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Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.tetlet.2005.04.015
DC FieldValue
dc.titleAn affinity-based probe for the proteomic profiling of aspartic proteases
dc.contributor.authorChattopadhaya, S.
dc.contributor.authorChan, E.W.S.
dc.contributor.authorYao, S.Q.
dc.date.accessioned2014-06-23T05:31:47Z
dc.date.available2014-06-23T05:31:47Z
dc.date.issued2005-06-06
dc.identifier.citationChattopadhaya, S., Chan, E.W.S., Yao, S.Q. (2005-06-06). An affinity-based probe for the proteomic profiling of aspartic proteases. Tetrahedron Letters 46 (23) : 4053-4056. ScholarBank@NUS Repository. https://doi.org/10.1016/j.tetlet.2005.04.015
dc.identifier.issn00404039
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/75555
dc.description.abstractWe have developed an affinity-based probe for the proteomic profiling of aspartic proteases. Our probe was shown to be selective towards aspartic proteases over other proteins. It was also shown that the strategy may be used to label selectively aspartic proteases in the presence of a large excess of other proteins, thus making it useful for future proteome profiling experiments. © 2005 Elsevier Ltd. All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.tetlet.2005.04.015
dc.sourceScopus
dc.subjectActivity-based profiling
dc.subjectAffinity-based profiling
dc.subjectAspartic proteases
dc.subjectEnzymes
dc.subjectPhotolabile probe
dc.subjectProteomics
dc.typeArticle
dc.contributor.departmentCHEMISTRY
dc.description.doi10.1016/j.tetlet.2005.04.015
dc.description.sourcetitleTetrahedron Letters
dc.description.volume46
dc.description.issue23
dc.description.page4053-4056
dc.description.codenTELEA
dc.identifier.isiut000229484600024
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