Zobrazeno 1 - 8
of 8
pro vyhledávání: '"John R. Bagu"'
Autor:
Leigh Willard, Pierre Lavigne, Brian D. Sykes, Robert F. Boyko, John R. Bagu, Charles F.B. Holmes
Publikováno v:
Protein Science. 9:252-264
The relationship between the structure of a free ligand in solution and the structure of its bound form in a complex is of great importance to the understanding of the energetics and mechanism of molecular recognition and complex formation. In this s
Autor:
S. F. Paul Man, Brian D. Sykes, Redwan Moqbel, Damon C. Mayes, Sorin Musat-Marcu, Paige Lacy, Erik J. Saude, John R. Bagu
Publikováno v:
Magnetic Resonance in Medicine. 52:807-814
Disorders of the respiratory system, such as cystic fibrosis (CF), involve the infiltration and activation of airway inflammatory cells, including neutrophils. This leads to the secretion of peroxidases, which react further with substrates in solutio
Autor:
David F. Lowry, John R. Bagu, Andrea G. Lindsey, David M. Wilson, Fayaz A. Khazi, David W. Hoyt
Publikováno v:
Journal of Molecular Biology. 329:311-322
Hydrogen bonded histidine-aspartate (His-Asp) pairs are critical constituents in several key enzymatic reactions. To date, the role that these pairs play in catalysis is best understood in serine and trypsin-like proteases, where structural and bioch
Publikováno v:
Journal of Biological Chemistry. 272:5087-5097
The hepatotoxic cyclic heptapeptide microcystins and cyclic pentapeptide nodularins are powerful liver tumor promoters and potent inhibitors of the catalytic subunits of protein phosphatase-1 and −2A (PP-1c and PP-2Ac). In marked contrast to microc
Publikováno v:
Canadian Journal of Botany. 71:174-182
A mutant (NL-51) of the unicellular green alga Chlamydomonas reinhardtii Dangeard isolated from a wild-type strain (137c+) was shown to be resistant to the bipyridilium herbicide paraquat at the concentration at which growth of the wild type was inhi
Autor:
Raymond J. Andersen, David Williams, Frank D. Sönnichsen, Brian D. Sykes, John R. Bagu, Charles F.B. Holmes
Publikováno v:
Nature Structural & Molecular Biology. 2:114-116
A comparison of the structures of two cyanobacterial toxins yields insights into how they may inhibit protein phosphatase-1 and -2A and why microcystins but not motuporin may covalently modify their protein phosphatase targets.
Publikováno v:
Biochemical and biophysical research communications. 270(2)
The catalytic cores of PP-1c and PP-2B (calcineurin) are structurally conserved. However, PP-2B is resistant to inhibition by toxins of the okadaic acid and cyclic peptide classes, while PP-1c is potently inhibited. Molecular docking of the structure
Autor:
Redwan Moqbel, Don D. Sin, Paul Man, Brian D. Sykes, Paige Lacy, John R. Bagu, Sorin Musat-Marcu, Melody Prodaniuk, Erik J. Saude
Publikováno v:
Journal of Allergy and Clinical Immunology. 109:S345-S345