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High-throughput identification of dominant negative polypeptides in yeast
Dominant negative polypeptides can inhibit protein function by binding to the wild type version or by titrating a ligand. Here, we use high-throughput sequencing of libraries composed of fragments of yeast genes to identify dominant negative polypeptides based on their depletion during cell growth....
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6555411/ https://www.ncbi.nlm.nih.gov/pubmed/30962621 http://dx.doi.org/10.1038/s41592-019-0368-0 |
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author | Dorrity, Michael W. Queitsch, Christine Fields, Stanley |
author_facet | Dorrity, Michael W. Queitsch, Christine Fields, Stanley |
author_sort | Dorrity, Michael W. |
collection | PubMed |
description | Dominant negative polypeptides can inhibit protein function by binding to the wild type version or by titrating a ligand. Here, we use high-throughput sequencing of libraries composed of fragments of yeast genes to identify dominant negative polypeptides based on their depletion during cell growth. The method can uncover numerous inhibitory polypeptides for a protein and thereby define these fragments with exquisite resolution, even pinpointing individual residues with critical functional roles. |
format | Online Article Text |
id | pubmed-6555411 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
record_format | MEDLINE/PubMed |
spelling | pubmed-65554112019-10-08 High-throughput identification of dominant negative polypeptides in yeast Dorrity, Michael W. Queitsch, Christine Fields, Stanley Nat Methods Article Dominant negative polypeptides can inhibit protein function by binding to the wild type version or by titrating a ligand. Here, we use high-throughput sequencing of libraries composed of fragments of yeast genes to identify dominant negative polypeptides based on their depletion during cell growth. The method can uncover numerous inhibitory polypeptides for a protein and thereby define these fragments with exquisite resolution, even pinpointing individual residues with critical functional roles. 2019-04-08 2019-05 /pmc/articles/PMC6555411/ /pubmed/30962621 http://dx.doi.org/10.1038/s41592-019-0368-0 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 Dorrity, Michael W. Queitsch, Christine Fields, Stanley High-throughput identification of dominant negative polypeptides in yeast |
title | High-throughput identification of dominant negative polypeptides in yeast |
title_full | High-throughput identification of dominant negative polypeptides in yeast |
title_fullStr | High-throughput identification of dominant negative polypeptides in yeast |
title_full_unstemmed | High-throughput identification of dominant negative polypeptides in yeast |
title_short | High-throughput identification of dominant negative polypeptides in yeast |
title_sort | high-throughput identification of dominant negative polypeptides in yeast |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6555411/ https://www.ncbi.nlm.nih.gov/pubmed/30962621 http://dx.doi.org/10.1038/s41592-019-0368-0 |
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