+ |
arginine | up-regulates activity
|
mTORC1 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-268013 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
27126896 |
Importantly, asparagine/glutamine pre-load only results in mTOR activation following amino acid stimulation (Fig. 5a), indicating that it is their exchange factor roles that elicit mTORC1 activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
arginine | up-regulates quantity
|
AminoAcids |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264756 |
|
|
|
|
pmid |
sentence |
29259120 |
All extant life employs the same 20 amino acids for protein biosynthesis |
|
Publications: |
1 |
+ |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
arginine |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270365 |
|
|
Homo sapiens |
|
pmid |
sentence |
28271488 |
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that specifically aminoacylate one tRNA molecule by the cognate amino acid. In mammals, nine synthetases, those specific for amino acids Arg, Asp, Gln, Glu, Ile, Leu, Lys, Met and Pro, associate into a multi-aminoacyl-tRNA synthetase complex, an association which is believed to play a key role in the cellular organization of translation, but also in the regulation of the translational and nontranslational functions of these enzymes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
arginine | up-regulates quantity
precursor of
|
Arg-tRNA(Arg) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270370 |
|
|
Homo sapiens |
|
pmid |
sentence |
28271488 |
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that specifically aminoacylate one tRNA molecule by the cognate amino acid. In mammals, nine synthetases, those specific for amino acids Arg, Asp, Gln, Glu, Ile, Leu, Lys, Met and Pro, associate into a multi-aminoacyl-tRNA synthetase complex, an association which is believed to play a key role in the cellular organization of translation, but also in the regulation of the translational and nontranslational functions of these enzymes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |