Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Simon C. Allen"'
Autor:
Efstratia H. Vatzaki, K. Ravi Acharya, Simon C. Allen, Joseph Stackhouse, Steven A. Benner, Demetres D. Leonidas, Katrin Trautwein-Fritz
Publikováno v:
European Journal of Biochemistry. 260:176-182
A variant of bovine pancreatic ribonuclease A has been prepared with seven amino acid substitutions (Q55K, N62K, A64T, Y76K, S80R, E111G, N113K). These substitutions recreate in RNase A the basic surface found in bovine seminal RNase, a homologue of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24987f4d4dbb2ac4072e349fd31a7ae0
https://doi.org/10.1046/j.1432-1327.1999.00142.x
https://doi.org/10.1046/j.1432-1327.1999.00142.x
Autor:
Kathleen A. Palmer, Harold A. Scheraga, Robert Shapiro, Bert L. Vallee, Simon C. Allen, K. Ravi Acharya
Publikováno v:
Journal of Protein Chemistry. 13:649-658
The three-dimensional structure of human angiogenin has been determined by X-ray crystallography and is compared here with an earlier model which predicted its structure, based on the homology of angiogenin with bovine pancreatic ribonuclease A. Comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9ef2052bbe5ec6e1e07e94a383ce145
https://doi.org/10.1007/bf01890464
https://doi.org/10.1007/bf01890464
Publikováno v:
Proceedings of the National Academy of Sciences. 91:2915-2919
Angiogenin, a potent inducer of neovascularization, is the only angiogenic molecule known to exhibit ribonucleolytic activity. Its overall structure, as determined at 2.4 A, is similar to that of pancreatic ribonuclease A, but it differs markedly in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71a0916d03ea188321e6d73186264439
https://doi.org/10.1073/pnas.91.8.2915
https://doi.org/10.1073/pnas.91.8.2915
Purification, characterisation and mutagenesis of highly expressed recombinant yeast pyruvate kinase
Autor:
Linda A. Fothergill-Gilmore, Simon C. Allen, Teresa McNALLY, Hilary Muirhead, Toby H. L. Murcott
Publikováno v:
European journal of biochemistry. 198(2)
Recombinant yeast pyruvate kinase has been purified from a strain of Saccharomyces cerevisiae expressing the enzyme to very high levels. Expression was from a multicopy plasmid under the control of the yeast phosphoglycerate kinase promoter. The gene
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a7bc5b48b216d7f4382ada471d6f0e6
https://pubmed.ncbi.nlm.nih.gov/1645661
https://pubmed.ncbi.nlm.nih.gov/1645661