INT181084

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Context Info
Confidence 0.42
First Reported 2005
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 6
Total Number 6
Disease Relevance 2.91
Pain Relevance 0.62

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, S100a9) extracellular region (S100a8, S100a9) plasma membrane (S100a8, S100a9)
cytoskeleton (S100a8, S100a9) cytoplasm (S100a8, S100a9) nucleus (S100a9)
Anatomy Link Frequency
filaments 1
keratinocytes 1
S100a8 (Mus musculus)
S100a9 (Mus musculus)
Pain Link Frequency Relevance Heat
Inflammation 340 97.20 Very High Very High Very High
cytokine 42 81.64 Quite High
imagery 3 39.08 Quite Low
Inflammatory response 58 16.84 Low Low
fibrosis 32 16.32 Low Low
metalloproteinase 6 15.04 Low Low
Osteoarthritis 6 13.04 Low Low
Abeta 36 5.00 Very Low Very Low Very Low
chemokine 27 5.00 Very Low Very Low Very Low
Arthritis 6 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Injury 341 99.20 Very High Very High Very High
INFLAMMATION 401 97.20 Very High Very High Very High
Targeted Disruption 19 86.24 High High
Frailty 2 83.56 Quite High
Colon Cancer 3 73.64 Quite High
Eczema 2 70.28 Quite High
Leukemia 2 65.08 Quite High
Cancer 101 62.48 Quite High
Apoptosis 42 58.16 Quite High
Wound Healing 24 50.00 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
For example, it has been noted that S100A8, S100A9 and their heterodimer or tetramer manifested differential efficacy in terms of certain bioprocesses [28-30].
S100A8 Binding (heterodimer) of S100A9
1) Confidence 0.42 Published 2010 Journal Molecular Vision Section Body Doc Link PMC2994359 Disease Relevance 0.33 Pain Relevance 0.12
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 MRP14 associated with injury
2) Confidence 0.33 Published 2005 Journal Genome Biol Section Body Doc Link PMC549066 Disease Relevance 0.47 Pain Relevance 0.08
As discussed previously, both the genes for MRP8 and its binding partner MRP14 are upregulated by wound-edge keratinocytes.
MRP8 Binding (binding) of MRP14 in keratinocytes associated with injury
3) Confidence 0.31 Published 2005 Journal Genome Biol Section Body Doc Link PMC549066 Disease Relevance 1.30 Pain Relevance 0.27
Some form heterodimers with other S100 proteins – for example the S100A8/S100A9 heterodimer is actually the preferred form found within the cell.
S100A8 Binding (heterodimer) of S100A9
4) Confidence 0.11 Published 2009 Journal J Transl Med Section Body Doc Link PMC2666642 Disease Relevance 0.11 Pain Relevance 0.03
S100A8 and S100A9 interact with both type III intermediate filaments and keratin filaments for the purpose of wound repair.
S100A8 Binding (interact) of S100A9 in filaments associated with injury
5) Confidence 0.11 Published 2009 Journal J Transl Med Section Body Doc Link PMC2666642 Disease Relevance 0.58 Pain Relevance 0.08
Some form heterodimers with other S100 proteins – for example the S100A8/S100A9 heterodimer is actually the preferred form found within the cell.
S100A8 Binding (heterodimer) of S100A9
6) Confidence 0.11 Published 2009 Journal J Transl Med Section Body Doc Link PMC2666642 Disease Relevance 0.11 Pain Relevance 0.03

General Comments

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