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StaPLs: versatile genetically encoded modules for engineering drug-inducible proteins
Robust approaches for chemogenetic control of protein function would enable many biological applications. We describe stabilizable polypeptide linkages (StaPLs) based on hepatitis C virus protease. StaPLs undergo autoproteolysis to cleave proteins by default, while protease inhibitors prevent cleava...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6456726/ https://www.ncbi.nlm.nih.gov/pubmed/29967496 http://dx.doi.org/10.1038/s41592-018-0041-z |
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author | Jacobs, Conor L. Badiee, Ryan K. Lin, Michael Z. |
author_facet | Jacobs, Conor L. Badiee, Ryan K. Lin, Michael Z. |
author_sort | Jacobs, Conor L. |
collection | PubMed |
description | Robust approaches for chemogenetic control of protein function would enable many biological applications. We describe stabilizable polypeptide linkages (StaPLs) based on hepatitis C virus protease. StaPLs undergo autoproteolysis to cleave proteins by default, while protease inhibitors prevent cleavage and preserve protein function. We created StaPLs responsive to different clinically approved drugs to bidirectionally control transcription with zinc-finger-based effectors, and used StaPLs to create single-chain drug-stabilizable variants of CRISPR/Cas9 and caspase-9. |
format | Online Article Text |
id | pubmed-6456726 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
record_format | MEDLINE/PubMed |
spelling | pubmed-64567262019-04-10 StaPLs: versatile genetically encoded modules for engineering drug-inducible proteins Jacobs, Conor L. Badiee, Ryan K. Lin, Michael Z. Nat Methods Article Robust approaches for chemogenetic control of protein function would enable many biological applications. We describe stabilizable polypeptide linkages (StaPLs) based on hepatitis C virus protease. StaPLs undergo autoproteolysis to cleave proteins by default, while protease inhibitors prevent cleavage and preserve protein function. We created StaPLs responsive to different clinically approved drugs to bidirectionally control transcription with zinc-finger-based effectors, and used StaPLs to create single-chain drug-stabilizable variants of CRISPR/Cas9 and caspase-9. 2018-07-02 2018-07 /pmc/articles/PMC6456726/ /pubmed/29967496 http://dx.doi.org/10.1038/s41592-018-0041-z Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Jacobs, Conor L. Badiee, Ryan K. Lin, Michael Z. StaPLs: versatile genetically encoded modules for engineering drug-inducible proteins |
title | StaPLs: versatile genetically encoded modules for engineering drug-inducible proteins |
title_full | StaPLs: versatile genetically encoded modules for engineering drug-inducible proteins |
title_fullStr | StaPLs: versatile genetically encoded modules for engineering drug-inducible proteins |
title_full_unstemmed | StaPLs: versatile genetically encoded modules for engineering drug-inducible proteins |
title_short | StaPLs: versatile genetically encoded modules for engineering drug-inducible proteins |
title_sort | stapls: versatile genetically encoded modules for engineering drug-inducible proteins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6456726/ https://www.ncbi.nlm.nih.gov/pubmed/29967496 http://dx.doi.org/10.1038/s41592-018-0041-z |
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