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PASTMUS: mapping functional elements at single amino acid resolution in human cells
Identification of functional elements for a protein of interest is important for achieving a mechanistic understanding. However, it remains cumbersome to assess each and every amino acid of a given protein in relevance to its functional significance. Here, we report a strategy, PArsing fragmented DN...
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| Published in: | Genome Biology 2019-12, Vol.20 (1), p.279-279, Article 279 |
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| Main Authors: | , , , , , , , , , |
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| cites | cdi_FETCH-LOGICAL-c661t-3b8fe9b2142fef45e584724b25ce673c224da632a74cc632f7e50898b487eca3 |
| container_end_page | 279 |
| container_issue | 1 |
| container_start_page | 279 |
| container_title | Genome Biology |
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| creator | Zhang, Xinyi Yue, Di Wang, Yinan Zhou, Yuexin Liu, Ying Qiu, Yeting Tian, Feng Yu, Ying Zhou, Zhuo Wei, Wensheng |
| description | Identification of functional elements for a protein of interest is important for achieving a mechanistic understanding. However, it remains cumbersome to assess each and every amino acid of a given protein in relevance to its functional significance. Here, we report a strategy, PArsing fragmented DNA Sequences from CRISPR Tiling MUtagenesis Screening (PASTMUS), which provides a streamlined workflow and a bioinformatics pipeline to identify critical amino acids of proteins in their native biological contexts. Using this approach, we map six proteins-three bacterial toxin receptors and three cancer drug targets, and acquire their corresponding functional maps at amino acid resolution. |
| doi_str_mv | 10.1186/s13059-019-1897-7 |
| format | article |
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However, it remains cumbersome to assess each and every amino acid of a given protein in relevance to its functional significance. Here, we report a strategy, PArsing fragmented DNA Sequences from CRISPR Tiling MUtagenesis Screening (PASTMUS), which provides a streamlined workflow and a bioinformatics pipeline to identify critical amino acids of proteins in their native biological contexts. Using this approach, we map six proteins-three bacterial toxin receptors and three cancer drug targets, and acquire their corresponding functional maps at amino acid resolution.</description><identifier>ISSN: 1474-760X</identifier><identifier>ISSN: 1474-7596</identifier><identifier>EISSN: 1474-760X</identifier><identifier>DOI: 10.1186/s13059-019-1897-7</identifier><identifier>PMID: 31842968</identifier><language>eng</language><publisher>England: BioMed Central</publisher><subject>Amino Acid Sequence ; Amino acids ; antineoplastic agents ; bacterial toxins ; Bioinformatics ; Cell Cycle Proteins - chemistry ; CRISPR ; Deoxyribonucleic acid ; DNA ; gene editing ; Genes ; Genomes ; Genotype & phenotype ; Heparin-binding EGF-like Growth Factor - chemistry ; Humans ; Method ; Mutagenesis ; Mutation ; neoplasms ; Nucleotide sequence ; nucleotide sequences ; Polo-Like Kinase 1 ; Protein Serine-Threonine Kinases - chemistry ; Proteins ; Proto-Oncogene Proteins - chemistry ; receptors ; screening ; Sequence Analysis, Protein - methods ; Structure-Activity Relationship</subject><ispartof>Genome Biology, 2019-12, Vol.20 (1), p.279-279, Article 279</ispartof><rights>2019. This work is licensed under http://creativecommons.org/licenses/by/4.0/ (the “License”). 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However, it remains cumbersome to assess each and every amino acid of a given protein in relevance to its functional significance. Here, we report a strategy, PArsing fragmented DNA Sequences from CRISPR Tiling MUtagenesis Screening (PASTMUS), which provides a streamlined workflow and a bioinformatics pipeline to identify critical amino acids of proteins in their native biological contexts. 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However, it remains cumbersome to assess each and every amino acid of a given protein in relevance to its functional significance. Here, we report a strategy, PArsing fragmented DNA Sequences from CRISPR Tiling MUtagenesis Screening (PASTMUS), which provides a streamlined workflow and a bioinformatics pipeline to identify critical amino acids of proteins in their native biological contexts. Using this approach, we map six proteins-three bacterial toxin receptors and three cancer drug targets, and acquire their corresponding functional maps at amino acid resolution.</abstract><cop>England</cop><pub>BioMed Central</pub><pmid>31842968</pmid><doi>10.1186/s13059-019-1897-7</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0002-8053-2423</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Genome Biology, 2019-12, Vol.20 (1), p.279-279, Article 279 |
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| source | Publicly Available Content Database; PubMed Central |
| subjects | Amino Acid Sequence Amino acids antineoplastic agents bacterial toxins Bioinformatics Cell Cycle Proteins - chemistry CRISPR Deoxyribonucleic acid DNA gene editing Genes Genomes Genotype & phenotype Heparin-binding EGF-like Growth Factor - chemistry Humans Method Mutagenesis Mutation neoplasms Nucleotide sequence nucleotide sequences Polo-Like Kinase 1 Protein Serine-Threonine Kinases - chemistry Proteins Proto-Oncogene Proteins - chemistry receptors screening Sequence Analysis, Protein - methods Structure-Activity Relationship |
| title | PASTMUS: mapping functional elements at single amino acid resolution in human cells |
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