Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10800003 | Biochimica et Biophysica Acta (BBA) - General Subjects | 2015 | 13 Pages |
Abstract
Our results suggest that the accumulation of pathogenic lysozymes in the ER caused ER stress and the UPR response mainly via the IRE1α pathway.
Keywords
eIF2αP58IPKXBP-1sGrowth arrest and DNA damage-inducible proteinErdj4EDEM1HRD1p-eIF2αXBP-1GRP94Gadd45PDIATF6αIRE1UPRGAPDHATF4DAPIC/EBP homologous proteinGRP78/BiPRNA interferenceRNAiAmyloidosisinositol-requiring enzyme 1ER stressCHOPMutantsdiamidino-2-phenylindoleARMETendoplasmic reticulumeukaryotic initiation factor 2αactivating transcription factor 6αlysozymeUnfolded protein responseprotein disulfide isomerasePERKglyceraldehyde-3-phosphate dehydrogenase
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Authors
Yoshiki Kamada, Takahiro Kusakabe, Yasushi Sugimoto,