| + |
Autophagy | up-regulates 
|
Protein_aggregates |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262269 |
|
|
|
|
| pmid |
sentence |
| 32218723 |
In many neurodegenerative conditions protein aggregation may occurs without specific GOF mutations in genes encoding aggregate-prone proteins. In these conditions protein aggregation is associated to the decline of cellular degradative functions, specifically of the autophagy-lysosomal pathway (ALP) (Figure 1). |
|
| Publications: |
1 |
| + |
SOD1 | up-regulates quantity
|
Protein_aggregates |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262279 |
|
|
Homo sapiens |
Motoneuron |
| pmid |
sentence |
| 22051914 |
SOD1 inclusions are found in motor neurons of patients with FALS, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TARDBP | up-regulates quantity
|
Protein_aggregates |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262278 |
|
|
Homo sapiens |
Motoneuron |
| pmid |
sentence |
| 22051914 |
Pathological protein aggregates, identified as compact or skein-like ubiquitinated inclusions, are a cardinal feature of ALS.4–6 The identification of TDP-43 as the major protein constituent of these inclusions initi- ated a major shift in our understanding of the patho- biology of ALS |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FUS | up-regulates quantity
|
Protein_aggregates |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262277 |
|
|
Homo sapiens |
Motoneuron |
| pmid |
sentence |
| 22051914 |
Similarly, cytoplasmic inclu- sions containing mutant fused in sarcoma (FUS) protein have been observed in some patients with FUS-related FALS. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Unfolded_Proteins | up-regulates
|
Protein_aggregates |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262268 |
|
|
|
|
| pmid |
sentence |
| 9502314 |
Inclusion body formation and other aggregates formed during protein folding have been assumed to arise from hydrophobic aggregation of the unfolded or denatured states |
|
| Publications: |
1 |
| + |
SOD1 | up-regulates 
|
Protein_aggregates |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262796 |
|
|
Mus musculus |
NSC-34 Cell |
| pmid |
sentence |
| 29371591 |
Incubating SOD1G93A or SOD1G85R, another well-established misfolded SOD1 mutant, in the absence of recombinant MIF resulted in an exponential increase in thioflavin T (ThT) fluorescence (which correlates with amyloid aggregate formation) |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
OPTN | up-regulates
|
Protein_aggregates |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262275 |
|
|
|
|
| pmid |
sentence |
| 27181519 |
Optineurin and TBK1 have also been discovered co-localizing in protein aggregates, and the phosphorylation of optineurin at serine 177 has been shown to be critical to its function in mediating clearance of aggregated proteins via autophagy |
|
| Publications: |
1 |
3.0
Protein_aggregates