Zobrazeno 1 - 10 of 10 pro vyhledávání: '"Amy E. McGrath"'
1
Genetic Encoding of para-Pentafluorosulfanyl Phenylalanine: A Highly Hydrophobic and Strongly Electronegative Group for Stable Protein Interactions
Autor: Gottfried Otting, Adarshi P. Welegedara, Haocheng Qianzhu, Mithun C. Mahawaththa, Nicholas E. Dixon, Amy E. McGrath, Thomas Huber, Holly Williamson
Publikováno v: Journal of the American Chemical Society. 142:17277-17281
SF5Phe, para-pentafluorosulfanyl phenylalanine, is an unnatural amino acid with extreme physicochemical properties, which is stable in physiological conditions. Here we present newly developed aminoacyl-tRNA synthetases that enable genetic encoding o
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2a754766a97b2a6952213f950eab94dc
https://doi.org/10.1021/jacs.0c07976
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2
Single-molecule live-cell imaging reveals RecB-dependent function of DNA polymerase IV in double strand break repair
Autor: Myron F. Goodman, Antoine M. van Oijen, Andrew Robinson, Phuong Pham, Roger Woodgate, Michael M. Cox, Megan E. Cherry, Slobodan Jergic, John P. McDonald, Amy E. McGrath, Yvonne Hellmich, Steven T. Bruckbauer, Camille Henry, Harshad Ghodke, Matthew L Ritger, Elizabeth A. Wood, Sarah S. Henrikus
Publikováno v: Nucleic Acids Research
Several functions have been proposed for the Escherichia coli DNA polymerase IV (pol IV). Although much research has focused on a potential role for pol IV in assisting pol III replisomes in the bypass of lesions, pol IV is rarely found at the replic
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d48cb406560110ff8a1ecd452c27e612
https://pubmed.ncbi.nlm.nih.gov/32687193
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3
Modulation of DNA polymerase IV activity by UmuD and RecA* observed by single-molecule time-lapse microscopy
Autor: Amy E. McGrath, M. L. Ritger, Sarah S. Henrikus, Andrew Robinson, Michael M. Cox, Slobodan Jergic, Myron F. Goodman, van Oijen Am, P. T. Pham, Harshad Ghodke, Elizabeth A. Wood
DNA polymerase IV (pol IV) is expressed at increased levels inEscherichia colicells suffering high levels of DNA damage. In a recent single-molecule imaging study, we demonstrated that elevating the pol IV concentration is not sufficient to provide a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a4a70be32afc3758540db826b235ec9
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4
Crystal structures and biochemical characterization of DNA sliding clamps from three Gram-negative bacterial pathogens
Autor: Alexander P Martyn, Fay E. Dawes, Aaron J. Oakley, Nicholas E. Dixon, Jennifer L. Beck, Amy E. McGrath, Michael J. Kelso, Louise R. Whittell
Publikováno v: Journal of structural biology. 204(3)
Bacterial sliding clamps bind to DNA and act as protein-protein interaction hubs for several proteins involved in DNA replication and repair. The partner proteins all bind to a common pocket on sliding clamps via conserved linear peptide sequence mot
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19e420cd14dcad18736a1f76c6d17241
https://pubmed.ncbi.nlm.nih.gov/31097372
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5
Rational Design of a 3
Autor: Kate L, Wegener, Amy E, McGrath, Nicholas E, Dixon, Aaron J, Oakley, Denis B, Scanlon, Andrew D, Abell, John B, Bruning
Publikováno v: Chemistry (Weinheim an der Bergstrasse, Germany). 24(44)
The human sliding clamp (PCNA) controls access to DNA for many proteins involved in DNA replication and repair. Proteins are recruited to the PCNA surface by means of a short, conserved peptide motif known as the PCNA-interacting protein box (PIP-box
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c8bfc8d97ee88568487d07e4bd99c1ba
https://pubmed.ncbi.nlm.nih.gov/29917264
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