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Unnatural amino acids increase sensitivity and provide for the design of highly selective caspase su...

Unnatural amino acids increase sensitivity and provide for the design of highly selective caspase su...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4131180

Unnatural amino acids increase sensitivity and provide for the design of highly selective caspase substrates

About this item

Full title

Unnatural amino acids increase sensitivity and provide for the design of highly selective caspase substrates

Publisher

London: Nature Publishing Group UK

Journal title

Cell death and differentiation, 2014-09, Vol.21 (9), p.1482-1492

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Traditional combinatorial peptidyl substrate library approaches generally utilize natural amino acids, limiting the usefulness of this tool in generating selective substrates for proteases that share similar substrate specificity profiles. To address this limitation, we synthesized a Hybrid Combinatorial Substrate Library (HyCoSuL) with the general...

Alternative Titles

Full title

Unnatural amino acids increase sensitivity and provide for the design of highly selective caspase substrates

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4131180

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4131180

Other Identifiers

ISSN

1350-9047

E-ISSN

1476-5403

DOI

10.1038/cdd.2014.64

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