| + |
EEF1A2 | up-regulates 
relocalization
|
Thr-tRNA(Thr) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269536 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23699257 |
During protein synthesis, eEF1A binds to and delivers aminoacylated tRNAs (aa-tRNAs) to the elongating ribosome (Fig. 1). GTP bound to eEF1A is hydrolyzed upon codon-anticodon match between an aa-tRNA in the A site of the ribosome and mRNA bound to the ribosome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
tRNA(Thr) | up-regulates quantity
precursor of
|
Thr-tRNA(Thr) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270507 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25824639 |
Here we show, using X-ray crystal structures and functional analyses, that a single molecule of borrelidin simultaneously occupies four distinct subsites within the catalytic domain of bacterial and human ThrRSs. These include the three substrate-binding sites for amino acid, ATP and tRNA associated with aminoacylation, and a fourth 'orthogonal' subsite created as a consequence of binding. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EEF1A1P5 | up-regulates
relocalization
|
Thr-tRNA(Thr) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269556 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23699257 |
During protein synthesis, eEF1A binds to and delivers aminoacylated tRNAs (aa-tRNAs) to the elongating ribosome (Fig. 1). GTP bound to eEF1A is hydrolyzed upon codon-anticodon match between an aa-tRNA in the A site of the ribosome and mRNA bound to the ribosome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TARS1 | up-regulates quantity
chemical modification
|
Thr-tRNA(Thr) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270506 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25824639 |
Here we show, using X-ray crystal structures and functional analyses, that a single molecule of borrelidin simultaneously occupies four distinct subsites within the catalytic domain of bacterial and human ThrRSs. These include the three substrate-binding sites for amino acid, ATP and tRNA associated with aminoacylation, and a fourth 'orthogonal' subsite created as a consequence of binding. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Translation elongation and termination |
| + |
EEF1A1 | up-regulates
relocalization
|
Thr-tRNA(Thr) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269516 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23699257 |
During protein synthesis, eEF1A binds to and delivers aminoacylated tRNAs (aa-tRNAs) to the elongating ribosome (Fig. 1). GTP bound to eEF1A is hydrolyzed upon codon-anticodon match between an aa-tRNA in the A site of the ribosome and mRNA bound to the ribosome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Translation elongation and termination |
| + |
threonine | up-regulates quantity
precursor of
|
Thr-tRNA(Thr) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270508 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25824639 |
Here we show, using X-ray crystal structures and functional analyses, that a single molecule of borrelidin simultaneously occupies four distinct subsites within the catalytic domain of bacterial and human ThrRSs. These include the three substrate-binding sites for amino acid, ATP and tRNA associated with aminoacylation, and a fourth 'orthogonal' subsite created as a consequence of binding. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
Thr-tRNA(Thr)