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http://purl.uniprot.org/citations/10922362http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10922362http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10922362http://www.w3.org/2000/01/rdf-schema#comment"Hyperhomocysteinemia, a risk factor for vascular disease, injures endothelial cells through undefined mechanisms. We previously identified several homocysteine-responsive genes in cultured human vascular endothelial cells, including the endoplasmic reticulum (ER)-resident molecular chaperone GRP78/BiP. Here, we demonstrate that homocysteine induces the ER stress response and leads to the expression of a novel protein, Herp, containing a ubiquitin-like domain at the N terminus. mRNA expression of Herp was strongly up-regulated by inducers of ER stress, including mercaptoethanol, tunicamycin, A23187, and thapsigargin. The ER stress-dependent induction of Herp was also observed at the protein level. Immunochemical analyses using Herp-specific antibodies indicated that Herp is a 54-kDa, membrane-associated ER protein. Herp is the first integral membrane protein regulated by the ER stress response pathway. Both the N and C termini face the cytoplasmic side of the ER; this membrane topology makes it unlikely that Herp acts as a molecular chaperone for proteins in the ER, in contrast to GRP78 and other ER stress-responsive proteins. Herp may, therefore, play an unknown role in the cellular survival response to stress."xsd:string
http://purl.uniprot.org/citations/10922362http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m002063200"xsd:string
http://purl.uniprot.org/citations/10922362http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m002063200"xsd:string
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/author"Kato H."xsd:string
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/author"Kato H."xsd:string
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/author"Miyata T."xsd:string
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/author"Miyata T."xsd:string
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/author"Kokame K."xsd:string
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/author"Kokame K."xsd:string
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/author"Agarwala K.L."xsd:string
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/author"Agarwala K.L."xsd:string
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/pages"32846-32853"xsd:string
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/pages"32846-32853"xsd:string
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/title"Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress."xsd:string
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/title"Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress."xsd:string
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/volume"275"xsd:string
http://purl.uniprot.org/citations/10922362http://purl.uniprot.org/core/volume"275"xsd:string
http://purl.uniprot.org/citations/10922362http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10922362
http://purl.uniprot.org/citations/10922362http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10922362