INT268028

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Context Info
Confidence 0.37
First Reported 2009
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 7
Total Number 9
Disease Relevance 0
Pain Relevance 0.61

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

ATPase activity (Abcc8) plasma membrane (Abcc8) transmembrane transport (Abcc8)
Anatomy Link Frequency
neurons 1
Schwann cells 1
Abcc8 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
addiction 6 85.08 High High
Spinal nerve ligature 135 78.08 Quite High
nociceptor 6 58.60 Quite High
Pain 81 50.00 Quite Low
potassium channel 18 50.00 Quite Low
isoflurane 21 37.12 Quite Low
anesthesia 18 36.24 Quite Low
nMDA receptor 6 31.20 Quite Low
unmyelinated 3 22.24 Low Low
Neuropathic pain 66 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Injury 30 47.60 Quite Low
Nervous System Injury 75 41.16 Quite Low
Nociception 27 37.56 Quite Low
Hypoxia 9 33.20 Quite Low
Natriuresis 6 9.52 Low Low
Neuropathic Pain 81 5.00 Very Low Very Low Very Low
Hyperalgesia 69 5.00 Very Low Very Low Very Low
Pain 33 5.00 Very Low Very Low Very Low
Death 30 5.00 Very Low Very Low Very Low
Ganglion Cysts 12 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Because the alkylating agent NEM directly interacts with this residue [59], it is likely that cysteine nitrosylation by NO modulates nucleotides-SUR1 interaction, resulting in allosteric activation of the KATP channel.
SUR1 Binding (interaction) of
1) Confidence 0.37 Published 2009 Journal Mol Pain Section Body Doc Link PMC2673211 Disease Relevance 0 Pain Relevance 0.04
Cys717 is the sole cysteine residue located on the highly conserved Walker A (ATP-binding) motifs of SURI.
SUR Binding (binding) of
2) Confidence 0.36 Published 2009 Journal Mol Pain Section Body Doc Link PMC2673211 Disease Relevance 0 Pain Relevance 0.04
To further investigate the distribution of these SUR1 positive funnel-shaped patterns at a higher resolution, we employed EM (Fig. 5) that showed binding of gold-labeled anti-SUR1 and anti-Kir6.2 antibodies on axonal membrane and in the myelin sheath, within sites that are characteristic for Schmidt-Lanterman incisures (SLI) formed by the Schwann cells (Fig. 5C, Fig. 6A).
SUR1 Binding (binding) of in Schwann cells
3) Confidence 0.33 Published 2010 Journal Mol Pain Section Body Doc Link PMC2825500 Disease Relevance 0 Pain Relevance 0.06
In neurons pre-incubated with anti-SUR1 antibody, excised patch recordings also showed KATP channel activity (Fig. 3D and 3E), but the blocking effect of glybenclamide, which binds to the SUR1 subunit, was significantly suppressed compared to that in the absence of the anti-SUR1 antibody (Fig. 3G).
SUR1 subunit Binding (binds) of in neurons
4) Confidence 0.33 Published 2010 Journal Mol Pain Section Body Doc Link PMC2825500 Disease Relevance 0 Pain Relevance 0.06
We identified this co-localization of Kir6.2 with SUR1 subunits by staining with antibody against Kir6.2, and with BODIPY-Glybenclamide, which specifically binds to SUR1 with high affinity at concentrations <40 nM [15].
SUR1 Binding (binds) of
5) Confidence 0.33 Published 2010 Journal Mol Pain Section Body Doc Link PMC2825500 Disease Relevance 0 Pain Relevance 0.41
This observation, in contrast to activation of wild type SUR1/Kir6.2 channels, indicates that NO interacts with the SUR1 subunit, rather than the Kir6.2 subunit.


SUR1 Neg (NO) Binding (interacts) of
6) Confidence 0.28 Published 2009 Journal Mol Pain Section Body Doc Link PMC2673211 Disease Relevance 0 Pain Relevance 0
Effects of cysteine mutation within nucleotide-binding domain of SUR1
SUR1 Binding (domain) of
7) Confidence 0.28 Published 2009 Journal Mol Pain Section Body Doc Link PMC2673211 Disease Relevance 0 Pain Relevance 0
In addition, the highly conserved Walker A (ATP-binding) motifs of SUR1 contain one single cysteine residue, at position 717 (C717) in NBD1.
SUR1 Binding (binding) of
8) Confidence 0.28 Published 2009 Journal Mol Pain Section Body Doc Link PMC2673211 Disease Relevance 0 Pain Relevance 0
Previous studies using mutagenesis have revealed that thiol-reagents modify KATP channel activity by interacting with a single cysteine residue at either Kir6.2 or SUR1.
SUR1 Binding (interacting) of
9) Confidence 0.27 Published 2009 Journal Mol Pain Section Body Doc Link PMC2673211 Disease Relevance 0 Pain Relevance 0

General Comments

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