+ |
RNA Polymerase III | up-regulates quantity
chemical modification
|
tRNA(Thr) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269497 |
|
|
Homo sapiens |
|
pmid |
sentence |
27911719 |
RNAPIII is specialized for transcription of short, abundant nonprotein-coding RNA transcripts. In addition to all tRNAs, RNAPIII transcribes the 5S rRNA and other essential RNAs, including the U6 small nuclear RNA (snRNA), the snR52 small nucleolar RNA and the RNA components of the signal recognition particle (SRP1) and RNase P (RPR1) |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TARS1 | down-regulates quantity
chemical modification
|
tRNA(Thr) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270501 |
|
|
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 |
+ |
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 |