PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 35162999-5 2022 We sought to determine whether PDIA3 is required for disulfide bonds of NA, its activity, and propagation of the virus. Disulfides 53-62 protein disulfide isomerase associated 3 Mus musculus 31-36 35162999-6 2022 Requirement of disulfides for NA oligomerization and activity were determined using biotin switch and redox assays in WT and PDIA3-/- in A549 cells. Disulfides 15-25 protein disulfide isomerase associated 3 Mus musculus 125-130 33541434-0 2021 Protein disulfide isomerase ERp57 protects early muscle denervation in experimental ALS. Disulfides 8-17 protein disulfide isomerase associated 3 Mus musculus 28-33 33541434-5 2021 ERp57 catalyzes disulfide bond formation and isomerization in the endoplasmic reticulum (ER), constituting a central component of protein quality control mechanisms. Disulfides 16-25 protein disulfide isomerase associated 3 Mus musculus 0-5 22207737-1 2012 A close homologue to protein disulfide isomerase (PDI) called ERp57 forms disulfide bonds in glycoproteins in the endoplasmic reticulum and is expressed on the platelet surface. Disulfides 29-38 protein disulfide isomerase associated 3 Mus musculus 62-67 32316996-0 2020 Disulfide isomerase ERp57 improves the stability and immunogenicity of H3N2 influenza virus hemagglutinin. Disulfides 0-9 protein disulfide isomerase associated 3 Mus musculus 20-25 30399388-2 2019 In the present study, we investigated the effects of protein disulfide-isomerase A3 (PDIA3), an ER-resident chaperone that catalyzes disulfide-bond formation in a subset of glycoproteins, against oxidative damage in the hypoxic HT22 cell line and against ischemic damage in the gerbil hippocampus. Disulfides 61-70 protein disulfide isomerase associated 3 Mus musculus 85-90 26361352-1 2015 ERp57 (also known as grp58 and PDIA3) is a protein disulfide isomerase that catalyzes disulfide bonds formation of glycoproteins as part of the calnexin and calreticulin cycle. Disulfides 51-60 protein disulfide isomerase associated 3 Mus musculus 0-5 26361352-1 2015 ERp57 (also known as grp58 and PDIA3) is a protein disulfide isomerase that catalyzes disulfide bonds formation of glycoproteins as part of the calnexin and calreticulin cycle. Disulfides 51-60 protein disulfide isomerase associated 3 Mus musculus 21-26 26361352-1 2015 ERp57 (also known as grp58 and PDIA3) is a protein disulfide isomerase that catalyzes disulfide bonds formation of glycoproteins as part of the calnexin and calreticulin cycle. Disulfides 51-60 protein disulfide isomerase associated 3 Mus musculus 31-36 25704664-3 2015 ERp57 is a member of the protein disulfide isomerase (PDI) family and facilitates correct folding of newly synthesized glycoproteins by rearrangement of native disulfide bonds. Disulfides 33-42 protein disulfide isomerase associated 3 Mus musculus 0-5 30647818-12 2018 We analyzed cartilage-specific ERp57 knockout mice and demonstrated that the deficiency of this single protein disulfide isomerase, which is responsible for formation of disulfide bridges in ECM glycoproteins, is sufficient to induce ER stress and to cause an ER stress-related bone phenotype. Disulfides 111-120 protein disulfide isomerase associated 3 Mus musculus 31-36 26435004-9 2016 Furthermore, we observed that disulfide bridges in eotaxin, epidermal growth factor, and periostin were also decreased in the lungs of house dust mite-challenged ERp57-deleted mice. Disulfides 30-39 protein disulfide isomerase associated 3 Mus musculus 162-167 24364984-7 2013 SiRNA-mediated knockdown of ATF6alpha and ERp57 during HDM administration in mice resulted in a decrease in components of HDM-induced ER stress, disulfide mediated oligomerization of Bak, and activation of caspase-3. Disulfides 145-154 protein disulfide isomerase associated 3 Mus musculus 42-47 20130111-6 2010 Moreover, treatment with sulfhydryl-modifying agents that oxidize SH-groups of cysteine residues to disulfide bonds abolished ATRA-mediated RARA nuclear localization, suggesting that the thiol oxidoreductase activity of GRp58 may be required for RARA nuclear import. Disulfides 100-109 protein disulfide isomerase associated 3 Mus musculus 220-225 19687800-4 2010 We showed that a large disulfide-bonded complex was present in the mouse cells that included ERp57, tapasin, and K(d). Disulfides 23-32 protein disulfide isomerase associated 3 Mus musculus 93-98 15772339-0 2005 The disulfide isomerase Grp58 is a protective factor against prion neurotoxicity. Disulfides 4-13 protein disulfide isomerase associated 3 Mus musculus 24-29 8050492-9 1994 These results indicate that ERp61 may be involved in disulfide bond formation for such proteins. Disulfides 53-62 protein disulfide isomerase associated 3 Mus musculus 28-33 34904718-2 2022 Here, we report identification of a homozygous c.170G>A (p.Cys57Tyr or C57Y) mutation in the gene coding for protein disulfide isomerase A3 (PDIA3, also known as ERp57), an enzyme that catalyzes formation of disulfide bonds in the endoplasmic reticulum, to be associated with syndromic intellectual disability. Disulfides 208-217 protein disulfide isomerase associated 3 Mus musculus 109-139 34904718-2 2022 Here, we report identification of a homozygous c.170G>A (p.Cys57Tyr or C57Y) mutation in the gene coding for protein disulfide isomerase A3 (PDIA3, also known as ERp57), an enzyme that catalyzes formation of disulfide bonds in the endoplasmic reticulum, to be associated with syndromic intellectual disability. Disulfides 208-217 protein disulfide isomerase associated 3 Mus musculus 141-146 34904718-2 2022 Here, we report identification of a homozygous c.170G>A (p.Cys57Tyr or C57Y) mutation in the gene coding for protein disulfide isomerase A3 (PDIA3, also known as ERp57), an enzyme that catalyzes formation of disulfide bonds in the endoplasmic reticulum, to be associated with syndromic intellectual disability. Disulfides 208-217 protein disulfide isomerase associated 3 Mus musculus 162-167 34904718-6 2022 Biochemical studies show that PDIA3C57Y has decreased catalytic activity and forms disulfide-crosslinked aggregates that abnormally interact with chaperones in the endoplasmic reticulum. Disulfides 83-92 protein disulfide isomerase associated 3 Mus musculus 30-35