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dc.contributor.authorKamer, Kimberli J
dc.contributor.authorDeerinck, Thomas J
dc.contributor.authorEllisman, Mark H
dc.contributor.authorMootha, Vamsi K
dc.contributor.authorLam, Stephanie Shih-Min
dc.contributor.authorMartell, Jeffrey Daniel
dc.contributor.authorTing, Alice Y
dc.date.accessioned2017-07-11T13:04:21Z
dc.date.available2017-07-11T13:04:21Z
dc.date.issued2014-11
dc.date.submitted2014-03
dc.identifier.issn1548-7091
dc.identifier.issn1548-7105
dc.identifier.urihttp://hdl.handle.net/1721.1/110613
dc.description.abstractAPEX is an engineered peroxidase that functions as an electron microscopy tag and a promiscuous labeling enzyme for live-cell proteomics. Because limited sensitivity precludes applications requiring low APEX expression, we used yeast-display evolution to improve its catalytic efficiency. APEX2 is far more active in cells, enabling the use of electron microscopy to resolve the submitochondrial localization of calcium uptake regulatory protein MICU1. APEX2 also permits superior enrichment of endogenous mitochondrial and endoplasmic reticulum membrane proteins.en_US
dc.description.sponsorshipNational Institutes of Health (U.S.) (DP1 OD003961)en_US
dc.language.isoen_US
dc.publisherNature Publishing Groupen_US
dc.relation.isversionofhttp://dx.doi.org/10.1038/nmeth.3179en_US
dc.rightsArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.en_US
dc.sourcePMCen_US
dc.titleDirected evolution of APEX2 for electron microscopy and proximity labelingen_US
dc.typeArticleen_US
dc.identifier.citationLam, Stephanie S; Martell, Jeffrey D; Kamer, Kimberli J et al. "Directed evolution of APEX2 for electron microscopy and proximity labeling." Nature Methods 12, 1: 51–54 (January 2015) © 2015 Nature America, Incen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Chemistryen_US
dc.contributor.mitauthorLam, Stephanie Shih-Min
dc.contributor.mitauthorMartell, Jeffrey Daniel
dc.contributor.mitauthorTing, Alice Y
dc.relation.journalNature Methodsen_US
dc.eprint.versionAuthor's final manuscripten_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsLam, Stephanie S; Martell, Jeffrey D; Kamer, Kimberli J; Deerinck, Thomas J; Ellisman, Mark H; Mootha, Vamsi K; Ting, Alice Yen_US
dspace.embargo.termsNen_US
dc.identifier.orcidhttps://orcid.org/0000-0002-2687-3470
dc.identifier.orcidhttps://orcid.org/0000-0002-8277-5226
mit.licensePUBLISHER_POLICYen_US
mit.metadata.statusComplete


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