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Sökning: id:"swepub:oai:DiVA.org:kth-141008" > Multicolor Fluoresc...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004180naa a2200541 4500
001oai:DiVA.org:kth-141008
003SwePub
008140205s2014 | |||||||||||000 ||eng|
009oai:prod.swepub.kib.ki.se:129082602
024a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-1410082 URI
024a https://doi.org/10.1021/nn406113m2 DOI
024a http://kipublications.ki.se/Default.aspx?queryparsed=id:1290826022 URI
040 a (SwePub)kthd (SwePub)ki
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Rönnlund, Daniel,d 1984-u KTH,Experimentell biomolekylär fysik4 aut0 (Swepub:kth)u1vmbh2t
2451 0a Multicolor Fluorescence Nanoscopy by Photobleaching :b Concept Verification and its Application to Resolve Selective Storage of Proteins in Platelets
264 c 2014-04-24
264 1b American Chemical Society (ACS),c 2014
338 a electronic2 rdacarrier
500 a Updated from "Submitted" to "Published". QC 20140630
520 a Fluorescence nanoscopy provides means to discernthe finer details of protein localization and interaction in cells by offeringan order of magnitude higher resolution than conventional optical imagingtechniques. However, these super resolution techniques put higher demands onthe optical system as well as on the fluorescent probes, making multicolorfluorescence nanoscopy a challenging task. Here we present a new and simpleprocedure which exploits the photostability and excitation spectra of dyes toincrease the number of simultaneous recordable targets in STED nanoscopy. Weuse this procedure to demonstrate four color STED imaging of platelets with ≤40 nm resolution and low crosstalk. Platelets can selectively store, sequesterand release a multitude of different proteins, and in a manner specific fordifferent physiological and disease states. By applying multicolor nanoscopy tostudy platelets, we can achieve spatial mapping of the protein organizationwith a high resolution, for multiple proteins at the same time and in the samecell. This provides a means to identify specific platelet activation states fordiagnostic purposes and to understand the underlying protein storage andrelease mechanisms. We studied the organization of the pro- and anti-angiogenicproteins VEGF and PF-4 together with fibrinogen and filamentous actin, andfound distinct features in their respective protein localization. Further,colocalization analysis revealed only minor overlap between the proteins VEGFand PF-4 indicating that they have separate storage and release mechanisms,corresponding well with their opposite rules as pro- and anti-angiogenicproteins, respectively.
650 7a NATURVETENSKAPx Fysik0 (SwePub)1032 hsv//swe
650 7a NATURAL SCIENCESx Physical Sciences0 (SwePub)1032 hsv//eng
653 a multicolor
653 a super resolution microscopy
653 a photobleaching
653 a STED
653 a platelets
653 a thrombocytes
653 a α-granules
653 a Biological Physics
653 a Biologisk fysik
700a Xu, Leiu KTH,Experimentell biomolekylär fysik4 aut0 (Swepub:kth)u1zr7k1u
700a Perols, Annau KTH,Proteinteknologi4 aut0 (Swepub:kth)u11lpgnl
700a Eriksson Karlström, Amelieu KTH,Proteinteknologi4 aut0 (Swepub:kth)u10x6l4n
700a Auer, Gertu Karolinska Institutet4 aut
700a Widengren, Jerkeru KTH,Experimentell biomolekylär fysik4 aut0 (Swepub:kth)u1i3g09c
700a Gad, AKBu Karolinska Institutet4 aut
710a KTHb Experimentell biomolekylär fysik4 org
773t ACS Nanod : American Chemical Society (ACS)g 8:5, s. 4358-4365q 8:5<4358-4365x 1936-0851x 1936-086X
856u https://kth.diva-portal.org/smash/get/diva2:693793/FULLTEXT01.pdfx primaryx Raw objecty fulltext:preprint
856u http://kth.diva-portal.org/smash/get/diva2:693793/FULLTEXT01
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-141008
8564 8u https://doi.org/10.1021/nn406113m
8564 8u http://kipublications.ki.se/Default.aspx?queryparsed=id:129082602

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