INT181018

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Context Info
Confidence 0.45
First Reported 2005
Last Reported 2011
Negated 0
Speculated 2
Reported most in Body
Documents 20
Total Number 25
Disease Relevance 22.14
Pain Relevance 3.18

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 (S100a8) extracellular region (S100a8) plasma membrane (S100a8)
cytoskeleton (S100a8) cytoplasm (S100a8)
Anatomy Link Frequency
neutrophil 4
filaments 3
granulocytes 1
monocytes 1
endothelial cells 1
S100a8 (Mus musculus)
Pain Link Frequency Relevance Heat
Inflammation 1070 100.00 Very High Very High Very High
cytokine 215 100.00 Very High Very High Very High
Inflammatory response 255 87.32 High High
Arthritis 27 74.16 Quite High
chemokine 162 71.92 Quite High
imagery 9 71.24 Quite High
Neuritis 1 70.08 Quite High
rheumatoid arthritis 67 65.12 Quite High
Central nervous system 16 54.12 Quite High
antagonist 1 45.52 Quite Low
Disease Link Frequency Relevance Heat
INFLAMMATION 1343 100.00 Very High Very High Very High
Death 34 100.00 Very High Very High Very High
Multiple Sclerosis 52 99.92 Very High Very High Very High
Immunization 25 99.28 Very High Very High Very High
Mycobacterial Infection 583 98.72 Very High Very High Very High
Injury 1316 98.64 Very High Very High Very High
Disease 370 98.32 Very High Very High Very High
Infection 515 97.68 Very High Very High Very High
Chemical Burns 18 97.60 Very High Very High Very High
Targeted Disruption 149 97.28 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Interestingly, another member of the late effector cluster, the intracellular Ca2+-binding protein MRP8 (S100A8) is expressed in a similar temporal and spatial pattern to K6 (Figure 4o and 4p).
S100A8 Binding (binding) of
1) Confidence 0.45 Published 2005 Journal Genome Biol Section Body Doc Link PMC549066 Disease Relevance 0.52 Pain Relevance 0
Interestingly, another member of the late effector cluster, the intracellular Ca2+-binding protein MRP8 (S100A8) is expressed in a similar temporal and spatial pattern to K6 (Figure 4o and 4p).
MRP8 Binding (binding) of
2) Confidence 0.45 Published 2005 Journal Genome Biol Section Body Doc Link PMC549066 Disease Relevance 0.52 Pain Relevance 0
MRP8 binds to keratin filaments as an MRP8/14 heterodimer in a Ca2+dependent manner [20,21] and is postulated to interact with these keratin filaments and guide cytoskeletal rearrangements during tissue repair [22].
MRP8 Binding (interact) of in filaments
3) Confidence 0.45 Published 2005 Journal Genome Biol Section Body Doc Link PMC549066 Disease Relevance 0.50 Pain Relevance 0.03
MRP8 binds to keratin filaments as an MRP8/14 heterodimer in a Ca2+dependent manner [20,21] and is postulated to interact with these keratin filaments and guide cytoskeletal rearrangements during tissue repair [22].
MRP8 Spec (postulated) Binding (binds) of in filaments
4) Confidence 0.45 Published 2005 Journal Genome Biol Section Body Doc Link PMC549066 Disease Relevance 0.44 Pain Relevance 0
As discussed previously, both the genes for MRP8 and its binding partner MRP14 are upregulated by wound-edge keratinocytes.
MRP8 Binding (binding) of in keratinocytes associated with injury
5) Confidence 0.45 Published 2005 Journal Genome Biol Section Body Doc Link PMC549066 Disease Relevance 1.30 Pain Relevance 0.27
In fact, S100A8 and S100A9, either as is or in form of heterodimers [30-33], have been shown to promote death or permeability of vascular endothelial cells by binding to specific molecules on them [34,35].
S100A8 Binding (binding) of in endothelial cells associated with death
6) Confidence 0.37 Published 2010 Journal Molecular Vision Section Body Doc Link PMC2994359 Disease Relevance 0.42 Pain Relevance 0.12
Depletion of neutrophils abrogated S-CorNV and S100A8 and S100A9 production
S100A8 Binding (abrogated) of in neutrophils
7) Confidence 0.37 Published 2010 Journal Molecular Vision Section Body Doc Link PMC2994359 Disease Relevance 0.46 Pain Relevance 0.07
Coli, suggesting that endogenous S100A8/A9 does not play a major role in the pathogenesis of E.
S100A8 Binding (endogenous) of
8) Confidence 0.36 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2954806 Disease Relevance 1.58 Pain Relevance 0.16
