INT646

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Context Info
Confidence 0.41
First Reported 1977
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 37
Total Number 37
Disease Relevance 6.13
Pain Relevance 2.25

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

transport (Mb)
Anatomy Link Frequency
plasma 2
chest 2
cavities 1
C16 1
brain 1
Mb (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Angina 23 99.44 Very High Very High Very High
cocaine 9 99.08 Very High Very High Very High
addiction 4 97.08 Very High Very High Very High
Potency 6 88.36 High High
imagery 23 84.12 Quite High
Mechanosensation 2 72.16 Quite High
Pain 1 70.52 Quite High
ischemia 1 57.44 Quite High
anesthesia 24 25.00 Low Low
ketamine 23 10.44 Low Low
Disease Link Frequency Relevance Heat
Myocardial Infarction 37 99.56 Very High Very High Very High
Angina 20 99.44 Very High Very High Very High
Coronary Artery Disease 4 99.28 Very High Very High Very High
Emergencies 3 98.12 Very High Very High Very High
Rhabdomyolysis 9 97.96 Very High Very High Very High
Cv General 3 Under Development 3 96.36 Very High Very High Very High
Cocaine Dependence 1 81.20 Quite High
Alzheimer's Dementia 161 78.84 Quite High
Disease 3 77.88 Quite High
Hypertension 1 76.56 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Plasma myoglobin appeared to be more sensitive than creatine kinase-MB for the early diagnosis of acute myocardial infarction; using a cut-off value of 100 micrograms/l, 90% of acute myocardial infarction cases were correctly recognized by plasma myoglobin 6 hours after the onset of chest pain, with a diagnostic specificity of 100% for non-acute myocardial infarction chest pain subjects.
plasma myoglobin Binding (recognized) of in Plasma associated with angina and myocardial infarction
1) Confidence 0.41 Published 1994 Journal Eur J Clin Chem Clin Biochem Section Abstract Doc Link 8086517 Disease Relevance 0.74 Pain Relevance 0.28
Control SPR experiments examining the binding of S-MB to chipped MB, and also MB to chipped S-MB, produced not only low-response sensorgrams which nearly overlap that obtained for MB binding to chipped MB (Fig. 10), but also higher KD values than that observed for S-MB binding to itself (Table 2).
MB Binding (binding) of
2) Confidence 0.33 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
Consistent with this are SPR results indicating that MB will bind to either DPPC or the synthetic lipid DEPN-8 with high affinity [16].
MB Binding (bind) of
3) Confidence 0.33 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
We conclude that a combination of creatine kinase-MB and troponin T during the first 6 hours enables early detection or exclusion of acute myocardial infarction in this population.
kinase-MB Binding (combination) of associated with myocardial infarction
4) Confidence 0.31 Published 2000 Journal Am. J. Cardiol. Section Abstract Doc Link 11113415 Disease Relevance 0.34 Pain Relevance 0.17
3 nsec, confirming that the dimer S-MB-SDS complex is stable in water for the 10 nsec run.
dimer S-MB Binding (complex) of
5) Confidence 0.29 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
Because both saposin C (Fig. 1) [20] and the “10 nsec” dimer S-MB model (Figs. 11B and 12) share an open, ‘saposin-like’ conformation when bound to submicellar SDS, it is tempting to speculate that dimer S-MB may exert its surfactant activities by analogously binding to lipid bilayers and monolayers.
dimer S-MB Binding (binding) of
6) Confidence 0.29 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0.04
Because MB and S-MB are each likely exposed to water when bound to lipids at the polar headgroup region [30], [49], [97], we anticipate that our PASTA and AGGRESCAN results in Fig. 9 will also accurately forecast aggregated domains in MB and S-MB.
MB Binding (bound) of
7) Confidence 0.28 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0.36 Pain Relevance 0
The respective binding affinities of S-MB and MB, both to themselves (self-association) and to each other (cross-association), were measured with surface plasmon resonance (SPR) spectroscopy using a Biacore 3000 system (Biacore, Uppsala, Sweden) [16], [59].
MB Binding (affinities) of
8) Confidence 0.28 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
Control SPR experiments examining the binding of S-MB to chipped MB, and also MB to chipped S-MB, produced not only low-response sensorgrams which nearly overlap that obtained for MB binding to chipped MB (Fig. 10), but also higher KD values than that observed for S-MB binding to itself (Table 2).
MB Binding (binding) of
9) Confidence 0.28 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
SPR, predictive aggregation algorithms, and MD and docking simulations further suggested a preliminary model for dimeric S-MB with SDS, in which monomers non-covalently associate to form a dimer S-MB peptide with a ‘saposin-like’ fold in both aqueous and lipid environments.
MB Binding (associate) of
10) Confidence 0.25 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
-sheet, MB likely assumes ?
MB Binding (sheet) of
11) Confidence 0.25 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0.06 Pain Relevance 0
Each monomer in the “10 nsec” dimer S-MB model optimizes its interactions with SDS, yet the overall organization of the dimer S-MB and its local two-fold axis are still retained.
dimer S-MB Binding (interactions) of
12) Confidence 0.25 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0.03
Conceivably, an analogous dimer S-MB model may also account for the strong binding of S-MB to itself seen in SPR studies (Fig. 10; Table 2).
MB Binding (binding) of
13) Confidence 0.25 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
An independent analysis of the self-associating domains in MB was similarly conducted with AGGRESCAN, a predictive algorithm which combines the known aggregation tendency of amino acids with earlier findings that short sequences (?
MB Binding (associating) of
14) Confidence 0.25 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0.07 Pain Relevance 0
Nevertheless, these interpeptide interactions are apparently too weak to promote oligomers for MB on SDS-PAGE, as only the monomer was observed in Fig. 8.
MB Binding (oligomers) of
15) Confidence 0.25 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
Given that MB and S-MB in lipids and lipid-mimics show similarly high ?
MB Binding (show) of
16) Confidence 0.25 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
Conventional 12C-FTIR spectroscopy indicated that oxidized MB has elevated ?
MB Binding (oxidized) of
17) Confidence 0.25 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
Because MB and S-MB are each likely exposed to water when bound to lipids at the polar headgroup region [30], [49], [97], we anticipate that our PASTA and AGGRESCAN results in Fig. 9 will also accurately forecast aggregated domains in MB and S-MB.
MB Binding (bound) of
18) Confidence 0.24 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0.36 Pain Relevance 0
Because S-MB predominately formed dimers in the above SDS-PAGE (see above), potential 3D-interactions between S-MB monomers were next assessed with several docking algorithms.
MB Binding (interactions) of
19) Confidence 0.24 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
The above results also indicate not only that the extended N-terminal insertion sequence (residues 1–12) anchors the dimer S-MB in lipids and promotes the self-association of S-MB, but also that these two structural properties may be antagonistic to some extent.
MB Binding (association) of
20) Confidence 0.24 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0.04

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