| + |
CFH | down-regulates activity 
binding
|
C3 |
0.916 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252141 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19050261 |
As a regulator of the alternative pathway, FH binds to C3b and inhibits the binding of factor B to C3b, acts as a cofactor for the factor I-mediated cleavage of C3b to iC3b (cofactor activity), and accelerates the decay of C3bBb, the alternative pathway C3 convertase (decay-accelerating activity) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CFHR1 | down-regulates activity
binding
|
CFH |
0.515 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263476 |
|
|
in vitro |
|
| pmid |
sentence |
| 27814381 |
Finally, we have been able to establish that CFHR1 can sterically inhibit the interaction that CFH/CFHL-1 SCR1-4 makes with C3b.|CFH regulates the alternative pathway of complement in both the fluid phase and on self-surfaces: It competes with complement factor B (CFB) for binding to C3b and C3(H2O) thereby blocking the formation of the pro-convertase complexes, C3bB and C3(H2O)B. It also accelerates the decay of any existing C3bBb or C3(H2O)Bb. |these data have allowed us to consolidate one possible model of CFHR1-mediated deregulation of CFH/CFHL-1 on an activating surface in which CFHR1 directly competes with or blocks both CFH-binding sites on C3b |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CFH | down-regulates activity
binding
|
CFB |
0.497 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252142 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19050261 |
As a regulator of the alternative pathway, FH binds to C3b and inhibits the binding of factor B to C3b, acts as a cofactor for the factor I-mediated cleavage of C3b to iC3b (cofactor activity), and accelerates the decay of C3bBb, the alternative pathway C3 convertase (decay-accelerating activity) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTX3 | up-regulates activity 
binding
|
CFH |
0.408 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252140 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19050261 |
Our findings identify PTX3 as a unique FH ligand in that it can bind both of the two hot-spots of FH, namely SCR7 and SCR19-20 and indicate that PTX3 participates in the localization of functionally active FH. PTX3 binds FH without interfering with its complement inhibitory function. Therefore PTX3 may contribute to focusing FH regulatory action, prevent excessive complement activation, and thus exert an important function in the control of inflammation in response to tissue injury. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CFH | down-regulates activity
binding
|
CRP |
0.568 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252145 |
|
|
Homo sapiens |
Retinal Pigment Epithelium Cell |
| pmid |
sentence |
| 26961257 |
In this study, we provide mechanistic insight into how CRP contributes to the development of AMD. In particular, we show that monomeric CRP (mCRP) but not the pentameric form (pCRP) upregulates IL-8 and CCL2 levels in retinal pigment epithelial cells. Further, we show that complement factor H (FH) binds mCRP to dampen its proinflammatory activity. FH from AMD patients carrying the “risk” His402 polymorphism displays impaired binding to mCRP, and therefore proinflammatory effects of mCRP remain unrestrained. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CFH | up-regulates activity
binding
|
CFI |
0.918 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263490 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26806831 |
FH also serves as cofactor for the serine protease factor I (FI) that cleaves C3b into iC3b, unable to form C3 convertase (Fig 1B). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CFH
- 
- 