INT121077

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Context Info
Confidence 0.25
First Reported 2004
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 20
Total Number 20
Disease Relevance 1.41
Pain Relevance 0.28

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

mitochondrion (Sds) lyase activity (Sds) cellular_component (Sds)
cellular amino acid metabolic process (Sds) cytoplasm (Sds)
Anatomy Link Frequency
cavity 7
Sds (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Opioid 6 75.00 Quite High
imagery 16 56.16 Quite High
analgesia 1 48.08 Quite Low
antinociception 1 33.36 Quite Low
Neurotransmitter 1 20.08 Low Low
anesthesia 18 15.92 Low Low
ketamine 18 13.68 Low Low
Inflammation 42 5.00 Very Low Very Low Very Low
Inflammatory response 12 5.00 Very Low Very Low Very Low
alcohol 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Vomiting 10 99.16 Very High Very High Very High
Overactive Bladder 2 98.28 Very High Very High Very High
Recurrence 6 98.00 Very High Very High Very High
Depression 16 73.52 Quite High
Stress 4 68.32 Quite High
Bone Cancer 2 11.68 Low Low
Osteoporosis 6 9.72 Low Low
Sperm Disorder 2 6.88 Low Low
Adult Respiratory Distress Syndrome 144 5.00 Very Low Very Low Very Low
Alzheimer's Dementia 112 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
There was also a strong association between SDS scores and CMEs for nausea, vomiting, and voiding and general recovery validation measures, although the association was significantly weaker than that for symptom-specific validation measures.
SDS Binding (association) of associated with vomiting and overactive bladder
1) Confidence 0.25 Published 2004 Journal Anesth. Analg. Section Abstract Doc Link 15333398 Disease Relevance 1.03 Pain Relevance 0.26
mL of water, and any MTT-formazan formed by SDH activity in the cells was solubilized with 6% dimethylsulfoxide–NaOH (0.1?
SDH Binding (activity) of
2) Confidence 0.18 Published 2010 Journal International Journal of Biomaterials Section Body Doc Link PMC2927743 Disease Relevance 0 Pain Relevance 0
Our results showed an increase in SDH activity by 48?
SDH Binding (activity) of
3) Confidence 0.18 Published 2010 Journal International Journal of Biomaterials Section Body Doc Link PMC2927743 Disease Relevance 0.16 Pain Relevance 0
However, the activities of SDH and LDH were significantly decreased by ?
SDH Binding (activities) of
4) Confidence 0.17 Published 2010 Journal J Biomed Sci Section Body Doc Link PMC2994374 Disease Relevance 0.07 Pain Relevance 0
Maximum levels of SDS bound to proteins (or peptides) occur at ?
SDS Binding (bound) of
5) Confidence 0.14 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
Our MD simulations suggest that the N-terminal insertion sequence is critical for maintaining the dimer S-MB structure, because this hydrophobic sequence and the bundle of N- and C-terminal helices together make up the interior surface of the exposed cavity which binds SDS (see below).
SDS Binding (binds) of in cavity
6) Confidence 0.14 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
MW determinations for proteins and peptides in SDS-PAGE are possible because SDS molecules bind with high affinity to both hydrophobic protein sites [89] and positively-charged amino acid residues, and also because a consistent amount of detergent generally binds to proteins [90].
SDS Binding (bind) of
7) Confidence 0.14 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
The interior of this central cavity in dimer S-MB is now lined with hydrophobic amino-acid sidechains capable of interacting with hydrophobic detergents such as SDS.
SDS Binding (interacting) of in cavity
8) Confidence 0.11 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0.07 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.
SDS Binding (interactions) of
9) Confidence 0.11 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0.03
3 nsec, confirming that the dimer S-MB-SDS complex is stable in water for the 10 nsec run.
SDS Binding (complex) of
10) Confidence 0.11 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
In our present SDS-PAGE study, MB was initially dissolved in the loading buffer at ?
SDS Binding (study) of
11) Confidence 0.11 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
The reorganization of bound SDS likely provides the thermodynamic driving force for the conversion of the dimer S-MB-SDS complex to the oblate spheroid conformation (i.e., “10 nsec” structure”) in Fig. 11B.
SDS Binding (bound) of
12) Confidence 0.11 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
This restructuring of bound SDS is also probably responsible for the lengthwise narrowing of the central portion of dimer S-MB, in which the distance between the ?
SDS Binding (bound) of
13) Confidence 0.11 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
In the “0 nsec” dimer S-MB structure of Fig. 11A, anionic SDS closely associates not only with exposed nonpolar residues through hydrophobic interactions, but also with positively-charged Arg and Lys residues through electrostatic interactions.
SDS Binding (associates) of
14) Confidence 0.11 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0.07 Pain Relevance 0
The effective clamping down on the bound SDS molecules by the dimer S-MB leaves in the “10 nsec” structure is probably due to strong hydrophobic interactions between the SDS detergent molecules and the nonpolar sidechains that project from the backbones of the helical bundle and the N-terminal sequence in the interior of the cavity (Fig. 12A).
SDS Binding (interactions) of in cavity
15) Confidence 0.11 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
Also contributing to the stability of the dimer S-MB complex are the Arg and Lys residues at the surface periphery of the cavity, which form electrostatic interactions between the negatively-charged headgroups of SDS and the positively-charged Arg (residues 12A, 17A, 12B and 17B) and Lys (16A, 24A, 16B and 24B).
SDS Binding (interactions) of in cavity
16) Confidence 0.11 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
SDS molecules predominately bind to an exposed central cavity formed by the hydrophobic residues that line the concave side of the “10 nsec” dimer S-MB model; contrarily, few SDS bind to the opposing convex side that is enriched with polar and positively-charged residues (Figs. 11 and 12).
SDS Binding (bind) of in cavity
17) Confidence 0.11 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
SDS molecules predominately bind to an exposed central cavity formed by the hydrophobic residues that line the concave side of the “10 nsec” dimer S-MB model; contrarily, few SDS bind to the opposing convex side that is enriched with polar and positively-charged residues (Figs. 11 and 12).
SDS Binding (bind) of in cavity
18) Confidence 0.11 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
MW determinations for proteins and peptides in SDS-PAGE are possible because SDS molecules bind with high affinity to both hydrophobic protein sites [89] and positively-charged amino acid residues, and also because a consistent amount of detergent generally binds to proteins [90].
SDS Binding (binds) of
19) Confidence 0.11 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
The effective clamping down on the bound SDS molecules by the dimer S-MB leaves in the “10 nsec” structure is probably due to strong hydrophobic interactions between the SDS detergent molecules and the nonpolar sidechains that project from the backbones of the helical bundle and the N-terminal sequence in the interior of the cavity (Fig. 12A).
SDS Binding (bound) of in cavity
20) Confidence 0.11 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0

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