| + |
CRYAB | up-regulates activity 
binding
|
CRYGS |
0.555 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253623 |
|
|
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 |
| + |
TFAP2B | up-regulates quantity by expression
transcriptional regulation
|
CRYAB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253637 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21556774 |
Aberrant expression of CRYAB has been shown to be associated with several neurological diseases and malignant neoplasms. To identify transcriptional regulators of CRYAB expression, we examined its promoter for binding sites of transcription factors and identified four potential AP-2 binding sites in addition to a p53 binding site reported previously|Taken together, our results indicate that AP-2_ up-regulates the transcription of the CRYAB gene through stabilizing p53 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TP53 | up-regulates quantity by expression
transcriptional regulation
|
CRYAB |
0.483 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253638 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21556774 |
Aberrant expression of CRYAB has been shown to be associated with several neurological diseases and malignant neoplasms. To identify transcriptional regulators of CRYAB expression, we examined its promoter for binding sites of transcription factors and identified four potential AP-2 binding sites in addition to a p53 binding site reported previously|Taken together, our results indicate that AP-2_ up-regulates the transcription of the CRYAB gene through stabilizing p53 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TFAP2A | up-regulates quantity by expression
transcriptional regulation
|
CRYAB |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253636 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21556774 |
Aberrant expression of CRYAB has been shown to be associated with several neurological diseases and malignant neoplasms. To identify transcriptional regulators of CRYAB expression, we examined its promoter for binding sites of transcription factors and identified four potential AP-2 binding sites in addition to a p53 binding site reported previously|Taken together, our results indicate that AP-2_ up-regulates the transcription of the CRYAB gene through stabilizing p53 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CRYAB | up-regulates activity
binding
|
CRYGD |
0.536 |
| 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 |
| + |
CRYAB | up-regulates activity
binding
|
CRYGC |
0.547 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253622 |
|
|
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 |
3.0
CRYAB
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