Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones.
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ISD11 co-localizes with frataxin and mitochondria
"Immunofluorescence analysis demonstrated that ISD11 co-localized with both frataxin and with mitochondria."
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ISD11 depletion causes decline of NFS1/ISCU complex and aconitase activity
"Upon ISD11 depletion by siRNA in HEK293T cells, the amount of the Nfs1/ISCU protein complex declined, as did the activity of the iron-sulfur cluster enzyme aconitase"
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Frataxin-ISD11 interaction is nickel-dependent
"The frataxin/ISD11 interaction was also decreased by the chelator EDTA, and was increased by supplementation with nickel but not other metal ions"
A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis.
Mammalian frataxin: an essential function for cellular viability through an interaction with a preformed ISCU/NFS1/ISD11 iron-sulfur assembly complex.
The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans.
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NFS1 and ISD11 localize to mitochondria and nucleus
"NFS1 and ISD11 are present in mitochondria and in the nucleus"
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ISD11 is a stabilization factor for NFS1
"ISD11 was described as a stabilization factor of NFS1 which is essential for its activity in FeS cluster formation in mitochondria"
Mapping Key Residues of ISD11 Critical for NFS1-ISD11 Subcomplex Stability: IMPLICATIONS IN THE DEVELOPMENT OF MITOCHONDRIAL DISORDER, COXPD19.
Mitochondrial Protein Interaction Mapping Identifies Regulators of Respiratory Chain Function.
Architecture of the Human Mitochondrial Iron-Sulfur Cluster Assembly Machinery.
Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions.
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Crystal structure shows ISD11 subunits form dimeric core of SDA complex
"the SDA structure adopts an unexpected architecture in which a pair of ISD11 subunits form the dimeric core of the SDA complex"
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ACP acyl chain occupies hydrophobic core of ISD11
"the 4'-phosphopantetheine-conjugated acyl-group of ACP occupies the hydrophobic core of ISD11, explaining the basis of ACP stabilization"
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ISD11 clarifies critical role in eukaryotic Fe-S assemblies
"a pair of ISD11 subunits form the dimeric core of the SDA complex, which clarifies the critical role of ISD11 in eukaryotic assemblies"
Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex.
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Crystal structures of NFS1-ISD11-ACP complexes with/without ISCU
"we present crystal structures of three different NFS1-ISD11-ACP complexes with and without ISCU"
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ISD11 homodimerizes in the complex
"Crystal structures of (NFS1-ISD11-ACP)2 and (NFS1-ISD11-ACP-ISCU)2 complexes"
Structure of the human frataxin-bound iron-sulfur cluster assembly complex provides insight into its activation mechanism.
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3.2A cryo-EM structure of NFS1-ISD11-ACP-ISCU-FXN complex
"Here the 3.2 Å resolution cryo-electron microscopy structure of the FXN-bound active human complex, containing two copies of the NFS1-ISD11-ACP-ISCU-FXN hetero-pentamer"
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ISD11 is accessory protein in core ISC complex
"cysteine desulfurase NFS1 that is activated by frataxin (FXN), scaffold protein ISCU, accessory protein ISD11, and acyl-carrier protein ACP"
Structure of the Human ACP-ISD11 Heterodimer.
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2.0A crystal structure of ACP-ISD11 heterodimer
"the structure of the human mitochondrial ACP-ISD11 heterodimer was determined at 2.0 Å resolution"
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Phosphopantetheine-acyl chain interacts with ISD11 residues
"The 4'-phosphopantetheine-acyl chain, which is covalently bound to ACP, interacts with several residues of ISD11"
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ACP-ISD11 modulates NFS1 foldability
"modulating together with ACP the foldability of ISD11"
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
N-terminal tyrosine of ISCU2 triggers [2Fe-2S] cluster synthesis by ISCU2 dimerization.
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High resolution crystal structures of NFS1-ISD11-ACP-ISCU2 complexes
"we crystallized the dimeric (NIAU2)2 complex containing wild-type or various mutant ISCU2 proteins...for wild-type ISCU2, diffracted up to 1.8 Å resolution"
FXN:NFS1:ISD11:ISCU assembles 2Fe-2S iron-sulfur cluster
Transfer of Fe-S clusters to SDHB
2Fe-2S is inserted in UQCRFS1
Deep research report on LYRM4