| + |
S100A8 | up-regulates activity 
binding
|
AGER |
0.323 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261919 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28137827 |
RAGE and TLR4 are well-characterized S100A8 and S100A9 receptors and expressed in AML cells Once secreted, S100A8 and S100A9 induce immune and inflammatory responses9 through interaction with receptors such as Toll-like receptor 4 (TLR4), receptor for advanced glycation end-product (RAGE), and CD33 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
S100A8 | form complex 
binding
|
Calprotectin complex |
0.716 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262832 |
|
|
|
|
| pmid |
sentence |
| 9867828 |
Using the two-hybrid system we analyzed the dimerization of MRP8 (S100A8) and MRP14 (S100A9), two S100 proteins expressed in myeloid cells. It is reported that the MRP8-MRP14 heteromer is the clearly preferred complex in both man and mouse. |
|
| Publications: |
1 |
| + |
S100A8 | down-regulates activity 
binding
|
TLR4 |
0.515 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261921 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28137827 |
Interestingly, in the present study, we report that extracellular S100A9 induces terminal differentiation of myeloid leukemia cells in human and murine AMLs after TLR4 activation, which is highly expressed by primary myelomonocytic and monocytic leukemia cells. In contrast, anti-S100A8 induced the differentiation of AML cells, suggesting that the differentiation-promoting effect of S100A9 is inhibited by S100A8. ) S100A8 could bind to TLR4 and activate different signaling pathways, leading to the inhibition of cellular differentiation induced by S100A9. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
calcium(2+) | up-regulates activity
chemical activation
|
S100A8 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261935 |
|
|
Homo sapiens |
Phagocyte |
| pmid |
sentence |
| 16690079 |
S100 proteins comprise the largest family of calcium-binding proteins. Members of this family usually form homo- or heterodimers, which may associate to higher-order oligomers in a calcium-dependent manner. The heterodimers of S100A8 and S100A9 represent the major calcium-binding proteins in phagocytes. Both proteins regulate migration of these cells via modulation of tubulin polymerization. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
S100A8 | up-regulates quantity by stabilization
binding
|
Tubulin |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261937 |
|
|
Homo sapiens |
Monocyte |
| pmid |
sentence |
| 16690079 |
Calcium-induced complexes of S100A8 and S100A9 have been shown to colocalize with microtubules (MTs) during activation of monocytes. Functional analyses demonstrated that the complexes are involved in cytoskeletal organization and that they directly bind to tubulin and promote tubulin polymerization in a calcium-dependent manner |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
S100A8
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