INT32781

Context Info Confidence 0.47 First Reported 1985 Last Reported 2010 Negated 0 Speculated 2 Reported most in Body Documents 7 Total Number 11 Disease Relevance 4.31 Pain Relevance 1.98

extracellular region (Vip)

Anatomy Link Frequency pituitary 2 regulatory T cell 2 skeleton 1 Vip (Mus musculus)

Pain Link Frequency Relevance Heat rheumatoid arthritis 99 99.60 monoamine 2 99.36 Inflammation 114 97.28 Serotonin 2 97.24 Neurotransmitter 6 93.92 cytokine 204 89.84 Peripheral nervous system 3 87.20 Central nervous system 69 82.88 Potency 2 79.04 agonist 2 76.64

Disease Link Frequency Relevance Heat Rheumatoid Arthritis 99 99.60 Fatigue 33 98.40 Autoimmune Disease 57 98.28 Nociception 6 97.32 INFLAMMATION 147 97.28 Hypoxia 9 95.76 Increased Venous Pressure Under Development 6 86.60 Pneumonia 117 82.96 Sprains And Strains 108 82.16 Bacterial Meningitis 18 78.80

Sentences Mentioned In

Key:

Protein

Mutation

Event

Anatomy

Negation

Speculation

Pain term

Disease term

We have examined the interactions, in eliciting cAMP accumulation, between vasoactive intestinal polypeptide (VIP) and the three monoamines norepinephrine (NE), histamine (HIS), and serotonin (5-hydroxytryptamine, 5-HT) in mouse cerebral cortical slices.

vasoactive intestinal polypeptide Spec (examined) Binding (interactions) of associated with serotonin and monoamine

1) Confidence 0.47 Published 1985 Journal J. Neurosci. Section Abstract Doc Link 2983040 Disease Relevance 0 Pain Relevance 0.34

We have examined the interactions, in eliciting cAMP accumulation, between vasoactive intestinal polypeptide (VIP) and the three monoamines norepinephrine (NE), histamine (HIS), and serotonin (5-hydroxytryptamine, 5-HT) in mouse cerebral cortical slices.

VIP Spec (examined) Binding (interactions) of associated with serotonin and monoamine

2) Confidence 0.46 Published 1985 Journal J. Neurosci. Section Abstract Doc Link 2983040 Disease Relevance 0 Pain Relevance 0.34

The biological effects of VIP are mediated by G protein-coupled receptors (VPAC1 and VPAC2) that bind VIP and pituitary adenylate cyclase-activating polypeptide (PACAP) with equal affinity, and a PACAP selective receptor (PAC1) [25].

VIP Binding (bind) of in pituitary

3) Confidence 0.32 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1257432 Disease Relevance 0.40 Pain Relevance 0.19

VIP has also been implicated in the neuro-osteogenic interactions in the skeleton.

VIP Binding (interactions) of in skeleton

4) Confidence 0.32 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1257432 Disease Relevance 0.63 Pain Relevance 0.28

Treatment in PACAP/VIP postulated autoimmune neuropsychiatric fatigue-related disorders

VIP Binding (Treatment) of associated with fatigue

5) Confidence 0.28 Published 2009 Journal Neuropsychiatric Disease and Treatment Section Body Doc Link PMC2695238 Disease Relevance 0.62 Pain Relevance 0.10

They have key roles in blood vessels in the CNS84 and VIP is associated with maintaining functional integrity of the BBB.83 PACAP and VIP influence regulatory T cell (Treg)29 and other immune functions.

VIP Binding (associated) of in regulatory T cell

6) Confidence 0.28 Published 2009 Journal Neuropsychiatric Disease and Treatment Section Body Doc Link PMC2695238 Disease Relevance 0.66 Pain Relevance 0.23

The biological effects of VIP are mediated by G protein-coupled receptors (VPAC1 and VPAC2) that bind VIP and pituitary adenylate cyclase-activating polypeptide (PACAP) with equal affinity, and a PACAP selective receptor (PAC1) [25].

VIP Binding (bind) of in pituitary

7) Confidence 0.28 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1257432 Disease Relevance 0.47 Pain Relevance 0.22

They have key roles in blood vessels in the CNS84 and VIP is associated with maintaining functional integrity of the BBB.83 PACAP and VIP influence regulatory T cell (Treg)29 and other immune functions.

VIP Binding (integrity) of in regulatory T cell

8) Confidence 0.25 Published 2009 Journal Neuropsychiatric Disease and Treatment Section Body Doc Link PMC2695238 Disease Relevance 0.67 Pain Relevance 0.24

Thus, the identification of peptides that bind to multiple HLA types, the so-called “promiscuous” or “universal” epitope(s), could lead to effective coverage of the human population using peptide-based vaccine.

peptides Binding (bind) of

9) Confidence 0.01 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2828482 Disease Relevance 0.05 Pain Relevance 0

This analysis revealed that nearly all PspA peptides could potentially bind a variety of mouse and human MHC class II molecules.

peptides Binding (bind) of

10) Confidence 0.01 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2828482 Disease Relevance 0.32 Pain Relevance 0

To identify the immunodominant epitopes of PspA, we used in silico MHC affinity measurement methods using both affinity data from the Immune Epitope Database and Analysis Resource (IEDB) [14], eluted peptide data from the SYFPEITHI [12] database as well as RANKPEP [15], SVMHC [16], and MHCPred tools [17], [18], which predicted the PspA peptides that bind HLA-DR, -DQ, and -DP alleles.

peptides Binding (bind) of

11) Confidence 0.01 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2828482 Disease Relevance 0.47 Pain Relevance 0.04

General Comments

This test has worked.