As both the MRP8/MRP14 heterodimer and a homodimer, MRP8 is a potent chemoattractant [22,23] and, interestingly, the MRP8/14 heterodimer also has an entirely different role, operating as a wound antimicrobial factor, although the MRP14 subunit seems to be responsible for this activity [24].
MRP8 Binding (heterodimer) of associated with injury
9) Confidence 0.35 Published 2005 Journal Genome Biol Section Body Doc Link PMC549066 Disease Relevance 0.47 Pain Relevance 0.08
The heterophilic binding partner of MRP8 is MRP14, which does not appear in the same cluster but rather is expressed within the early inflammation cluster (see later), since, in addition to keratinocyte expression, it is expressed at high levels by wound leukocytes.
MRP8 Binding (binding) of in leukocytes associated with inflammation and injury
10) Confidence 0.35 Published 2005 Journal Genome Biol Section Body Doc Link PMC549066 Disease Relevance 0.44 Pain Relevance 0.05
As both the MRP8/MRP14 heterodimer and a homodimer, MRP8 is a potent chemoattractant [22,23] and, interestingly, the MRP8/14 heterodimer also has an entirely different role, operating as a wound antimicrobial factor, although the MRP14 subunit seems to be responsible for this activity [24].
MRP8 Binding (homodimer) of associated with injury
11) Confidence 0.35 Published 2005 Journal Genome Biol Section Body Doc Link PMC549066 Disease Relevance 0.46 Pain Relevance 0.08
Interestingly, S100A8/A9 protein complex interacts with TLR4 [12] and the extent of S100A8/A9 expression correlates with disease activity in several inflammatory disorders [9], [10], [15], [16].
S100A8 Binding (interacts) of associated with inflammation and disease
12) Confidence 0.35 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2954806 Disease Relevance 1.28 Pain Relevance 0.20
However, we do not know whether these genes work via pro-inflammatory or pro-angiogenic pathways under these conditions.
pro-inflammatory Spec (whether) Binding (work) of associated with inflammation
13) Confidence 0.32 Published 2010 Journal Molecular Vision Section Body Doc Link PMC2994359 Disease Relevance 0.67 Pain Relevance 0.18
S100A8 and S100A9 interact with both type III intermediate filaments and keratin filaments for the purpose of wound repair.
S100A8 Binding (interact) of in filaments associated with injury
14) Confidence 0.25 Published 2009 Journal J Transl Med Section Body Doc Link PMC2666642 Disease Relevance 0.58 Pain Relevance 0.08
In the presence of calcium, S100A8 and S100A9 form tetramers and bind directly to microtubules.
S100A8 Binding (bind) of
15) Confidence 0.25 Published 2009 Journal J Transl Med Section Body Doc Link PMC2666642 Disease Relevance 0.48 Pain Relevance 0.09
S100A8/9 binds to heparan sulfate, proteoglycans, and carboxylated N-glycans [103].
S100A8 Binding (binds) of
16) Confidence 0.25 Published 2009 Journal J Transl Med Section Body Doc Link PMC2666642 Disease Relevance 0.48 Pain Relevance 0.11
Importantly, S100A8, S100A9, and S100A8/A9 have each been shown to induce neutrophil chemotaxis [60], [61].
S100A8 Binding (induce) of in neutrophil
17) Confidence 0.14 Published 2011 Journal PLoS ONE Section Body Doc Link PMC3020951 Disease Relevance 1.54 Pain Relevance 0.16
Importantly, S100A8, S100A9, and S100A8/A9 have each been shown to induce neutrophil chemotaxis [60], [61].
S100A8 Binding (induce) of in neutrophil
18) Confidence 0.14 Published 2011 Journal PLoS ONE Section Body Doc Link PMC3020951 Disease Relevance 1.55 Pain Relevance 0.16
S100A8 and S100A9 are small calcium-binding proteins that are expressed in tuberculosis patients [59] and produced by activated neutrophils and monocytes.
S100A8 Binding (binding) of in monocytes associated with mycobacterial infection
19) Confidence 0.14 Published 2011 Journal PLoS ONE Section Body Doc Link PMC3020951 Disease Relevance 1.68 Pain Relevance 0.07
The predominant role of the innate immune system in systemic onset disease is also underscored by the high expression and serum concentrations of the calcium-binding proteins S100A8, S100A9, and S100A12, which are specifically secreted during activation of neutrophilic granulocytes and monocytes47).
S100A8 Binding (binding) of in granulocytes associated with disease
20) Confidence 0.11 Published 2010 Journal Korean Journal of Pediatrics Section Body Doc Link PMC3012271 Disease Relevance 1.02 Pain Relevance 0.24

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