INT23669

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Context Info
Confidence 0.47
First Reported 1986
Last Reported 2010
Negated 5
Speculated 1
Reported most in Body
Documents 24
Total Number 25
Disease Relevance 11.37
Pain Relevance 2.69

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

transferase activity, transferring glycosyl groups (St8sia2) Golgi apparatus (St8sia2)
Anatomy Link Frequency
platelets 7
blood cell 4
leukocytes 3
neutrophils 2
blood 1
St8sia2 (Mus musculus)
Pain Link Frequency Relevance Heat
tetrodotoxin 30 100.00 Very High Very High Very High
sodium channel 18 99.24 Very High Very High Very High
GABA receptor 1 98.24 Very High Very High Very High
Opioid 1 97.36 Very High Very High Very High
addiction 4 96.82 Very High Very High Very High
GABAergic 6 96.00 Very High Very High Very High
Dopamine 2 95.40 Very High Very High Very High
Crohn's disease 20 95.08 Very High Very High Very High
Kinase C 12 92.96 High High
antagonist 9 78.32 Quite High
Disease Link Frequency Relevance Heat
Targeted Disruption 7 99.80 Very High Very High Very High
Hemolytic Uremic Syndrome 820 99.70 Very High Very High Very High
Infection 43 97.84 Very High Very High Very High
Graft Vs Host Disease 20 95.96 Very High Very High Very High
Disease 121 95.08 Very High Very High Very High
Increased Venous Pressure Under Development 40 94.40 High High
Systemic Lupus Erythematosus 20 93.72 High High
Stress 184 93.36 High High
Injury 60 92.80 High High
Endotoxemia 80 92.52 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The concentration dependence for TTX inhibition of both specific 3H-STX and 3H-BTX-B binding is identical, suggesting that inhibition of 3H-BTX-B binding is due to a direct effect of TTX/STX binding at their specific sodium channel site.
STX Binding (binding) of associated with tetrodotoxin, addiction and sodium channel
1) Confidence 0.47 Published 1986 Journal J. Neurosci. Section Abstract Doc Link 2426426 Disease Relevance 0 Pain Relevance 0.65
Saxitoxin (STX), its analogs, and tetrodotoxin (TTX) can inhibit the action of veratridine and ouabain leaving the cell morphologically normal.
STX Neg (inhibit) Binding (inhibit) of associated with tetrodotoxin
2) Confidence 0.36 Published 2000 Journal Toxicology Section Abstract Doc Link 11118665 Disease Relevance 0.23 Pain Relevance 0.67
The fact that TTX- and STX-modified sodium channels are blocked to sodium flux has precluded drawing any direct conclusions regarding the effect of TTX/STX on BTX binding based on electrophysiological or 22Na flux measurements.
STX Binding (binding) of associated with tetrodotoxin and sodium channel
3) Confidence 0.35 Published 1986 Journal J. Neurosci. Section Abstract Doc Link 2426426 Disease Relevance 0 Pain Relevance 0.67
The results are summarized in Table 2 and showed that Stx bound mostly to monocytes and platelets, particularly after activation, and that minimal binding to platelet-free neutrophils was detected.
Stx Binding (bound) of in monocytes
4) Confidence 0.07 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2735777 Disease Relevance 0.07 Pain Relevance 0.11
Stx has been previously shown to circulate in HUS patients bound to platelets [21] and neutrophils [41], [42] although the binding of Stx on neutrophils has been questioned [43].
Stx Binding (binding) of in platelets associated with hemolytic uremic syndrome
5) Confidence 0.07 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2735777 Disease Relevance 0.30 Pain Relevance 0
Stx could also bind to monocytes [45] (resting or activated) but did not bind to neutrophils (resting or activated).
Stx Neg (not) Binding (bind) of in neutrophils
6) Confidence 0.07 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2735777 Disease Relevance 0.40 Pain Relevance 0
Thus neutrophils circulating during the acute phase of HUS appear to be able to bind Stx and our results indicate that Stx circulates bound to leukocytes, platelets and blood cell aggregates.
Stx Binding (bound) of in leukocytes associated with hemolytic uremic syndrome
7) Confidence 0.07 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2735777 Disease Relevance 0.58 Pain Relevance 0
Furthermore, Stx can interact directly with platelets inducing their activation [27].
Stx Binding (interact) of in platelets
8) Confidence 0.07 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2735777 Disease Relevance 1.44 Pain Relevance 0.03
Interestingly, experiments using whole blood from HUS patients showed that Stx was bound to leukocyte-platelet aggregates composed either of neutrophils or of monocytes but was also present on neutrophils and monocytes that were not in complex with platelets.
Stx Binding (bound) of in blood associated with hemolytic uremic syndrome
9) Confidence 0.07 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2735777 Disease Relevance 0.32 Pain Relevance 0
We show that Stx did not bind to resting platelets in vitro (Table 2) but bound to activated platelets.
Stx Neg (not) Binding (bind) of in platelets
10) Confidence 0.07 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2735777 Disease Relevance 0.29 Pain Relevance 0
Thus neutrophils circulating during the acute phase of HUS appear to be able to bind Stx and our results indicate that Stx circulates bound to leukocytes, platelets and blood cell aggregates.
Stx Binding (bind) of in leukocytes associated with hemolytic uremic syndrome
11) Confidence 0.07 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2735777 Disease Relevance 0.58 Pain Relevance 0
We show that Stx did not bind to resting platelets in vitro (Table 2) but bound to activated platelets.
Stx Binding (bound) of in platelets
12) Confidence 0.07 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2735777 Disease Relevance 0.35 Pain Relevance 0
Determination of surface-bound TF or Stx on platelet-leukocyte aggregates was performed using a three-color analysis procedure for simultaneous detection of platelet-leukocyte aggregates and TF or Stx2 presence on blood cell aggregates.
Stx Binding (bound) of in blood cell
13) Confidence 0.05 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2735777 Disease Relevance 0 Pain Relevance 0
The interaction between Stx or LPS and blood cells induced platelet-leukocyte aggregate formation and tissue factor (TF) release, as detected by flow cytometry in whole blood.
Stx Binding (interaction) of in leukocyte
14) Confidence 0.05 Published 2009 Journal PLoS ONE Section Abstract Doc Link PMC2735777 Disease Relevance 0.26 Pain Relevance 0
As enterohemorrhagic Escherichia coli (EHEC) may cause hemolytic uremic syndrome (HUS), in which microthrombi cause tissue damage, this study investigated whether the interaction between blood cells and EHEC virulence factors Shiga toxin (Stx) and lipopolysaccharide (LPS) led to release of TF.


