| + |
Immune complexes | up-regulates activity 
|
FCGR2B |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249522 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 25475856 |
Low affinity-activating Fcgamma receptors (FcgammaRs) that bind immune complexes are controlled by a single inhibitory receptor, FcgammaRIIb (CD32b). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Immune complexes | up-regulates activity
|
FCGR1A |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249521 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 18064051 |
Immune complexes bind to activating Fc receptors (FcR) and inhibitory FcRs that are expressed by innate immune effector cells such as basophils, mast cells, neutrophils, monocytes and macrophages, in which they trigger the indicated effector responses. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Immune complexes | up-regulates activity
|
FCGR3A |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249523 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 17558411 |
After binding their antibody ligands, FcgRI and FcgRIII deliver activating signals through an association with the FcRg-chain (FcRg), a transmembrane adaptor protein with an immuno-receptor tyrosine-based activation motif in its cytoplasmic domain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Immune complexes | up-regulates activity
relocalization
|
FCAR |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264859 |
|
|
|
|
| pmid |
sentence |
| 12768205 |
Both monomeric and dimeric IgA can bind to FcalphaRI, and monomeric or dimeric IgA immune complexes can activate phagocytosis and other immune responses through the clustering of FcalphaRI |
|
| Publications: |
1 |
| + |
Immune complexes | up-regulates activity 
binding
|
Complement C1q |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263397 |
|
|
in vitro |
|
| pmid |
sentence |
| 29449492 |
We used IgG monoclonal antibodies (mAbs) oligomerized through antigen-binding on liposomes or preformed antibody complexes in solution and applied tomography and single-particle cryo–electron microscopy (cryo-EM) to resolve the mechanisms of C1 binding and activation.|Binding of C1 through its gC1q modules to mediators of inflammation, such as immunoglobulin G (IgG) or IgM antibodies (fig. S1, C and D), on cell surfaces activates the associated proteases and initiates the proteolytic cascade of complement |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Complement Signaling |
3.0
Immune complexes