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1دورية أكاديمية
المؤلفون: Wei Li Thong, Yingxin Zhang, Ying Zhuo, Katherine J. Robins, Joanna K. Fyans, Abigail J. Herbert, Brian J. C. Law, Jason Micklefield
المصدر: Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
مصطلحات موضوعية: Science
وصف الملف: electronic resource
Relation: https://doaj.org/toc/2041-1723
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المؤلفون: Jason Micklefield, Ying Zhuo, Katherine J Robins, Yingxin Zhang, Joanna K Fyans, Brian J. C. Law, Wei Li Thong, Abigail J Herbert
المصدر: Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
Thong, W L, Zhang, Y, Zhuo, Y, Robins, K J, Fyans, J K, Herbert, A J, Law, B J C & Micklefield, J 2021, ' Gene editing enables rapid engineering of complex antibiotic assembly lines ', Nature Communications, vol. 12, no. 1, 6872 . https://doi.org/10.1038/s41467-021-27139-1
Nature Communicationsمصطلحات موضوعية: CRISPR-Cas9 genome editing, Science, General Physics and Astronomy, Multienzyme complexes, Computational biology, Peptides, Cyclic, Article, General Biochemistry, Genetics and Molecular Biology, Peptides, Cyclic/biosynthesis, Lipopeptides, chemistry.chemical_compound, Protein Domains, Genome editing, Nonribosomal peptide, CRISPR-Associated Protein 9, Peptide Synthases, Gene knockout, Gene Editing, Gene Editing/methods, chemistry.chemical_classification, Multidisciplinary, Chemistry, Lipopeptide, Multienzyme Complexes/chemistry, General Chemistry, Lipopeptides/biosynthesis, Peptide Synthases/chemistry, Streptomyces, Anti-Bacterial Agents, Anti-Bacterial Agents/biosynthesis, Complementation, Mutation, Synthetic Biology, CRISPR-Cas Systems, Streptomyces/genetics
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المؤلفون: Sarah A. Shepherd, Anna-Winona Struck, Lu Shin Wong, Matthew R. Bennett, Jason Micklefield, Brian J. C. Law, Ying Zhuo
المصدر: Struck, A-W, Bennett, M, Shepherd, S, Law, B, Zhuo, Y, Wong, L S & Micklefield, J 2016, ' An Enzyme Cascade for Selective Modification of Tyrosine Residues in Structurally Diverse Peptides and Proteins. ', J. Am. Chem. Soc., vol. 138, pp. 3038–3045 . https://doi.org/10.1021/jacs.5b10928
مصطلحات موضوعية: 0301 basic medicine, Alkylation, Tyrosinase, Conjugated system, Catechol O-Methyltransferase, Hydroxylation, 010402 general chemistry, Peptides, Cyclic, 01 natural sciences, Biochemistry, Catalysis, Cofactor, Fungal Proteins, Levodopa, 03 medical and health sciences, chemistry.chemical_compound, Colloid and Surface Chemistry, Manchester Institute of Biotechnology, Moiety, chemistry.chemical_classification, biology, Monophenol Monooxygenase, Biomolecule, Proteins, General Chemistry, ResearchInstitutes_Networks_Beacons/manchester_institute_of_biotechnology, 0104 chemical sciences, 030104 developmental biology, Enzyme, chemistry, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, biology.protein, Tyrosine, Bioorthogonal chemistry, Agaricales, Peptides
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المؤلفون: Annabel C. Murphy, Peter F. Leadlay, Markiyan Samborskyy, Ying Zhuo, Brian J. C. Law, Daniel Francis, Yingxin Zhang, Michael Winn, Jason Micklefield, Lujing Ren
المصدر: Law, B, Zhuo, Y, Winn, M, Francis, D, Zhang, Y, Samborskyy, M, Murphy, A, Ren, L, Leadlay, P F & Micklefield, J 2018, ' A vitamin K-dependent carboxylase orthologue is involved in antibiotic biosynthesis ', Nature Catalysis, vol. 1, pp. 977-984 . https://doi.org/10.1038/s41929-018-0178-2
مصطلحات موضوعية: 0301 basic medicine, chemistry.chemical_classification, biology, Process Chemistry and Technology, 030106 microbiology, Streptomyces rimosus, Bioengineering, Malonic acid, biology.organism_classification, Biochemistry, Catalysis, Pyruvate carboxylase, Complementation, 03 medical and health sciences, chemistry.chemical_compound, 030104 developmental biology, Malonate, Enzyme, Biosynthesis, chemistry, Bacteria
وصف الملف: application/pdf
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb90ea95c5b43088e7553ecc5aab5c5f
https://pure.manchester.ac.uk/ws/files/81218400/41929_2018_178_Author.pdf -
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المؤلفون: Jason Micklefield, Ming-Cheng Wu, Barrie Wilkinson, Brian J. C. Law
المصدر: Current Opinion in Biotechnology. 23:931-940
