| + |
CRYBB2 | up-regulates activity 
binding
|
CRYBB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252154 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16319073 |
βB2-crystallin is the major component of β-crystallin and is a dimer at low concentrations. At high concentrations or in the lens, βB2-crystallin forms hetero-oligomers with other β-crystallins. These oligomeric β-crystallins further participate in the formation of a supramolecular assembly that is important in lens function-lens transparency. |
|
| 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 |
| + |
CRYBB2 | up-regulates activity
binding
|
CRYBB1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252153 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16319073 |
At high concentrations or in the lens, βB2-crystallin forms hetero-oligomers with other β-crystallins. These oligomeric β-crystallins further participate in the formation of a supramolecular assembly that is important in lens function-lens transparency. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CRYBB2 | up-regulates 
|
Maintenance_of_lens_transparency |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252151 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16319073 |
At high concentrations or in the lens, βB2-crystallin forms hetero-oligomers with other β-crystallins. These oligomeric β-crystallins further participate in the formation of a supramolecular assembly that is important in lens function-lens transparency. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CRYBB2 | up-regulates activity
binding
|
CRYBB3 |
0.464 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252152 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16319073 |
At high concentrations or in the lens, βB2-crystallin forms hetero-oligomers with other β-crystallins. These oligomeric β-crystallins further participate in the formation of a supramolecular assembly that is important in lens function-lens transparency. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CRYBB2
- 
- 