His-87 ligand in mitoNEET is crucial for the transfer of iron sulfur clusters from mitochondria to cytosolic aconitase

scientific article published on 8 January 2016

His-87 ligand in mitoNEET is crucial for the transfer of iron sulfur clusters from mitochondria to cytosolic aconitase is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1016/J.BBRC.2016.01.040
P8608Fatcat IDrelease_dvn5a4og2jgfjevjs6dvp5qfim
P698PubMed publication ID26778000

P2093author name stringBo Shen
Jin Zhao
Tang Li
Guoqiang Tan
Danhui Liu
Feiyan Pan
Jianxin Lyu
Yin Ma
P2860cites workMitoneet mediates TNFα-induced necroptosis promoted by exposure to fructose and ethanolQ30571859
P433issue1
P304page(s)226-232
P577publication date2016-01-08
P1433published inBiochemical and Biophysical Research CommunicationsQ864228
P1476titleHis-87 ligand in mitoNEET is crucial for the transfer of iron sulfur clusters from mitochondria to cytosolic aconitase
P478volume470

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cites work (P2860)
Q47193380Analysis of NFU-1 metallocofactor binding-site substitutions-impacts on iron-sulfur cluster coordination and protein structure and function.
Q50944156Cytosolic iron chaperones: Proteins delivering iron cofactors in the cytosol of mammalian cells.
Q33808884Discovery of Novel Insulin Sensitizers: Promising Approaches and Targets.
Q91558418Glycogen branching enzyme controls cellular iron homeostasis via Iron Regulatory Protein 1 and mitoNEET
Q36352074Interactions between mitoNEET and NAF-1 in cells
Q39038630Model of the MitoNEET [2Fe-2S] Cluster Shows Proton Coupled Electron Transfer
Q51761614Phylogenetic analysis of the CDGSH iron-sulfur binding domain reveals its ancient origin.
Q50051515The unique fold and lability of the [2Fe-2S] clusters of NEET proteins mediate their key functions in health and disease

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