Iron

heat shock protein family A (Hsp70) member 9 ; Homo sapiens







10 Article(s)
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Pub. Year
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1 30933555 Biophysical Consequences of EVEN-PLUS Syndrome Mutations for the Function of Mortalin. 2019 Apr 25 1
2 29689452 Role of the HSPA9/HSC20 chaperone pair in promoting directional human iron-sulfur cluster exchange involving monothiol glutaredoxin 5. 2018 Jul 1
3 28380382 A Single Adaptable Cochaperone-Scaffold Complex Delivers Nascent Iron-Sulfur Clusters to Mammalian Respiratory Chain Complexes I-III. 2017 Apr 4 1
4 28848044 Regulation of mitochondrial protein import by the nucleotide exchange factors GrpEL1 and GrpEL2 in human cells. 2017 Nov 3 1
5 26702583 Mitochondrial Hspa9/Mortalin regulates erythroid differentiation via iron-sulfur cluster assembly. 2016 Jan 1
6 26749241 Disease-Causing SDHAF1 Mutations Impair Transfer of Fe-S Clusters to SDHB. 2016 Feb 9 1
7 27714045 Mammalian Fe-S proteins: definition of a consensus motif recognized by the co-chaperone HSC20. 2016 Oct 1 2
8 26491070 Congenital sideroblastic anemia due to mutations in the mitochondrial HSP70 homologue HSPA9. 2015 Dec 17 1
9 24606901 Cochaperone binding to LYR motifs confers specificity of iron sulfur cluster delivery. 2014 Mar 4 1
10 23940031 Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU). 2013 Oct 4 1