INT113865

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Context Info
Confidence 0.46
First Reported 2003
Last Reported 2009
Negated 3
Speculated 1
Reported most in Body
Documents 35
Total Number 36
Disease Relevance 3.18
Pain Relevance 1.12

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

extracellular space (CXADR) extracellular region (CXADR) cell adhesion (CXADR)
mitochondrion organization (CXADR) plasma membrane (CXADR) nucleus (CXADR)
Anatomy Link Frequency
CAR 30
uterine 1
knob 1
CXADR (Homo sapiens)
Pain Link Frequency Relevance Heat
agonist 61 100.00 Very High Very High Very High
Kinase C 27 98.84 Very High Very High Very High
Paracetamol 29 90.44 High High
Analgesic 1 66.04 Quite High
Hypoesthesia 1 46.52 Quite Low
peripheral neuropathy 2 44.40 Quite Low
imagery 42 32.00 Quite Low
Antiemetics 1 25.00 Low Low
anesthesia 3 24.64 Low Low
isoflurane 3 23.12 Low Low
Disease Link Frequency Relevance Heat
Cancer 88 100.00 Very High Very High Very High
Ocular Toxicity (including Many Sub-types) 23 100.00 Very High Very High Very High
Small Cell Lung Cancer 4 100.00 Very High Very High Very High
Cervical Cancer 2 100.00 Very High Very High Very High
Thymoma 2 100.00 Very High Very High Very High
Infection 96 99.80 Very High Very High Very High
Malignant Neoplastic Disease 4 98.92 Very High Very High Very High
Breast Cancer 14 98.68 Very High Very High Very High
Vomiting 1 98.40 Very High Very High Very High
Carcinoma 3 93.36 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
seems to be the mechanism underlying the loss of DNA binding of the CAR isoforms.
CAR Binding (binding) of in CAR
1) Confidence 0.46 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0.04
Usually, CAR binds to DNA as a heterodimer with RXR.
CAR Binding (binds) of in CAR
2) Confidence 0.46 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0.10
Constitutive and ligand-induced interaction of CAR isoforms with coactivators
CAR Binding (interaction) of in CAR
3) Confidence 0.46 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0
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.
CAR Binding (interaction) of in CAR
4) Confidence 0.46 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.
CAR Binding (interaction) of in CAR
5) Confidence 0.46 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0
causes the loss of constitutive coactivator interaction of CAR(SV2) and of the other isoforms, as they all are compromised in heterodimerization with RXR?.
CAR Binding (interaction) of in CAR
6) Confidence 0.46 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0
We showed that none of the CAR protein variants bind to DNA as a heterodimer with RXR?.
CAR Binding (bind) of in CAR
7) Confidence 0.46 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0.05
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].
CAR Binding (binding) of in CAR
8) Confidence 0.46 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0.04
To transactivate the expression of its target genes, CAR has to bind to its response elements as a heterodimer with RXR?.
CAR Binding (bind) of in CAR
9) Confidence 0.46 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0.03
Reference CAR(SV1) showed a strong constitutive interaction with the coactivators tested.
CAR Binding (interaction) of in CAR
10) Confidence 0.40 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0
As expected, the human CAR-specific ligand CITCO enhanced interaction of reference CAR(SV1) with each of the coactivators analyzed.
CAR Spec (analyzed) Binding (interaction) of in CAR
11) Confidence 0.40 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0
To investigate DNA binding of CAR variant proteins to response elements in the XREM of CYP3A4 [17] and in the -7.8 kb enhancer of MDR1 (Burk et al., to be published elsewhere), we performed electrophoretic mobility shift assays using in vitro translated RXR?
CAR Binding (binding) of in CAR
12) Confidence 0.36 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0.05
However, only reference CAR(SV1) was able to bind to the CAR-response elements DR3 of CYP3A4-XREM (Fig. 3C) and DR4(I) of MDR1 -7.8 kb enhancer (data not shown) as a heterodimer with RXR?.


CAR Binding (bind) of in CAR
13) Confidence 0.36 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0.04
For example, TCPOBOP and CITCO are agonistic ligands of mouse CAR and human CAR, respectively [9,10].
CAR Binding (ligands) of in CAR
14) Confidence 0.36 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0.10
For example, TCPOBOP and CITCO are agonistic ligands of mouse CAR and human CAR, respectively [9,10].
CAR Binding (ligands) of in CAR
15) Confidence 0.36 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0.10
CAR protein variants show compromised heterodimerization and DNA binding activities
CAR Binding (heterodimerization) of in CAR
16) Confidence 0.36 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0.03
Analyzing the sequences of 23 clones containing the complete open reading frame, we identified the originally published CAR cDNA sequence [4] here referred to as SV1 (8 clones), and the splicing variants SV2 (11 clones), SV4 (3 clones) and SV6 (1 clone) which arise from three different alternative splicing events (Fig. 1A), all resulting in ligand binding domain variant CAR proteins.
CAR Binding (binding) of in CAR
17) Confidence 0.36 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).
CAR Binding (role) of in CAR
18) Confidence 0.36 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0
CAR protein variants show compromised heterodimerization and DNA binding activities
CAR Binding (binding) of in CAR
19) Confidence 0.36 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0.03
CAR demonstrates constitutive interaction with coactivators, which is further enhanced by ligand binding [9].
CAR Binding (interaction) of in CAR
20) Confidence 0.36 Published 2004 Journal Nucl Recept Section Body Doc Link PMC406421 Disease Relevance 0 Pain Relevance 0

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