| + |
CRYAB | up-regulates activity 
binding
|
CRYGD |
0.541 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253621 |
|
|
in vitro |
|
| pmid |
sentence |
| 20621668 |
Human gamma-crystallins are long-lived, unusually stable proteins of the eye lens exhibiting duplicated, double Greek key domains. The lens also contains high concentrations of the small heat shock chaperone alpha-crystallin, which suppresses aggregation of model substrates in vitro. Mature-onset cataract is believed to represent an aggregated state of partially unfolded and covalently damaged crystallins. The alphaB-crystallin oligomers formed long-lived stable complexes with their gammaD-crystallin substrates. These in vitro results provide support for protein unfolding/protein aggregation models for cataract, with alpha-crystallin suppressing aggregation of damaged or unfolded proteins through early adulthood but becoming saturated with advancing age. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
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 |
3.0
CRYGD
- 
- 