INT59362

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Context Info
Confidence 0.38
First Reported 1993
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 22
Total Number 22
Disease Relevance 4.26
Pain Relevance 2.29

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

cytoplasm (PMP2)
Anatomy Link Frequency
leaflets 3
plasma 1
nodes 1
vesicles 1
PNS 1
PMP2 (Homo sapiens)
Pain Link Frequency Relevance Heat
Peripheral nervous system 112 100.00 Very High Very High Very High
Neuritis 83 99.48 Very High Very High Very High
Demyelination 40 93.28 High High
Central nervous system 72 90.92 High High
Multiple sclerosis 82 79.20 Quite High
Spinal cord 37 76.80 Quite High
Inflammation 43 75.00 Quite High
chemokine 38 75.00 Quite High
metalloproteinase 15 68.56 Quite High
Sciatic nerve 1 61.28 Quite High
Disease Link Frequency Relevance Heat
Immunization 2 100.00 Very High Very High Very High
Experimental Autoimmune Neuritis 83 99.48 Very High Very High Very High
Syndrome 139 99.24 Very High Very High Very High
Disease 67 94.92 High High
Demyelinating Disease 62 93.28 High High
Breast Cancer 3 88.20 High High
Neurodegenerative Disease 8 85.52 High High
Cancer 9 83.84 Quite High
Sprains And Strains 36 83.36 Quite High
Autoimmune Disease 5 83.00 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Binding of lipids to human P2: molecular docking simulations and fluorescence spectroscopy measurements
P2 Binding (Binding) of
1) Confidence 0.38 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858655 Disease Relevance 0 Pain Relevance 0
Thus, we further probed the interaction between human P2 and cholesterol using intrinsic Trp fluorescence.
P2 Binding (interaction) of
2) Confidence 0.38 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858655 Disease Relevance 0 Pain Relevance 0
P2 may bind myelin lipids, such as cholesterol, with high affinity, and it could interact with two apposing cytoplasmic leaflets of the multilayered myelin membrane simultaneously.
P2 Binding (bind) of in leaflets
3) Confidence 0.38 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858655 Disease Relevance 0.09 Pain Relevance 0.05
This charge distribution is shared by all the known P2 protein structures, and therefore, could be important for the interaction of P2 with two apposing membrane leaflets of myelin.
P2 Binding (interaction) of in leaflets
4) Confidence 0.38 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858655 Disease Relevance 0.29 Pain Relevance 0.18
While our experiments indicate cholesterol binding by P2, at the moment, it is unclear whether the bound cholesterol would originate from the plasma membrane or from free cholesterol.
P2 Binding (binding) of in plasma
5) Confidence 0.38 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858655 Disease Relevance 0 Pain Relevance 0
The binding of cholesterol to P2 was monitored by observing the protein fluorescence quenching induced by stoichiometric amounts of ligand.
P2 Binding (binding) of
6) Confidence 0.38 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858655 Disease Relevance 0 Pain Relevance 0
The crystal structure of human P2 was used as a starting point for lipid docking simulations, in order to investigate if the lipid constituents of myelin could be bound by P2.
P2 Binding (bound) of
7) Confidence 0.33 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858655 Disease Relevance 0 Pain Relevance 0
Experimental allergic neuritis, an animal model of GBS, is induced in laboratory animals by immunization with myelin P2 protein, some peptides of P2 protein, and galactocerebroside.
P2 protein Binding (immunization) of associated with syndrome, experimental autoimmune neuritis, immunization and neuritis
8) Confidence 0.31 Published 1993 Journal Pediatr. Res. Section Abstract Doc Link 8381954 Disease Relevance 1.43 Pain Relevance 0.30
A comparison between the three currently available crystal structures for P2 indicates a conformational change at the mouth of the lipid-binding cavity, involving Phe57, which lies in a loop between ?
P2 Binding (binding) of in cavity
9) Confidence 0.29 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858655 Disease Relevance 0 Pain Relevance 0
However, whether this is a result of the N-terminal segment binding to DPC micelles, of the binding of monomeric DPC inside P2, or both, remains a subject for future studies.


P2 Binding (binding) of in terminal segment
10) Confidence 0.29 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858655 Disease Relevance 0 Pain Relevance 0
Binding of lipids to human P2: molecular docking simulations and fluorescence spectroscopy measurements
P2 Binding (Binding) of
11) Confidence 0.29 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858655 Disease Relevance 0 Pain Relevance 0
Purification of recombinant human P2
P2 Binding (recombinant) of
12) Confidence 0.29 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858655 Disease Relevance 0.15 Pain Relevance 0
P2 may bind myelin lipids, such as cholesterol, with high affinity, and it could interact with two apposing cytoplasmic leaflets of the multilayered myelin membrane simultaneously.
P2 Binding (bind) of in leaflets
13) Confidence 0.29 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858655 Disease Relevance 0.09 Pain Relevance 0.05
The results do show that recombinant human P2 is folded, as expected, into a mainly ?
P2 Binding (recombinant) of
14) Confidence 0.29 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858655 Disease Relevance 0 Pain Relevance 0.03
Docking experiments using the high-resolution crystal structure identified cholesterol, one of the most abundant lipids in myelin, as a possible ligand for P2, a hypothesis that was proven by fluorescence spectroscopy.
P2 Binding (ligand) of
15) Confidence 0.28 Published 2010 Journal PLoS ONE Section Abstract Doc Link PMC2858655 Disease Relevance 0 Pain Relevance 0
Our recent neutron scattering experiments, indeed, have shown that upon binding to lipid bilayers, P2 decreases the lipid dynamics [7].
P2 Binding (binding) of
16) Confidence 0.28 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858655 Disease Relevance 0 Pain Relevance 0.31
Tryptophan fluorescence analysis of cholesterol binding to P2
P2 Binding (binding) of
17) Confidence 0.28 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858655 Disease Relevance 0 Pain Relevance 0
The crystal structure of human P2 was used as a starting point for lipid docking simulations, in order to investigate if the lipid constituents of myelin could be bound by P2.
P2 Binding (bound) of
18) Confidence 0.28 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858655 Disease Relevance 0 Pain Relevance 0
In future studies, we aim to investigate whether P2 is able to bind cholesterol from vesicles, in experiments analogous to those reported for NPC2 [62], [63].


P2 Binding (bind) of in vesicles
19) Confidence 0.28 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2858655 Disease Relevance 0.07 Pain Relevance 0.04
For integrating pathways P1 and P2, as in Figure 1A, PINT uses the following criteria to determine if nodes N1 and N2 can be linkers:
P2 Binding (integrating) of in nodes
20) Confidence 0.14 Published 2010 Journal Nucleic Acids Research Section Body Doc Link PMC2896112 Disease Relevance 0 Pain Relevance 0

General Comments

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