Zobrazeno 1 - 10
of 103
pro vyhledávání: '"A. M. Hounslow"'
Autor:
L. Milanesi, C. R. Trevitt, B. Whitehead, A. M. Hounslow, S. Tomas, L. L. P. Hosszu, C. A. Hunter, J. P. Waltho
Publikováno v:
Magnetic Resonance, Vol 2, Pp 629-642 (2021)
Using a combination of NMR and fluorescence measurements, we have investigated the structure and dynamics of the complexes formed between calcium-loaded calmodulin (CaM) and the potent breast cancer inhibitor idoxifene, a derivative of tamoxifen. Hig
Externí odkaz:
https://doaj.org/article/eb536940a86b4a8cb729724a9b268250
Publikováno v:
Biomolecular NMR Assignments. 16:247-251
Enterococcus faecalis is a major causative agent of hospital acquired infections. The ability of E. faecalis to evade the host immune system is essential during pathogenesis, which has been shown to be dependent on the complete separation of daughter
Publikováno v:
ACS Omega, Vol 1, Iss 4, Pp 669-679 (2016)
Externí odkaz:
https://doaj.org/article/b66d13d8313046149de176abd30a754e
Publikováno v:
Frontiers in Molecular Biosciences, Vol 5 (2018)
We have used NMR and computational methods to characterize the dynamics of the ribonuclease barnase over a wide range of timescales in free and inhibitor-bound states. Using temperature- and denaturant-dependent measurements of chemical shift, we sho
Externí odkaz:
https://doaj.org/article/36e10a5ca2514b99be6ec5e2bbc29727
Protein structures calculated using NMR data are less accurate and less well defined than they could be. Here we use the program ANSURR to show that this deficiency is at least in part due to a lack of hydrogen bond restraints. We then describe a pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42f4267301a0a980206103435c1c3c73
https://doi.org/10.2139/ssrn.4392150
https://doi.org/10.2139/ssrn.4392150
Autor:
Laszlo Luis Pereira Hosszu, Daljit Sangar, Mark Batchelor, Emmanuel Risse, Andrea M. Hounslow, Jonathan P. Waltho, John Collinge, Jan Bieschke
Prion diseases, a group of incurable, lethal neurodegenerative disorders of mammals including humans, are caused by prions, assemblies of misfolded host prion protein (PrP). The pathway of PrP misfolding is still unclear, though previous data indicat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7943559c2079282e34a026b2035ff433
https://doi.org/10.1101/2022.09.20.508729
https://doi.org/10.1101/2022.09.20.508729
Autor:
Laszlo L. P. Hosszu, Daljit Sangar, Mark Batchelor, Emmanuel Risse, Andrea M. Hounslow, John Collinge, Jonathan P. Waltho, Jan Bieschke
Publikováno v:
Journal of Molecular Biology. :168158
Autor:
Henry P. Wood, Nicola J. Baxter, F. Aaron Cruz-Navarrete, Clare R. Trevitt, Jonathan P. Waltho, Andrea M. Hounslow
Publikováno v:
Green Chemistry. 23:752-762
Manipulation of enzyme behaviour represents a sustainable technology that can be harnessed to enhance the production of valuable metabolites and chemical precursors. β-Glucose 1,6-bisphosphate (βG16BP) is a native reaction intermediate in the catal
Autor:
Angus J. Robertson, Andrew L. Lovering, Elżbieta Jagielska, Bartłomiej Salamaga, Luz S Gonzalez-Delgado, Stéphane Mesnage, Hannah Walters-Morgan, Michael P. Williamson, Izabela Sabała, Andrea M. Hounslow
Publikováno v:
Nature chemical biology
Lysostaphin is a bacteriolytic enzyme targeting peptidoglycan, the essential component of the bacterial cell envelope. It displays a very potent and specific activity towards staphylococci, including methicillin-resistant Staphylococcus aureus (MRSA)
Autor:
Nicola J. Baxter, Andrea M. Hounslow, Henry P. Wood, Jonathan P. Waltho, F. Aaron Cruz-Navarrete
Publikováno v:
Biomolecular Nmr Assignments
Cruz-Navarrete, F A, Baxter, N J, Wood, H P, Hounslow, A M & Waltho, J P 2019, ' 1H, 15N and 13C backbone resonance assignments of the P146A variant of β-phosphoglucomutase from Lactococcus lactis in its substrate-free form ', Biomolecular NMR Assignments . https://doi.org/10.1007/s12104-019-09904-y
Cruz-Navarrete, F A, Baxter, N J, Wood, H P, Hounslow, A M & Waltho, J P 2019, ' 1H, 15N and 13C backbone resonance assignments of the P146A variant of β-phosphoglucomutase from Lactococcus lactis in its substrate-free form ', Biomolecular NMR Assignments . https://doi.org/10.1007/s12104-019-09904-y
β-Phosphoglucomutase (βPGM) is a magnesium-dependent phosphoryl transfer enzyme that catalyses the reversible isomerisation of β-glucose 1-phosphate and glucose 6-phosphate, via two phosphoryl transfer steps and a β-glucose 1,6-bisphosphate inter