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pro vyhledávání: '"Samantha L. Taylor"'
Autor:
Samantha L. Taylor, Fabian Kurth, Mark J. Howard, Mark A. Schembri, Alastair G. McEwan, Nathan P. King, M. Pilar Argente, Begoña Heras, Gordon J. King, Maud E. S. Achard, Mark Shepherd
Publikováno v:
Antioxidants & Redox Signaling. 19:1494-1506
Aims: The prototypical protein disulfide bond (Dsb) formation and protein refolding pathways in the bacterial periplasm involving Dsb proteins have been most comprehensively defined in Escherichia coli. However, genomic analysis has revealed several
Publikováno v:
Mol. BioSyst.. 9:571-577
This review aims to illustrate that STD NMR is not simply a method for drug screening and discovery, but has qualitative and quantitative applications that can answer fundamental and applied biological and biomedical questions involving molecular int
Autor:
Samantha L. Taylor, Christopher M. Johnson, Michelle L. Rowe, Stephen E. J. Rigby, Martin J. Warren, Alan Scott, Andy Lawrence, Mark J. Howard, Richard W. Pickersgill, Michael A. Geeves
Publikováno v:
Bioscience Reports
Bioscience Reports, Vol 34, Iss 4, p e00120 (2014)
Bioscience Reports, Vol 34, Iss 4, p e00120 (2014)
Adenosylcobalamin, the coenzyme form of vitamin B12, is one Nature's most complex coenzyme whose de novo biogenesis proceeds along either an anaerobic or aerobic metabolic pathway. The aerobic synthesis involves reduction of the centrally chelated co
Autor:
Arefeh Seyedarabi, Jitka Waterman, Evelyne Deery, Michael A. Geeves, David G. Brown, Mark J. Howard, Andy Lawrence, Keith S. Wilson, Susanne Schroeder, Richard W. Pickersgill, Martin J. Warren, Samantha L. Taylor
Publikováno v:
Nature chemical biology
The biosynthesis of many vitamins and coenzymes has often proven difficult to elucidate owing to a combination of low abundance and kinetic lability of the pathway intermediates. Through a serial reconstruction of the cobalamin (vitamin B(12)) pathwa
Autor:
Samantha L. Taylor, Harriet Crawley-Snowdon, Mark J. Howard, Mark Shepherd, Richard A. Williamson, Jane L. Wagstaff, Michelle L. Rowe
Publikováno v:
Chemical communications (Cambridge, England)
NMR spectroscopy was used to measure reduction potentials of four redox proteins by following multiple (15)N HSQC protein resonances across a titration series using mixtures of oxidised and reduced glutathione. Results for PDI a, PDI ab and DsbA agre