Zobrazeno 1 - 10
of 130
pro vyhledávání: '"Ronald W. Woodard"'
Autor:
Rekha G. Panchal, Vladislav A. Litosh, S. Ashraf Ahmed, Ronald W. Woodard, Todd M. Kijek, Joel A. Bozue
Publikováno v:
Analytical biochemistry. 622
Arabinose 5-phosphate isomerase (API) catalyzes the reversible isomerization of Ribulose 5-phosphate (Ru5P) to Arabinose 5-Phosphate (Ar5P) for the production of 3-deoxy-2-octulosonic acid 8-phosphate (KDO), a component of bacterial lipopolysaccharid
Publikováno v:
PLoS ONE, Vol 6, Iss 8, p e23231 (2011)
Lipopolysaccharide (LPS) is located on the surface of Gram-negative bacteria and is responsible for maintaining outer membrane stability, which is a prerequisite for cell survival. Furthermore, it represents an important barrier against hostile envir
Externí odkaz:
https://doaj.org/article/45058fedffa54cddafc403b8013a07f5
Autor:
Timothy C. Meredith, Uwe Mamat, Thomas Scior, Dominik Schwudke, Nicolas Gisch, Ursula Schombel, Gloria Komazin, Ronald W. Woodard, Michael Maybin
Publikováno v:
J Biol Chem
Lipopolysaccharide (LPS) from the Gram-negative bacterial outer membrane potently activates the human innate immune system. LPS is recognized by the Toll-like receptor 4/myeloid differentiation factor-2 (TLR4/MD2) complex, leading to the release of p
Publikováno v:
Journal of Bacteriology. 199
d -Arabinose-5-phosphate (A5P) isomerases (APIs) catalyze the interconversion of d -ribulose-5-phosphate and d -arabinose-5-phosphate. Various Gram-negative bacteria, such as the uropathogenic Escherichia coli strain CFT073, contain multiple API para
Publikováno v:
Journal of Bacteriology. 196:2861-2868
Arabinose-5-phosphate isomerases (APIs) catalyze the interconversion of d -ribulose-5-phosphate and d -arabinose-5-phosphate, the first step in the biosynthesis of 3-deoxy- d -manno-octulosonic acid (Kdo), an essential component of the lipopolysaccha
Publikováno v:
Applied and Environmental Microbiology. 79:4192-4198
Cutinase is a multifunctional esterase with potential industrial applications. In the present study, a truncated version of the extracellular Thermobifida fusca cutinase without a signal peptide (referred to as cutinase NS ) was heterologously expres
Publikováno v:
Applied Microbiology and Biotechnology. 97:6705-6713
Secretion of cytoplasmic expressed proteins into culture medium has significant commercial advantages in large-scale production of proteins. Our previous study demonstrated that the membrane permeability of Escherichia coli could be significantly imp
Autor:
Sonia Singh, Otto Holst, Ronald W. Woodard, Helgo Schmidt, Rolf Hilgenfeld, Guido Hansen, Buko Lindner, Jeroen R. Mesters, Koichi Fukase, Uwe Mamat, Anna Hanuszkiewicz
Publikováno v:
Proceedings of the National Academy of Sciences. 109:6253-6258
WaaA is a key enzyme in the biosynthesis of LPS, a critical component of the outer envelope of Gram-negative bacteria. Embedded in the cytoplasmic face of the inner membrane, WaaA catalyzes the transfer of 3-deoxy- d - manno -oct-2-ulosonic acid (Kdo
Autor:
Lily Zhou, Igor A. Shumilin, Vijayalakshmi Janakiraman, Ronald W. Woodard, Jing Wu, Robert H. Kretsinger, Ronald Bauerle
Publikováno v:
Bioorganic Chemistry. 40:79-86
The first enzyme in the shikimic acid biosynthetic pathway, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAH7PS), varies significantly in size and complexity in the bacteria and plants that express it. The DAH7PS from the archaebacterium Aer