PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26491070-2 2015 Here we demonstrate that mutations in HSPA9, a mitochondrial HSP70 homolog located in the chromosome 5q deletion syndrome 5q33 critical deletion interval and involved in mitochondrial Fe-S biogenesis, result in CSA inherited as an autosomal recessive trait. Iron 184-188 heat shock protein family A (Hsp70) member 4 Homo sapiens 61-66 16386335-10 2006 The synaptosomes isolated from gerbil pre-injected with FAEE and subsequently treated with AAPH or Fe(2+)/H(2)O(2) showed induction of heme oxygenase (HO-1) and heat shock protein 70 (HSP-70) but reduced inducible nitric oxide synthase (iNOS) levels. Iron 99-101 heat shock protein family A (Hsp70) member 4 Homo sapiens 161-182 16386335-10 2006 The synaptosomes isolated from gerbil pre-injected with FAEE and subsequently treated with AAPH or Fe(2+)/H(2)O(2) showed induction of heme oxygenase (HO-1) and heat shock protein 70 (HSP-70) but reduced inducible nitric oxide synthase (iNOS) levels. Iron 99-101 heat shock protein family A (Hsp70) member 4 Homo sapiens 184-190 12271059-0 1993 Newly Imported Rieske Iron-Sulfur Protein Associates with Both Cpn60 and Hsp70 in the Chloroplast Stroma. Iron 22-26 heat shock protein family A (Hsp70) member 4 Homo sapiens 73-78 32044184-2 2020 We are interested in HSP70 induction capability of an antitumor antibiotic bleomycin which produces oxidative stress by iron chelate formation and oxygen activation in a cell. Iron 120-124 heat shock protein family A (Hsp70) member 4 Homo sapiens 21-26 17275689-5 2007 In addition, the "intracellular calcein-chelatable iron pool" was determined in the presence or absence of Hsp70 and found to be related to the sensitivity of nuclear DNA to H(2)O(2). Iron 51-55 heat shock protein family A (Hsp70) member 4 Homo sapiens 107-112 23615440-1 2013 The mitochondrial Hsp70 chaperone Ssq1 plays a dedicated role in the maturation of iron-sulfur (Fe/S) proteins, an essential process of mitochondria. Iron 96-98 heat shock protein family A (Hsp70) member 4 Homo sapiens 18-23 21755988-9 2011 This supports a model in which Hsp70 binding to apo-nNOS stabilizes an open state of the heme/substrate binding cleft to facilitate thioredoxin access to the active site cysteine that coordinates with heme iron, permitting heme binding and dimerization to the active enzyme. Iron 206-210 heat shock protein family A (Hsp70) member 4 Homo sapiens 31-36