Stx Spec (whether) Binding (interaction) of in blood cells associated with hemolytic uremic syndrome
15) Confidence 0.05 Published 2009 Journal PLoS ONE Section Abstract Doc Link PMC2735777 Disease Relevance 0.28 Pain Relevance 0
HUS develops as a complication of Shiga toxin (Stx)-producing enterohemorrhagic Escherichia coli (EHEC) infection of which serotype O157:H7 is the most commonly detected.
Stx Binding (complication) of associated with hemolytic uremic syndrome and infection
16) Confidence 0.05 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2735777 Disease Relevance 1.58 Pain Relevance 0.08
Stx may contribute to the process by inducing endothelial cell damage [23] an effect enhanced in the presence of lipopolysaccharide (LPS) [24] which increases Stx binding [25].
Stx Binding (binding) of in endothelial cell
17) Confidence 0.05 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2735777 Disease Relevance 1.56 Pain Relevance 0.04
Stx could also bind to monocytes [45] (resting or activated) but did not bind to neutrophils (resting or activated).
Stx Neg (not) Binding (bind) of in neutrophils
18) Confidence 0.05 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2735777 Disease Relevance 0.41 Pain Relevance 0
The same investigators demonstrated rapid electrophysiological effects of STX, a diphenylacrylamide-based selective estrogen receptor modulator, in nER knockout animals; STX, which does not bind to either isoform of the nER, proved to be more potent than estradiol in their in vitro and in vivo test systems [55,56].
STX Neg (not) Binding (bind) of associated with targeted disruption
19) Confidence 0.04 Published 2010 Journal Mol Brain Section Body Doc Link PMC2841592 Disease Relevance 0.15 Pain Relevance 0.05
The synthetic nonsteroidal compound, STX binds to Gq-mER and mimics the action of E2 in ER?
STX Binding (binds) of
20) Confidence 0.03 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2910705 Disease Relevance 0.18 Pain Relevance 0.29

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