A cysteine-less and ultra-fast split intein rationally engineered from being aggregation-prone to hi...
A cysteine-less and ultra-fast split intein rationally engineered from being aggregation-prone to highly efficient in protein trans-splicing
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Publisher
London: Nature Publishing Group UK
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Language
English
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Publication information
Publisher
London: Nature Publishing Group UK
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Scope and Contents
Contents
Split inteins catalyze protein
trans
-splicing by ligating their extein sequences while undergoing self-excision, enabling diverse protein modification applications. However, many purified split intein precursors exhibit partial or no splicing activity for unknown reasons. The Aes123 PolB1 intein, a representative of the rare cysteine-less sp...
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Full title
A cysteine-less and ultra-fast split intein rationally engineered from being aggregation-prone to highly efficient in protein trans-splicing
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TN_cdi_doaj_primary_oai_doaj_org_article_8140390d0be64f059eb69ccab84594b4
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_8140390d0be64f059eb69ccab84594b4
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-025-57596-x
