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dc.contributor.authorPreissler, S
dc.date.accessioned2021-10-18T08:42:55Z
dc.date.available2021-10-18T08:42:55Z
dc.date.issued2020-11
dc.identifier.issn0947-0867
dc.identifier.others12268-020-1455-6
dc.identifier.other1455
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/329487
dc.description.abstract<jats:title>Abstract</jats:title><jats:p>Maintenance of protein homeostasis depends on cellular stress response pathways that mediate adaptive changes in gene expression. In the endoplasmic reticulum additional mechanisms adjust the availability of the abundant Hsp70-type chaperone, BiP, during short-term fluctuations in the unfolded protein load. Here, recent insights into the regulation of BiP by incorporation into inactive oligomers and reversible AMPylation are discussed.</jats:p>
dc.languagede
dc.publisherSpringer Science and Business Media LLC
dc.subjectWissenschaft
dc.titleRegulation of chaperone activity in the endoplasmic reticulum
dc.typeArticle
dc.date.updated2021-10-18T08:42:54Z
prism.endingPage614
prism.issueIdentifier6
prism.publicationNameBioSpektrum
prism.startingPage612
prism.volume26
dc.identifier.doi10.17863/CAM.76935
rioxxterms.versionofrecord10.1007/s12268-020-1455-6
rioxxterms.versionVoR
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/
dc.contributor.orcidPreissler, Steffen [0000-0001-7936-9836]
dc.identifier.eissn1868-6249
cam.issuedOnline2020-10-14


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