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ProteomicsERO1 alpha deficiency increases N-glycosylation of a proangiogenic VEGFA by MAGT1-dependent OST complex
N-glycosylation and disulfide bond formation are two essential steps in protein folding, that both take place in the endoplasmic reticulum (ER). These two modifications can influence each other, but the exact timing, as well as the mediators of this important crosstalk, are still not completely eluc...
ORGANISM(S): Homo sapiens (Human) 
2022-08-29 | PXD033941 | Pride
Vegfa Ero1 alpha N-glycosylation Nlc-esi-ms/ms Oxidative folding 
TranscriptomicsSEPN1-related myopathy depends on the ER oxidase ERO1 alpha and is responsive to the chemical chaperone TUDCA
SEPN1 is a type II protein of the endoplasmic reticulum (ER) whose loss of function gives rise to a collection of debilitating autosomal recessive myopathies gathered under the umbrella term of SEPN1-related myopathy (RM). At the moment, SEPN1-RM lacks an effective pharmacological treatment; thus, t...
ORGANISM(S): Mus musculus 
2024-02-14 | E-MTAB-12460 | biostudies-arrayexpress
TranscriptomicsDeficiency of ERO1 and activation of protein translation synergistically impair breast tumor resilience
Endoplasmic reticulum (ER) stress triggers an adaptive response which fosters tumor cell survival and resilience to stress conditions. Activation of the endoplasmic reticulum stress response, through its PERK branch, promotes the phosphorylation of the α-subunit of translation initiation factor eIF2...
ORGANISM(S): Homo sapiens 
2022-07-20 | E-MTAB-11313 | biostudies-arrayexpress
ProteomicsSEPN1-related myopathy depends on the oxidoreductase ERO1 alpha and is druggable with the chemical chaperone TUDCA
SEPN1-related myopathy depends on the oxidoreductase ERO1 alpha and is druggable with the chemical chaperone TUDCA
ORGANISM(S): Homo sapiens (Human) 
2024-05-24 | PXD047157 | Pride
Tudca Multi mini-core disease Er stress Ero1 Sepn1 Core myopathy 
GenomicsSEPN1-related myopathy depends on the ER oxidase ERO1 alpha and is responsive to the chemical chaperone TUDCA
SEPN1-related myopathy depends on the ER oxidase ERO1 alpha and is responsive to the chemical chaperone TUDCA
PRJEB64682 | ENA
GenomicsDeficiency of ERO1 and activation of protein translation synergistically impair breast tumor resilience
Deficiency of ERO1 and activation of protein translation synergistically impair breast tumor resilience
PRJEB52741 | ENA
UnknownAdiponectin secretion is regulated by SIRT1 and the endoplasmic reticulum oxidoreductase Ero1-L alpha.
Not available
S-EPMC1951471 | biostudies-literature
UnknownCancer-associated oxidoreductase ERO1-α drives the production of VEGF via oxidative protein folding and regulating the mRNA level.
Not available
S-EPMC4891497 | biostudies-literature
UnknownERO1 alpha deficiency impairs angiogenesis by increasing N-glycosylation of a proangiogenic VEGFA.
Not available
S-EPMC9463388 | biostudies-literature
TranscriptomicsGene-expression profiling of SEPN1 knockout or wild type mice injected with either ERO1 or PBS
Endoplasmic reticulum (ER) and oxidative stress are two related phenomena that have important metabolic consequences. As many skeletal muscle diseases are triggered by oxidative stress, we explored the chain of events linking a hyper oxidized ER (which causes ER and oxidative stress) with skeletal m...
ORGANISM(S): Mus musculus 
2016-10-01 | E-MTAB-4933 | biostudies-arrayexpress
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