File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Non-covalent Binding of Luminescent Transition Metal Polypyridine Complexes to Avidin, Iodole-binding Proteins and Estrogen Receptors

TitleNon-covalent Binding of Luminescent Transition Metal Polypyridine Complexes to Avidin, Iodole-binding Proteins and Estrogen Receptors
Authors
KeywordsAvidin
Biological probes
Biotin
Estrogen receptors
Indole-binding proteins
Issue Date2007
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/ccr
Citation
Coordination Chemistry Reviews, 2007, v. 251 n. 17-20, p. 2292-2310 How to Cite?
AbstractA number of luminescent transition metal complexes possess rich photophysical and photochemical properties that allow them to serve as useful labels and probes for biological molecules. This article describes the current trend in this area of research, with emphasis on our recent work on luminescent rhenium(I), iridium(III) and ruthenium(II) polypyridine complexes as non-covalent probes for avidin, indole-binding proteins and estrogen receptors. We focus on the molecular design, photophysical properties and biomolecule-binding behaviour of these systems; different approaches to enhancing the detection sensitivity are also discussed.
Persistent Identifierhttp://hdl.handle.net/10722/69031
ISSN
2021 Impact Factor: 24.833
2020 SCImago Journal Rankings: 5.166
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLo, KKWen_HK
dc.contributor.authorTsang, KHKen_HK
dc.contributor.authorSze, KSen_HK
dc.contributor.authorChung, CKen_HK
dc.contributor.authorLee, TKMen_HK
dc.contributor.authorZhang, KYen_HK
dc.contributor.authorHui, WKen_HK
dc.contributor.authorLi, CKen_HK
dc.contributor.authorLau, JSYen_HK
dc.contributor.authorNg, DCMen_HK
dc.contributor.authorZhu, Nen_HK
dc.date.accessioned2010-09-06T06:09:55Z-
dc.date.available2010-09-06T06:09:55Z-
dc.date.issued2007en_HK
dc.identifier.citationCoordination Chemistry Reviews, 2007, v. 251 n. 17-20, p. 2292-2310en_HK
dc.identifier.issn0010-8545en_HK
dc.identifier.urihttp://hdl.handle.net/10722/69031-
dc.description.abstractA number of luminescent transition metal complexes possess rich photophysical and photochemical properties that allow them to serve as useful labels and probes for biological molecules. This article describes the current trend in this area of research, with emphasis on our recent work on luminescent rhenium(I), iridium(III) and ruthenium(II) polypyridine complexes as non-covalent probes for avidin, indole-binding proteins and estrogen receptors. We focus on the molecular design, photophysical properties and biomolecule-binding behaviour of these systems; different approaches to enhancing the detection sensitivity are also discussed.-
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/ccren_HK
dc.relation.ispartofCoordination Chemistry Reviewsen_HK
dc.rightsCoordination Chemistry Reviews. Copyright © Elsevier BV.en_HK
dc.subjectAvidin-
dc.subjectBiological probes-
dc.subjectBiotin-
dc.subjectEstrogen receptors-
dc.subjectIndole-binding proteins-
dc.titleNon-covalent Binding of Luminescent Transition Metal Polypyridine Complexes to Avidin, Iodole-binding Proteins and Estrogen Receptorsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0010-8545&volume=&spage=2292&epage=2310&date=2007&atitle=Non-covalent+Binding+of+Luminescent+Transition+Metal+Polypyridine+Complexes+to+Avidin,+Iodole-binding+Proteins+and+Estrogen+Receptors+en_HK
dc.identifier.emailZhu, N: nzhu@hkucc.hku.hken_HK
dc.identifier.authorityZhu, N=rp00845en_HK
dc.identifier.doi10.1016/j.ccr.2006.12.005-
dc.identifier.scopuseid_2-s2.0-34548537941-
dc.identifier.hkuros143645en_HK
dc.identifier.volume251-
dc.identifier.issue17-20-
dc.identifier.spage2292-
dc.identifier.epage2310-
dc.identifier.isiWOS:000250605400012-
dc.publisher.placeNetherlands-
dc.identifier.issnl0010-8545-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats