Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Ashley J. Winter"'
Autor:
Ashley J. Winter, Matthew T. Rowe, Angus N. M. Weir, Nahida Akter, Sbusisiwe Z. Mbatha, Paul D. Walker, Christopher Williams, Zhongshu Song, Paul R. Race, Christine L. Willis, Matthew P. Crump
Publikováno v:
Winter, A J, Rowe, M T, Weir, A N M, Akter, N, Mbatha, S Z, Walker, P D, Williams, C, Song, Z, Race, P R, Willis, C L & Crump, M P 2022, ' Programmed Iteration Controls the Assembly of the Nonanoic Acid Side Chain of the Antibiotic Mupirocin ', Angewandte Chemie-International Edition, vol. 61, no. 50, e202212393 . https://doi.org/10.1002/anie.202212393
Mupirocin is a clinically important antibiotic produced by Pseudomonas fluorescens NCIMB 10586 that is assembled by a complex trans-AT polyketide synthase. The polyketide fragment, monic acid, is esterified by a 9-hydroxynonanoic acid (9HN) side chai
Autor:
Nahida Akter, Matthew T. Rowe, Ashley J. Winter, Christine L. Willis, Christopher Williams, Matthew P. Crump, Thomas J. Simpson, Paul R. Race, Zhongshu Song, Angus N M Weir, Luoyi Wang, Paul D. Walker
Publikováno v:
Walker, P D, Rowe, M T, Winter, A J, Weir, A N M, Akter, N, Wang, L, Race, P R, Williams, C, Song, Z, Simpson, T J, Willis, C L & Crump, M P 2020, ' A Priming Cassette Generates Hydroxylated Acyl Starter Units in Mupirocin and Thiomarinol Biosynthesis ', ACS Chemical Biology, vol. 2020 . https://doi.org/10.1021/acschembio.9b00969
Mupirocin, a commercially available antibiotic produced by Pseudomonas fluorescens NCIMB 10586, and thiomarinol, isolated from the marine bacterium Pseudoalteromonas sp. SANK 73390, both consist of a polyketide-derived monic acid homologue esterified
Autor:
Thitapa Thongkawphueak, Ashley J. Winter, Christopher Williams, Siriwat Soontaranon, Dominic J. Campopiano, Pakorn Wattana-Amorn, Matthew P. Crump, Hannah J. Maple, Chonthicha Kaewhan
Publikováno v:
Biochemistry. 60(3)
The acyl carrier protein (ACP) is an indispensable component of both fatty acid and polyketide synthases and is primarily responsible for delivering acyl intermediates to enzymatic partners. At present, increasing numbers of multidomain ACPs have bee
Autor:
Pakorn Wattana-Amorn, Ashley J. Winter, Waraporn Bunnak, Colin M. Lazarus, Matthew P. Crump, Paul R. Race
Publikováno v:
Bunnak, W, Winter, A J, Lazarus, C M, Crump, M P, Race, P R & Wattana-Amorn, P 2020, ' SAXS reveals highly flexible interdomain linkers of tandem acyl carrier protein–thioesterase domains from a fungal non-reducing polyketide synthase ', FEBS Letters . https://doi.org/10.1002/1873-3468.13954
Menisporopsin A is a fungal bioactive macrocyclic polylactone, the biosynthesis of which requires only reducing (R) and nonreducing (NR) polyketide synthases (PKSs) to guide a series of esterification and cyclolactonization reactions. There is no str
Autor:
Mariya Gromova, Ashley J. Winter, Philip Marsh, Richard W. Titball, Matthew P. Crump, Nicholas J. Harmer, Michail N. Isupov, Hannah Crocker, Christopher Williams, Oliver J Wilkinson, Mark S. Dillingham
Publikováno v:
Winter, A J, Williams, C, Isupov, M N, Crocker, H, Gromova, M, Marsh, P, Wilkinson, O J, Dillingham, M S, Harmer, N J, Titball, R W & Crump, M P 2018, ' The molecular basis of protein toxin HicA– dependent binding of the protein antitoxin HicB to DNA ', Journal of Biological Chemistry, vol. 293, no. 50, pp. 19429-19440 . https://doi.org/10.1074/jbc.RA118.005173
Toxin–antitoxin (TA) systems are present in many bacteria and play important roles in bacterial growth, physiology, and pathogenicity. Those that are best studied are the type II TA systems, in which both toxins and antitoxins are proteins. The Hic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50a99005831f1e01750c51836133ea6b
https://research-information.bris.ac.uk/ws/files/184673435/Winters_Crump_HicAB_R2combined_181018.pdf
https://research-information.bris.ac.uk/ws/files/184673435/Winters_Crump_HicAB_R2combined_181018.pdf
Autor:
Hans-Jürgen Hoppe, Ryan Nicholls, Karl Harlos, Imre Berger, Christopher Williams, Matthew P. Crump, Alice J. Bochel, Airlie J. McCoy, E. Yvonne Jones, A. Bassim Hassan, Ashley J. Winter
Publikováno v:
Bochel, A J, Williams, C, McCoy, A J, Hoppe, H-J, Winter, A J, Nicholls, R D, Berger, I & Crump, M P 2020, ' Structure of the Human Cation-Independent Mannose 6-Phosphate/IGF2 Receptor Domains 7-11 Uncovers the Mannose 6-Phosphate Binding Site of Domain 9 ', Structure . https://doi.org/10.1016/j.str.2020.08.002
Summary The cation-independent mannose 6-phosphate (M6P)/Insulin-like growth factor-2 receptor (CI-MPR/IGF2R) is an ∼300 kDa transmembrane protein responsible for trafficking M6P-tagged lysosomal hydrolases and internalizing IGF2. The extracellular