| + |
L-thyroxine | up-regulates 
|
Fatty_Acid_Biosynthesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267489 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24692351 |
TH stimulates both lipolysis and lipogenesis, although the direct action is lipolysis with lipogenesis thought to be stimulated to restore fat stores. Fatty acids produced from TH-induced lipolysis are the substrate for the increase in thermogenesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Liver |
| Pathways: | Thyroid Hormone Metabolism |
| + |
3,3',5'-triiodothyronine | up-regulates
|
Fatty_Acid_Biosynthesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267488 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24692351 |
TH stimulates both lipolysis and lipogenesis, although the direct action is lipolysis with lipogenesis thought to be stimulated to restore fat stores. Fatty acids produced from TH-induced lipolysis are the substrate for the increase in thermogenesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Liver |
| Pathways: | Thyroid Hormone Metabolism |
| + |
FASN | up-regulates
|
Fatty_Acid_Biosynthesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270536 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9356448 |
Our model of the native fatty acid synthase (FAS) depicts it as a dimer of two identical multifunctional proteins (Mr approximately 272,000) arranged in an antiparallel configuration so that the active Cys-SH of the beta-ketoacyl synthase of one subunit (where the acyl group is attached) is juxtaposed within 2 A of the pantetheinyl-SH of the second subunit (where the malonyl group is bound). This arrangement generates two active centers for fatty acid synthesis and predicts that if we have two appropriate halves of the monomer, we should be able to reconstitute an active fatty acid-synthesizing site |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268159 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9356448 |
Our model of the native fatty acid synthase (FAS) depicts it as a dimer of two identical multifunctional proteins (Mr approximately 272,000) arranged in an antiparallel configuration so that the active Cys-SH of the beta-ketoacyl synthase of one subunit (where the acyl group is attached) is juxtaposed within 2 A of the pantetheinyl-SH of the second subunit (where the malonyl group is bound). This arrangement generates two active centers for fatty acid synthesis and predicts that if we have two appropriate halves of the monomer, we should be able to reconstitute an active fatty acid-synthesizing site |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Circadian clock |
| + |
acetyl-CoA | up-regulates activity
|
Fatty_Acid_Biosynthesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267383 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10893421 |
Acetyl-CoA carboxylase (ACC) catalyzes the first committed step of the fatty acid synthetic pathway. Although ACC has often been proposed to be a major rate-controlling enzyme of this pathway, no direct tests of this proposal in vivo |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Citric acid cycle, Glycolysis and Gluconeogenesis |
3.0
Fatty_Acid_Biosynthesis