+ |
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 |
+ |
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 |