| + |
C1QA | form complex 
binding
|
Complement C1q |
0.628 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263390 |
|
|
in vitro |
|
| pmid |
sentence |
| 29449492 |
C1q comprises 18 polypeptide chains; three chains of C1q-A, -B, and -C trimerize to form six collagen-like triple helices connected to six globular (trimeric) ligand-recognition (gC1q) modules (fig. S1B) (1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
C1QC | form complex
binding
|
Complement C1q |
0.557 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263389 |
|
|
in vitro |
|
| pmid |
sentence |
| 29449492 |
C1q comprises 18 polypeptide chains; three chains of C1q-A, -B, and -C trimerize to form six collagen-like triple helices connected to six globular (trimeric) ligand-recognition (gC1q) modules (fig. S1B) (1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
C1QB | form complex
binding
|
Complement C1q |
0.629 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263388 |
|
|
in vitro |
|
| pmid |
sentence |
| 29449492 |
C1q comprises 18 polypeptide chains; three chains of C1q-A, -B, and -C trimerize to form six collagen-like triple helices connected to six globular (trimeric) ligand-recognition (gC1q) modules (fig. S1B) (1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
C1QBP | down-regulates activity 
binding
|
Complement C1q |
0.382 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263401 |
|
|
|
|
| pmid |
sentence |
| 28018340 |
Previous studies have shown that gC1qR inhibits aggregated IgG-mediated complement activation by binding to the gC1q site on C1q, thereby preventing IgG from binding to the gh’s (28), suggesting that the binding sites for gC1qR and IgG on C1q may be identical or at least overlapping. |
|
| 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 |
| + |
Complement C1q | form complex
binding
|
Complement C1 complex |
0.616 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263396 |
|
|
in vitro |
|
| pmid |
sentence |
| 29449492 |
The complement system is part of our innate immune system. The classical complement pathway is triggered by activation of the C1 initiation complex upon binding to cell surfaces. C1, or C1qr2s2, consists of four proteases, C1r and C1s, that associate with C1q, which contains antibody-binding sites.|The reconstruction reveals densities for all C1q collagen-like triple helices and gC1q modules, C1r and C1s proteases |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Complement Signaling |
3.0
Complement C1q
CPX-1919