| + |
APH1A | up-regulates 
binding
|
PSEN1 |
0.946 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97068 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12522139 |
Biochemical and genetic studies have recently identified nicastrin, aph-1, and pen-2 as essential cofactors that physically interact with ps1 and are necessary for the gamma-secretase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93262 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12297508 |
By using co-immunoprecipitation and nickel affinity pull-down approaches, we now show that mammalian aph-1 (maph-1), a conserved multipass membrane protein, physically associates with nicastrin and the heterodimers of the presenilin amino- and carboxyl-terminal fragments in human cell lines and in rat brain. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
NCSTN | up-regulates
binding
|
APH1A |
0.967 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96250 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12471034 |
We show that mammalian aph-1 (maph-1), a conserved multipass membrane protein, physically associates with nicastrin and the heterodimers of the presenilin amino- and carboxyl-terminal fragments in human cell lines and in rat brain. Similar to the loss of presenilin or nicastrin, the inactivation of endogenous maph-1 using small interfering rnas results in the decrease of presenilin levels, accumulation of gamma-secretase substrates (app carboxyl-terminal fragments), and reduction of gamma-secretase products (amyloid-beta peptides and the intracellular domains of app and notch). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-103611 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12857757 |
We show that mammalian aph-1 (maph-1), a conserved multipass membrane protein, physically associates with nicastrin and the heterodimers of the presenilin amino- and carboxyl-terminal fragments in human cell lines and in rat brain. Similar to the loss of presenilin or nicastrin, the inactivation of endogenous maph-1 using small interfering rnas results in the decrease of presenilin levels, accumulation of gamma-secretase substrates (app carboxyl-terminal fragments), and reduction of gamma-secretase products (amyloid-beta peptides and the intracellular domains of app and notch). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93313 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12297508 |
We show that mammalian aph-1 (maph-1), a conserved multipass membrane protein, physically associates with nicastrin and the heterodimers of the presenilin amino- and carboxyl-terminal fragments in human cell lines and in rat brain. Similar to the loss of presenilin or nicastrin, the inactivation of endogenous maph-1 using small interfering rnas results in the decrease of presenilin levels, accumulation of gamma-secretase substrates (app carboxyl-terminal fragments), and reduction of gamma-secretase products (amyloid-beta peptides and the intracellular domains of app and notch). |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
APH1A | up-regulates
binding
|
PSENEN |
0.962 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97104 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12522139 |
Furthermore, overexpression of aph-1 facilitates pen-2-mediated ps1 proteolysis, resulting in a significant increase in ps1 fragments. Our data reveal a direct role of pen-2 in proteolytic cleavage of ps1 and a regulatory function of aph-1, in coordination with pen-2, in the biogenesis of the ps1 complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APH1A | up-regulates
binding
|
NCSTN |
0.967 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93259 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12297508 |
By using co-immunoprecipitation and nickel affinity pull-down approaches, we now show that mammalian aph-1 (maph-1), a conserved multipass membrane protein, physically associates with nicastrin and the heterodimers of the presenilin amino- and carboxyl-terminal fragments in human cell lines and in rat brain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
APH1A | up-regulates
binding
|
PSEN2 |
0.921 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93265 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12297508 |
Gamma secretase subunit. Leads to ps1/ps2 eterodimer complex stabilisation. By using co-immunoprecipitation and nickel affinity pull-down approaches, we now show that mammalian aph-1 (maph-1), a conserved multipass membrane protein, physically associates with nicastrin and the heterodimers of the presenilin amino- and carboxyl-terminal fragments in human cell lines and in rat brain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
APH1A | form complex 
binding
|
gamma-secretase |
0.958 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-209714 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25610395 |
-Secretase is a four subunit, 19-pass transmembrane enzymeBiochemical studies indicated that -secretase activity is catalyzed by the presenilin (PS)-containing macromolecular complex (Li et al., 2000a). The search for other components of the complex revealed three additional proteins: nicastrin (Nct), anterior pharynx-defective-1 (Aph-1), and presenilin enhancer-2 (Pen-2) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
APH1A
- 
- 