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Iron-sulfur (Fe-S) clusters are necessary for several mitochondrial enzymes and other subcellular compartment proteins. Additionally we are shipping ISCU Antibodies (59) and many more products for this protein.
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We have shown that ASO treatment diminished aberrant splicing and increased ISCU protein levels in both patient fibroblasts and patient myotubes in a concentration dependent fashion. Upon ASO treatment, levels of SDHB (show SDHB Proteins) in patient myotubular cell lines increased to levels observed in control myotubular cell lines
The NFS1 (show NFS1 Proteins)/ISD11 (show LYRM4 Proteins) complex further interacts with scaffold protein (show HOMER1 Proteins) ISCU and regulator protein frataxin (show FXN Proteins), thereby forming a quaternary complex for Fe-S cluster formation.
Molecular dynamics flexible fitting of protein structures docked into the EM map of the model revealed a [FXN (show FXN Proteins)(42-210)]24.[NFS1 (show NFS1 Proteins)]24.[ISD11 (show LYRM4 Proteins)]24.[ISCU]24 complex, consistent with the measured 1:1:1:1 stoichiometry of its four components.
ISCU expression was decreased in the majority of human liver cancer tissues, and its reduced expression was significantly associated with p53 (show TP53 Proteins) mutation.
Thus, driven by acquired (hypoxia) or genetic causes, the miR (show MLXIP Proteins)-210-ISCU1/2 regulatory axis is a pathogenic lynchpin causing iron-sulfur deficiency and pulmonary hypertension.
The core Fe-S biosynthetic enzymatic complex generated [2Fe-2S] cluster intermediates that converted to stable [2Fe-2S] clusters bound to uncomplexed ISCU2.
IscU is a new substrate of MK2 (show KCNA2 Proteins) both in Drosophila cells and in human cells
Fe-S assembly protein (ISCU2) and frataxin (show FXN Proteins) convert substrates l-cysteine, ferrous iron, and electrons into Fe-S clusters.
the G50E iron-sulfur cluster scaffold protein (show NFU1 Proteins) (ISCU) mutation has a role in mitochondrial myopathy
NFS1 (show NFS1 Proteins) binds preferentially to the D-state of ISCU while mtHSP70 (show HSPA9 Proteins) binds preferentially to the D-state of ISCU and HSC20 (show HSCB Proteins) binds preferentially to the S-state of ISCU.
IscU is a marginally stable protein at low ionic strength to the point that undergoes cold denaturation at around -8 degrees C with a corresponding dramatic decrease of enthalpy, which is consistent with the fluxional nature of the protein.
mTORC1 associates with ISCU and phosphorylates ISCU at serine 14. This phosphorylation stabilized ISCU protein.
Data show that complete loss of ISCU results in early embryonic death and confirm a fundamental role for ISCU in mammals.
While IFN-gamma (show IFNG Proteins) alone induced Nfs1 (show NFS1 Proteins) protein instability, LPS (show TLR4 Proteins) triggered a delayed decline of Nfs1 (show NFS1 Proteins), rather involving transcriptional events or mRNA instability.
Iron-sulfur (Fe-S) clusters are necessary for several mitochondrial enzymes and other subcellular compartment proteins. They contain sulfur and iron, and are created via several steps that include cysteine desulfurases, iron donors, chaperones, and scaffold proteins. This gene encodes the two isomeric forms, ISCU1 and ISCU2, of the Fe-S cluster scaffold protein. Mutations in this gene have been found in patients with myopathy with severe exercise intolerance and myoglobinuria.
iron-sulfur cluster assembly enzyme ISCU, mitochondrial
, iron-sulfur cluster scaffold homolog (E. coli)
, iron-sulfur cluster assembly enzyme
, IscU iron-sulfur cluster scaffold homolog (E. coli)
, NifU-like N-terminal domain containing
, zC191D15.3 (novel protein with leucine-rich repeat domains)
, IscU iron-sulfur cluster scaffold homolog
, iron-sulfur cluster scaffold homolog
, nifU-like N-terminal domain-containing protein
, nifU-like protein