable of ligand binding.
SV2 Binding (binding) of in CAR
7) Confidence 0.39 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0
Altogether ligand-dependent coactivator interaction suggests a possible functional role for CAR(SV2).
SV2 Binding (role) of in CAR
8) Confidence 0.34 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0
Furthermore, CAR(SV3) transactivation activity and interaction with RXR?
SV3 Binding (interaction) of in CAR
9) Confidence 0.33 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0.03
The missing DNA binding activity of CAR(SV5) is in agreement with the observation that the structural similar mouse CAR2 also did not bind to DNA [15].
SV5 Binding (activity) of in CAR
10) Confidence 0.33 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0.04
In agreement with their impaired DNA binding, CAR protein variants SV2, SV4, SV5 and SV6 did not transactivate significantly either reporter gene construct tested.
SV5 Binding (binding) of in CAR
11) Confidence 0.33 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0.04
We recently reported that SV2 binds nucleotides, a feature that has also been reported for another MF family member, the human glucose transporter 1 (Glut1).
SV2 Binding (binds) of
12) Confidence 0.31 Published 2009 Journal PLoS ONE Section Abstract Doc Link PMC2669215 Disease Relevance 0 Pain Relevance 0.05
SVOP appears to have a binding site located in a region spanning transmembrane domains 9–12, whereas SV2 has two binding sites in its large cytoplasmic domains preceding transmembrane domains 1 and 7 [18].
SV2 Binding (binding) of
13) Confidence 0.30 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2669215 Disease Relevance 0 Pain Relevance 0
Dose dependent studies indicated that SVOP demonstrates the highest affinity for NAD, in contrast to SV2, which binds both NAD and ATP with equal affinity.
SV2 Binding (binds) of
14) Confidence 0.30 Published 2009 Journal PLoS ONE Section Abstract Doc Link PMC2669215 Disease Relevance 0 Pain Relevance 0.03
We recently reported that SV2 binds nucleotides.
SV2 Binding (binds) of
15) Confidence 0.30 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2669215 Disease Relevance 0.20 Pain Relevance 0.07
Unexpectedly, even CAR(SV5) which lacks the last 42 residues did not show decreased nuclear localization.
SV5 Neg (lacks) Binding (lacks) of in CAR
16) Confidence 0.30 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0
CAR(SV5)) are characterized by loss of ?
SV5 Binding (characterized) of in CAR
17) Confidence 0.30 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0
0.75 mM for ATP), SV2 shows an equal affinity for both NAD and ATP (?
SV2 Binding (affinity) of
18) Confidence 0.27 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2669215 Disease Relevance 0 Pain Relevance 0
A comparison of the binding sites in SVOP, SV2 and Glut1 is depicted in Figure 7, which indicate the nucleotide binding sites are different among them.
SV2 Binding (binding) of
19) Confidence 0.26 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2669215 Disease Relevance 0 Pain Relevance 0
In the studies reported here we report that both SVOP and SV2 are nucleotide-binding proteins although both the binding site and nucleotide preference differ between the two proteins.
SV2 Binding (binding) of
20) Confidence 0.26 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2669215 Disease Relevance 0 Pain Relevance 0

General Comments

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