INT292353

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Context Info
Confidence 0.08
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 8
Disease Relevance 0.68
Pain Relevance 0

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

extracellular space (Sftpb) extracellular region (Sftpb) molecular_function (Sftpb)
lipid metabolic process (Sftpb) lysosome (Sftpb) cytoplasm (Sftpb)
Anatomy Link Frequency
lung 2
Sftpb (Rattus norvegicus)
Pain Link Frequency Relevance Heat
imagery 8 36.36 Quite Low
ketamine 8 5.00 Very Low Very Low Very Low
anesthesia 8 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Shock 8 96.68 Very High Very High Very High
Interstitial Lung Diseases 8 85.04 High High
Infection 8 80.48 Quite High
Respiratory Distress 8 63.36 Quite High
Infant Respiratory Distress Syndrome 16 61.60 Quite High
Adult Respiratory Distress Syndrome 72 49.52 Quite Low
Alzheimer's Dementia 56 5.00 Very Low Very Low Very Low
Pulmonary Alveolar Proteinosis 24 5.00 Very Low Very Low Very Low
Primary Sclerosing Cholangitis 8 5.00 Very Low Very Low Very Low
Body Weight 8 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
This general approach has been previously used to investigate MD-simulated interactions between lipids and SP-B(1–25) [101]–[104].
SP-B Binding (interactions) of
1) Confidence 0.08 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
In the open conformation, the exposed amphipathic helices of SP-B would bind to lipid by inserting its hydrophobic residues to interact with fatty acyl chains, while charged and neutral residues would associate with the more polar lipid headgroup region [5], [30].
SP-B Binding (bind) of
2) Confidence 0.07 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
The cationic N-terminus of SP-B may here interact with anionic lipids to remove the driving force for lipid squeeze-out from the surface film [31], [32].
SP-B Binding (interact) of
3) Confidence 0.07 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0.10 Pain Relevance 0
Besides promoting peptide self-association, these and prior investigations with SP-B analogs indicate that the hydrophobic N-terminal insertion sequence may assist in anchoring S-MB into lipid bilayers and monolayers.
SP-B Binding (association) of
4) Confidence 0.07 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
Lastly, circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopy of native SP-B in membrane mimics indicated high ?
SP-B Binding (spectroscopy) of
5) Confidence 0.07 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
These findings are broadly supportive of previous experiments indicating that the dimeric full-length SP-B, associated through either covalent or non-covalent linkages, shows elevated in vitro and in vivo surfactant activities over those of the monomeric protein [92], [115].
SP-B Binding (associated) of
6) Confidence 0.06 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0 Pain Relevance 0
Despite dipalmitoyl phosphatidylcholine and phosphatidylglycerol constituting its main phospholipid components, the biophysical activity of surfactant in the lung largely depends on the presence of the hydrophobic surfactant protein B (SP-B), and to a lesser degree on the extremely hydrophobic surfactant protein C (SP-C) [3]–[5].
surfactant protein B Binding (presence) of in lung
7) Confidence 0.06 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0.29 Pain Relevance 0
Despite dipalmitoyl phosphatidylcholine and phosphatidylglycerol constituting its main phospholipid components, the biophysical activity of surfactant in the lung largely depends on the presence of the hydrophobic surfactant protein B (SP-B), and to a lesser degree on the extremely hydrophobic surfactant protein C (SP-C) [3]–[5].
SP-B Binding (presence) of in lung
8) Confidence 0.06 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2805716 Disease Relevance 0.29 Pain Relevance 0

General Comments

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