مصطلحات موضوعية: Biological Products, Natural product, business.industry, Biomedical Engineering, Structural diversity, Bioengineering, Genomics, Computational biology, Biology, Protein Engineering, Biosynthetic Pathways, Biotechnology, chemistry.chemical_compound, chemistry, Multigene Family, Biological property, Humans, Microbial genome, business
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::565cc94fb23c9432d8d476217bedb029
https://doi.org/10.1016/j .copbio.2012.03.008 -
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المؤلفون: Peter F. Leadlay, Daniel Zabala, Jason Micklefield, Brian J. C. Law, Lijiang Song, Gregory L. Challis, Markiyan Samborskyy, Douglas M. Roberts, Joshua W. Cartwright
المصدر: Journal of the American Chemical Society. 138(13)
مصطلحات موضوعية: 0301 basic medicine, Proteasome Endopeptidase Complex, Cytochrome, Carboxy-Lyases, Dinitrocresols, Dehydrogenase, Flavin group, 010402 general chemistry, 01 natural sciences, Biochemistry, Catalysis, Hydroxylation, 03 medical and health sciences, chemistry.chemical_compound, Colloid and Surface Chemistry, Methionine, Biosynthesis, Cytochrome P-450 Enzyme System, Flavins, medicine, chemistry.chemical_classification, biology, Stereoisomerism, General Chemistry, Dipeptides, Monooxygenase, Streptomyces, 0104 chemical sciences, 030104 developmental biology, Enzyme, chemistry, Proteasome inhibitor, biology.protein, Proteasome Inhibitors, medicine.drug
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المؤلفون: Brian J. C. Law, Mark L. Thompson, Sarah A. Shepherd, Jason Micklefield, David Leys, Colin Levy, Matthew R. Bennett
المصدر: Law, B, Bennett, M, Thompson, M, Levy, C, Shepherd, S, Leys, D & Micklefield, J 2016, ' Effects of Active-Site Modification and Quaternary Structure on the Regioselectivity of Catechol-O-Methyltransferase. ', Angewandte Chemie (International ed. in English), vol. 55, pp. 2683–2687 . https://doi.org/10.1002/anie.201508287
Angewandte Chemie (International Ed. in English)مصطلحات موضوعية: biocatalysis, Stereochemistry, methyltransferases, Catechol O-Methyltransferase, Crystallography, X-Ray, 010402 general chemistry, 01 natural sciences, Catalysis, chemistry.chemical_compound, Catalytic Domain, Manchester Institute of Biotechnology, Transferase, Protein Structure, Quaternary, Catechol-O-methyl transferase, biology, 010405 organic chemistry, Chemistry, Communication, Vanillin, fungi, Active site, Regioselectivity, protein engineering, General Medicine, General Chemistry, ResearchInstitutes_Networks_Beacons/manchester_institute_of_biotechnology, Communications, Enzyme structure, 0104 chemical sciences, enzyme structure, Biocatalysis, regioselectivity, biology.protein, Protein quaternary structure
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cf92073cfbfa88d0da6342ae144f60b
https://doi.org/10.1002/anie.201508287 -
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المؤلفون: Jason Micklefield, Matthew R. Bennett, Brian J. C. Law, Anna-Winona Struck, Barrie Wilkinson
المصدر: Law, B, Struck, A-W, Bennett, M, Wilkinson, B & Micklefield, J 2015, ' Site-specific Bioalkylation of Rapamycin by the RapM 16-O-Methyltransferase ', Chemical Science, vol. 6, pp. 2885-2892 . https://doi.org/10.1039/C5SC00164A
مصطلحات موضوعية: chemistry.chemical_classification, Methyltransferase, Methionine, biology, Stereochemistry, General Chemistry, Methylation, Desmethyl, ResearchInstitutes_Networks_Beacons/manchester_institute_of_biotechnology, O-methyltransferase, chemistry.chemical_compound, Enzyme, chemistry, Biosynthesis, Biochemistry, Manchester Institute of Biotechnology, biology.protein, Transferase
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abcf33accb427604034ce60d0f4a7cfc
https://www.research.manchester.ac.uk/portal/en/publications/sitespecific-bioalkylation-of-rapamycin-by-the-rapm-16omethyltransferase(c47efd92-4e20-47cc-9104-194dff9a604a).html -
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المؤلفون: Brian J C, Law, Anna-Winona, Struck, Matthew R, Bennett, Barrie, Wilkinson, Jason, Micklefield
المصدر: Chemical Science
مصطلحات موضوعية: Chemistry
URL الوصول: https://explore.openaire.eu/search/publication?articleId=pmid________::5a5ec0f4d54b6fd5b496a9f25041d90e
https://pubmed.ncbi.nlm.nih.gov/29403635