Gene Ontology annotation through association of InterPro records with GO terms
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
Combined Automated Annotation using Multiple IEA Methods
A novel mutation in the NADH-cytochrome b5 reductase gene of a Chinese patient with recessive congenital methemoglobinemia.
Enzymatic instability of NADH-cytochrome b5 reductase as a cause of hereditary methemoglobinemia type I (red cell type).
Identification of major proteins in the lipid droplet-enriched fraction isolated from the human hepatocyte cell line HuH7.
Structure of human erythrocyte NADH-cytochrome b5 reductase.
Recessive congenital methaemoglobinaemia: functional characterization of the novel D239G mutation in the NADH-binding lobe of cytochrome b5 reductase.
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The D239G variant alters nicotinamide-cofactor specificity, illustrating a mutant effect rather than identical wild-type NADH and NADPH activity.
"decreased specificity for NADH and increased specificity for NADPH"
Structural role of serine 127 in the NADH-binding site of human NADH-cytochrome b5 reductase.
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Human wild-type and Ser127 variants were assayed with NADH and cytochrome b5, directly anchoring the specific reductase chemistry.
"with cytochrome b5 as an electron acceptor"
Defining the membrane proteome of NK cells.
Role of cysteine residues in human NADH-cytochrome b5 reductase studied by site-directed mutagenesis. Cys-273 and Cys-283 are located close to the NADH-binding site but are not catalytically essential.
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Human cysteine substitutions alter the enzyme-FAD reduction rate and NADH-site behavior without making those cysteines universally catalytically essential.
"C273A and C273A/C283A mutants showed approximately one-fifth of the enzyme-FAD reduction rate"
Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes.
Endothelial cell expression of haemoglobin α regulates nitric oxide signalling.
Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2.
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The reconstituted system requires CYB5R3 electron delivery, while molybdenum-dependent terminal nitrite reduction occurs in mARC.
"mARC is the catalytic subunit"
Histone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry in Intact Cell Nuclei.
A reference map of the human binary protein interactome.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
The UFM1 system regulates ER-phagy through the ufmylation of CYB5R3.
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The study identifies ER-membrane CYB5R3 and distinguishes its ufmylated, inactivated cargo state.
"that localizes on the ER membrane"
An in-frame deletion of codon 298 of the NADH-cytochrome b5 reductase gene results in hereditary methemoglobinemia type II (generalized type). A functional implication for the role of the COOH-terminal region of the enzyme.
Identification of alternative first exons of NADH-cytochrome b5 reductase gene expressed ubiquitously in human cells.
An erythroid-specific transcript generates the soluble form of NADH-cytochrome b5 reductase in humans.
CYB5R3:FAD reduces CYB5A:ferriheme to CYB5A:heme
Exocytosis of azurophil granule lumen proteins
MARC1,MARC2 reduce N-hydroxylated compounds
Papillon-Lefèvre syndrome patient reveals species-dependent requirements for neutrophil defenses.
CYB5R3 source and assay guide