| + |
iron-sulfur cluster | up-regulates activity 
chemical activation
|
Mitochondrial respiratory chain complex III |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262137 |
|
|
|
|
| pmid |
sentence |
| 26083061 |
Respiratory chain complexes I–III depend on Fe-S clusters for function |
|
| Publications: |
1 |
| + |
Mitochondrial Fe-S Cluster Assembly Complex | up-regulates quantity
chemical modification
|
iron-sulfur cluster |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262129 |
|
|
in vitro |
|
| pmid |
sentence |
| 27519411 |
As the architecture of the human machinery remains undefined, we co-expressed in Escherichia coli the following four proteins involved in the initial step of Fe-S cluster synthesis: FXN42-210 (iron donor); [NFS1]·[ISD11] (sulfur donor); and ISCU (scaffold upon which new clusters are assembled). We purified a stable, active complex consisting of all four proteins with 1:1:1:1 stoichiometry. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
iron-sulfur cluster | up-regulates activity
chemical activation
|
Mitochondrial respiratory chain complex I |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262135 |
|
|
|
|
| pmid |
sentence |
| 26083061 |
Respiratory chain complexes I–III depend on Fe-S clusters for function |
|
| Publications: |
1 |
| + |
HSPA9 | up-regulates activity
relocalization
|
iron-sulfur cluster |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262131 |
|
|
|
|
| pmid |
sentence |
| 27714045 |
Cluster transfer from ISCU to recipient apoproteins is assisted by a dedicated chaperone/cochaperone (HSPA9/HSC20) system that facilitates cluster release from the primary scaffold ISCU and transfer to recipient apoproteins or to intermediate carriers |
|
| Publications: |
1 |
| + |
iron-sulfur cluster | up-regulates quantity
precursor of
|
D-threo-isocitrate(3-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262132 |
|
|
|
|
| pmid |
sentence |
| 26083061 |
Mitochondrial aconitase and succinate dehydrogenase were among the earliest mammalian Fe-S proteins identified.|The enzymatic activity of both proteins depends on the presence of intact Fe-S clusters |
|
| Publications: |
1 |
| + |
iron-sulfur cluster | up-regulates activity
chemical activation
|
PRIM2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262134 |
|
|
|
|
| pmid |
sentence |
| 26083061 |
Human DNA primase, are Fe-S proteins. The loss of an iron-sulfur cluster in RAD3 helicase results in a failure to unwind DNA1 |
|
| Publications: |
1 |
| + |
iron-sulfur cluster | up-regulates activity
chemical activation
|
SDHB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262133 |
|
|
|
|
| pmid |
sentence |
| 26083061 |
Succinate dehydrogenase subunit B contains three Fe-S clusters |The enzymatic activity of both proteins depends on the presence of intact Fe-S clusters |
|
| Publications: |
1 |
| + |
HSCB | up-regulates activity
relocalization
|
iron-sulfur cluster |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262130 |
|
|
|
|
| pmid |
sentence |
| 27714045 |
Cluster transfer from ISCU to recipient apoproteins is assisted by a dedicated chaperone/cochaperone (HSPA9/HSC20) system that facilitates cluster release from the primary scaffold ISCU and transfer to recipient apoproteins or to intermediate carriers |
|
| Publications: |
1 |
| + |
iron-sulfur cluster | up-regulates activity
chemical activation
|
Mitochondrial respiratory chain complex II |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262136 |
|
|
|
|
| pmid |
sentence |
| 26083061 |
Respiratory chain complexes I–III depend on Fe-S clusters for function |
|
| Publications: |
1 |
3.0
iron-sulfur cluster