INT292328

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Context Info
Confidence 0.11
First Reported 2010
Last Reported 2010
Negated 0
Speculated 1
Reported most in Body
Documents 1
Total Number 13
Disease Relevance 0.24
Pain Relevance 0.10

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) mitochondrion (Sds) lyase activity (Sds)
cellular_component (Sds) cellular amino acid metabolic process (Sds) cytoplasm (Sds)
Anatomy Link Frequency
cavities 1
cavity 1
Sds (Rattus norvegicus)
Mb (Rattus norvegicus)
Pain Link Frequency Relevance Heat
imagery 13 89.84 High High
ketamine 13 5.00 Very Low Very Low Very Low
anesthesia 13 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Depression 13 95.04 Very High Very High Very High
Alzheimer's Dementia 91 38.44 Quite Low
Adult Respiratory Distress Syndrome 117 22.44 Low Low
Pulmonary Alveolar Proteinosis 39 5.00 Very Low Very Low Very Low
Infant Respiratory Distress Syndrome 26 5.00 Very Low Very Low Very Low
Primary Sclerosing Cholangitis 13 5.00 Very Low Very Low Very Low
Body Weight 13 5.00 Very Low Very Low Very Low
Adhesions 13 5.00 Very Low Very Low Very Low
Interstitial Lung Diseases 13 5.00 Very Low Very Low Very Low
Injury 13 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The binding of SDS to the “0 nsec” dimer S-MB appears to be concentrated in two surface cavities near the center of the dimer peptide in Fig. 11A, and these two shallow depressions containing SDS are themselves related by the aforementioned two-fold axis.
SDS Binding (binding) of dimer S-MB in cavities associated with depression
1) Confidence 0.11 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0.10 Pain Relevance 0
Using input structures from ZDOCK and RosettaDock searches, MD simulations produced a “10 nsec” structure (Figs. 11B and 12) confirming the dimer S-MB may bind SDS to form a stable complex in water.
SDS Binding (bind) of dimer S-MB
2) Confidence 0.10 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
It is of particular interest that the “10 nsec” model for the dimer peptide in SDS (Figs. 11B and 12) may represent membrane-bound dimer S-MB, where the dimer adopts a relatively open ‘saposin-like’ conformation when interacting with membrane lipids.
SDS Binding (bound) of dimer S-MB
3) Confidence 0.10 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 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 (organization) of dimer S-MB
4) Confidence 0.10 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0.03
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 dimer S-MB in cavity
5) Confidence 0.10 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0.08 Pain Relevance 0
Our “10 nsec” model (Figs. 11B and 12) shows that dimer S-MB integrates a partial SDS micelle into its structure, which then separates the antiparallel ?
SDS Spec (partial) Binding (integrates) of dimer S-MB
6) Confidence 0.09 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
Our subsequent finding that S-MB, but not MB, primarily exists as a dimer in SDS-PAGE (Fig. 8) prompted us to next perform MD simulations to characterize the 3D-structure of dimeric S-MB peptide in SDS and water.
SDS Binding (dimer) of MB
7) Confidence 0.09 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
Our subsequent finding that S-MB, but not MB, primarily exists as a dimer in SDS-PAGE (Fig. 8) prompted us to next perform MD simulations to characterize the 3D-structure of dimeric S-MB peptide in SDS and water.
SDS Binding (dimer) of MB
8) Confidence 0.09 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
These SPR results indicating much higher self-association for S-MB than that noted for MB are supportive of our SDS-PAGE findings indicating dimer formation for S-MB but not for MB (Fig. 8).


SDS Binding (formation) of MB
9) Confidence 0.08 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.
SDS Binding (bound) of dimer S-MB
10) Confidence 0.08 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0.04
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 dimer S-MB
11) Confidence 0.08 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0.07 Pain Relevance 0
These SPR results indicating much higher self-association for S-MB than that noted for MB are supportive of our SDS-PAGE findings indicating dimer formation for S-MB but not for MB (Fig. 8).


SDS Binding (formation) of MB
12) Confidence 0.08 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 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 dimer S-MB
13) Confidence 0.08 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0.03

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