| + |
PI4KB | up-regulates 
|
Receptor_mediated_ endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260734 |
|
|
Chlorocebus aethiops |
Vero Cell |
| pmid |
sentence |
| 22253445 |
PI4KB knockdown inhibits SARS-CoV S-mediated entry, whereas PI3KR1 knockdown increases SARS-CoV S-mediated entry |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY |
| + |
SACM1L | down-regulates 
|
Receptor_mediated_ endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260735 |
|
|
Chlorocebus aethiops |
Vero Cell |
| pmid |
sentence |
| 22253445 |
Ectopic Expression of Sac1 Phosphatase Inhibits SARS-CoV S-mediated Entry |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY |
| + |
phosphatidylinositol 4-phosphate | up-regulates
|
Receptor_mediated_ endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260745 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 22253445 |
Further research suggested that PI4P plays an essential role in SARS-CoV spike-mediated entry, which is regulated by the PI4P lipid microenvironment. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY |
| + |
MYO1E | up-regulates
|
Receptor_mediated_ endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265425 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 17257598 |
We describe binding of two PRD-containing endocytic proteins, dynamin and synaptojanin-1, to the SH3 domain of Myo1E. This interaction was detected both in vitro, using pull-downs of purified proteins, and in vivo, using immunoprecipitation of protein complexes from synapse-enriched brain extract and immunolocalization of Myo1E and dynamin. Our observation of the interaction between human Myo1E and endocytic proteins suggests that this longtailed myosin may play a role in clathrin-dependent endocytosis.Interaction between Myo1E SH3 domain and PRD-containing endocytic proteins may promote recruitment of Myo1E to clathrin-coated structures since an inactivating mutation in the SH3 domain reduced Myo1E localization to clathrin-containing puncta. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| Tissue: |
Brain |
| + |
ACE2 | up-regulates
|
Receptor_mediated_ endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260235 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18554741 |
Endocytosis of the Receptor-Binding Domain of SARS-CoV Spike Protein Together With Virus Receptor ACE2. Here, we demonstrate that the RBD spike protein alone can be internalized together with ACE2. We propose that after binding to ACE2, the RBD spike protein activates the ACE2 mediated cellular endocytosis signal pathway, by which SARS-CoV enters the susceptible cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY |
| + |
Spike protein-ACE2 | up-regulates
|
Receptor_mediated_ endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260289 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18554741 |
Endocytosis of the Receptor-Binding Domain of SARS-CoV Spike Protein Together With Virus Receptor ACE2. Here, we demonstrate that the RBD spike protein alone can be internalized together with ACE2. We propose that after binding to ACE2, the RBD spike protein activates the ACE2 mediated cellular endocytosis signal pathway, by which SARS-CoV enters the susceptible cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | SARS-CoV ATTACHMENT AND ENTRY |
| + |
CoV2 Spike protein-ACE2 | up-regulates
|
Receptor_mediated_ endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260743 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32221306 |
We demonstrated that SARS-CoV-2 S protein entry on 293/hACE2 cells is mainly mediated through endocytosis, and that PIKfyve, TPC2, and cathepsin L are critical for virus entry. We further found that SARS-CoV-2 S protein could trigger syncytia in 293/hACE2 cells independent of exogenous protease. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY |
| + |
CoV2 spike protein-NRP1 | up-regulates 
|
Receptor_mediated_ endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262316 |
|
|
Mus musculus |
Olfactory Epithelium |
| pmid |
sentence |
| 33082293 |
NRP mediates entry of nanoparticles coated with SARS-CoV-2 (SARS-2) S–derived CendR peptides into cultured cells, olfactory epithelium, and the central nervous system of mice. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | SARS-CoV ATTACHMENT AND ENTRY |
| + |
AP-2/clathrin vescicle | up-regulates
|
Receptor_mediated_ endocytosis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260704 |
|
|
|
|
| pmid |
sentence |
| 17522231 |
These results suggest that when SARS-CoV binds ACE2 it is internalized and penetrates early endosomes in a clathrin-dependent manner |The clathrin-dependent endocytosis is initiated by the binding of adaptor protein 2 (AP2) complexes to the cytoplasmic tail of the cell-surface receptors, which recruits clathrins |
|
| Publications: |
1 |
| Pathways: | COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY |
3.0
Receptor_mediated_ endocytosis