| + |
CRYAA | up-regulates activity
binding
|
CRYBB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252155 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22982024 |
Aberrant protein interactions can lead to aggregation and insolubilization, such as occurs during cataract formation. Deamidation, a prevalent age-related modification in the lens of the eye, decreases stability of the major lens proteins, crystallins. Deamidation did not disrupt specific αA/βB2 interactions but favored aggregation before complex formation with αA. We conclude that deamidation contributes to cataract formation through destabilization of crystallins before they can be rescued by α-crystallin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CRYAA | up-regulates
|
Maintenance_of_lens_transparency |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252156 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22982024 |
Aberrant protein interactions can lead to aggregation and insolubilization, such as occurs during cataract formation. Deamidation, a prevalent age-related modification in the lens of the eye, decreases stability of the major lens proteins, crystallins. Deamidation did not disrupt specific αA/βB2 interactions but favored aggregation before complex formation with αA. We conclude that deamidation contributes to cataract formation through destabilization of crystallins before they can be rescued by α-crystallin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |