+ |
Host translation inhibitor nsp1 | up-regulates
|
Apoptosis |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262506 |
|
|
Homo sapiens |
NCI-H1299 Cell |
pmid |
sentence |
33188728 |
We present here data demonstrating that among all viral proteins, Nsp1 causes the most severe viability reduction in the cells of human lung origin. We found that introduction of Nsp1, but not other viral proteins, induced apoptosis in H1299 cells |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | SARS-COV APOPTOSIS, SARS-CoV MAPK PERTURBATION, SARS-CoV STRESS GRANULES, SARS-CoV ER STRESS |
+ |
Host translation inhibitor nsp1 | down-regulates activity
binding
|
RPS3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262507 |
|
|
in vitro |
|
pmid |
sentence |
33188728 |
Nsp1 Locks the 40S in a Conformation Incompatible with mRNA Loading and Disrupts Initiation Factor Binding. Molecular interactions between C-Nsp1 and 40S ribosome components, including uS3, h18, and uS5. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
Host translation inhibitor nsp1 | down-regulates activity
binding
|
40S cytosolic small ribosomal subunit |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262518 |
|
|
Homo sapiens |
NCI-H1299 Cell |
pmid |
sentence |
33188728 |
Our structure of the SARS-CoV-2 Nsp1 protein bound to the 40S ribosomal subunit establishes a mechanistic basis of the cellular effects of Nsp1, revealing a multifaceted mechanism of inhibition of the host protein synthesis at the initiation stage by the virusThis shows that Nsp1 not only plugs the mRNA entry channel but also keeps the 40S subunit in a conformation that is incompatible with mRNA loading. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | SARS-CoV STRESS GRANULES, SARS-CoV ER STRESS |
+ |
Host translation inhibitor nsp1 | down-regulates activity
binding
|
RPS2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262508 |
|
|
in vitro |
|
pmid |
sentence |
33188728 |
Nsp1 Locks the 40S in a Conformation Incompatible with mRNA Loading and Disrupts Initiation Factor Binding. Molecular interactions between C-Nsp1 and 40S ribosome components, including uS3, h18, and uS5. |
|
Publications: |
1 |
Organism: |
In Vitro |