Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Walter H. J. Ward"'
Publikováno v:
Journal of Histochemistry & Cytochemistry. 63:454-458
Cytochemical staining remains an efficient way of identifying females who are heterozygous for the X chromosome-linked glucose-6-phosphate dehydrogenase ( G6PD) gene. G6PD is highly polymorphic with certain alleles resulting in low intracellular G6PD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2674dc81b6f0166ee8ef3ac7ffcdcc5d
https://doi.org/10.1369/0022155415580594
https://doi.org/10.1369/0022155415580594
Autor:
Walter H. J. Ward
Publikováno v:
Kinase Drug Discovery ISBN: 9781849731744
There has been considerable mechanistic research on the inhibition of protein kinases, using a powerful combination of data on protein sequences, 3-D structures, binding and kinetics to yield insight, which not only helps to understand the biological
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6925e32f23e2694982a17e3d048cb5d2
https://doi.org/10.1039/9781849733557-00096
https://doi.org/10.1039/9781849733557-00096
Publikováno v:
Biochemistry. 26:4131-4138
Wild-type tyrosyl-tRNA synthetase (TyrTS) from Bacillus stearothermophilus is a symmetrical dimer. Four different heterodimeric enzymes have been produced by site-directed mutagenesis at the subunit interface so that the monomers are linked by a pote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dba02e4c21fa00128bad3a4162db037b
https://doi.org/10.1021/bi00387a058
https://doi.org/10.1021/bi00387a058
Autor:
Alan R. Fersht, Walter H. J. Ward
Publikováno v:
Biochemistry. 27:5525-5530
Tyrosyl-tRNA synthetase from Bacillus stearothermophilus is a classical example of an enzyme with half-of-the-sites activity. The enzyme crystallizes as a symmetrical dimer that is composed of identical subunits, each having a complete active site. I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0aaa807d336880e78fb96e3b734ad705
https://doi.org/10.1021/bi00415a021
https://doi.org/10.1021/bi00415a021
Autor:
Walter H. J. Ward
Publikováno v:
Trends in Biochemical Sciences. 12:28-31
Diphtheria toxin specifically catalyses inactivation of elongation factor-2causing inhibition of protein synthesis, so that uptake of a single molecule of toxin may kill any eukaryotic cell. Protein engineering of such powerful bacterial toxins could
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d4f7a3ebe277913f8165207d820d05c7
https://doi.org/10.1016/0968-0004(87)90013-2
https://doi.org/10.1016/0968-0004(87)90013-2
Publikováno v:
Journal of Biological Chemistry. 261:9576-9578
Heterodimers of tyrosyl-tRNA synthetase from Bacillus stearothermophilus have been produced by mutagenesis at the subunit interface. Oppositely charged groups have been engineered into the subunits so that they can form a complementary pair. Wild-typ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e9b35ce4cd870b88d6cca731eb8ae270
https://doi.org/10.1016/s0021-9258(18)67550-7
https://doi.org/10.1016/s0021-9258(18)67550-7
Autor:
Walter H. J. Ward, Alan R. Fersht
Publikováno v:
Biochemistry. 27(3)
The tyrosyl-tRNA synthetase from Bacillus stearothermophilus crystallizes as a symmetrical dimer with each subunit having a complete active site. The enzyme-substrate complexes, however, are known to be asymmetrical in solution because the enzyme exh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6504dd7f7ba68e5a52c6dc13a666235
https://pubmed.ncbi.nlm.nih.gov/3365365
https://pubmed.ncbi.nlm.nih.gov/3365365
Autor:
Walter H. J. Ward
Publikováno v:
Trends in Biochemical Sciences. 12:182
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b7199deb6081cbab8974627eb1ee770c
https://doi.org/10.1016/0968-0004(87)90088-0
https://doi.org/10.1016/0968-0004(87)90088-0