| + |
CRYGC | up-regulates 
|
Maintenance_of_lens_transparency |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253624 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10521291 |
The γ-crystallin proteins are tightly folded in two domains with no free loops. It is possible that the R58H mutation destabilizes the contact between lens-fiber cells, which is critical for the maintenance of lens transparency. Improper folding of CRYGD, the most abundantly expressed γ-crystallin in the lens, could well cause protein aggregation and lens opacification. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CRYGD | up-regulates
|
Maintenance_of_lens_transparency |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253620 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10521291 |
The γ-crystallin proteins are tightly folded in two domains with no free loops. It is possible that the R58H mutation destabilizes the contact between lens-fiber cells, which is critical for the maintenance of lens transparency. Improper folding of CRYGD, the most abundantly expressed γ-crystallin in the lens, could well cause protein aggregation and lens opacification. |
|
| 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 |
| + |
CRYGS | up-regulates
|
Maintenance_of_lens_transparency |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253625 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10521291 |
The γ-crystallin proteins are tightly folded in two domains with no free loops. It is possible that the R58H mutation destabilizes the contact between lens-fiber cells, which is critical for the maintenance of lens transparency. Improper folding of CRYGD, the most abundantly expressed γ-crystallin in the lens, could well cause protein aggregation and lens opacification. |
|
| 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 |
3.0
Maintenance_of_lens_transparency