| + |
Erythrocytic spectrin | down-regulates 
|
Membrane_disruption |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266028 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24302288 |
Spectrin is multifunctional, and spectrin-based networks are important for maintaining the shape and mechanical properties of erythrocytes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Membrane attack complex | up-regulates 
|
Membrane_disruption |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263456 |
|
|
in vitro |
|
| pmid |
sentence |
| 30552328 |
CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Complement Signaling |
| + |
Non-erythrocytic spectrin | down-regulates
|
Membrane_disruption |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266029 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24302288 |
Spectrin is a large, cytoskeletal, and heterodimeric protein composed of modular structure of alpha and beta subunits, it typically contains 106 contiguous amino acid sequence motifs called “spectrin repeats”. Spectrin is crucial for maintaining the stability and structure of the cell membrane and the shape of a cell |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
Membrane_disruption