Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Roger Bone"'
Autor:
Raymond Baker, L. Frank, John R. Atack, M.R. Knowles, Howard B. Broughton, Roger Bone, Scott J. Pollack, James P. Springer, C.I. Ragan, S.R. Fletcher, George McAllister, S.A. Osborne
Publikováno v:
Biochemistry. 33:9460-9467
The structures of ternary complexes of human inositol monophosphatase with inhibitory Gd3+ and either D- or L-myo-inositol 1-phosphate have been determined to 2.2-2.3 A resolution using X-ray crystallography. Substrate and metal are bound identically
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aae4a1a69e6db015f78bfc04480f3838
https://doi.org/10.1021/bi00198a011
https://doi.org/10.1021/bi00198a011
Publikováno v:
Biochemistry. 33:9468-9476
The structure of inositol monophosphatase has been determined to 2.60 A resolution in complexes with Mn2+ and with Mn2+ and phosphate. In the Mn2+ complex, three metal cations and one Cl were bound in the active site on each of the two subunits of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d08fba0d5e9ffefe48d0d9c93ee92ce
https://doi.org/10.1021/bi00198a012
https://doi.org/10.1021/bi00198a012
Publikováno v:
Proceedings of the National Academy of Sciences. 89:10031-10035
Inositol monophosphatase (EC 3.1.3.25), the putative molecular site of action of lithium therapy for manic-depressive illness, plays a key role in the phosphatidylinositol signaling pathway by catalyzing the hydrolysis of inositol monophosphates. To
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75a4e96d91588ab768310970abe383d0
https://doi.org/10.1073/pnas.89.21.10031
https://doi.org/10.1073/pnas.89.21.10031
Publikováno v:
Biochemistry. 30:2263-2272
The structures of the complexes with alpha-lytic protease of both phosphorus stereoisomers of N-[(2S)-2-[[[(1R)-1-[N-[(tert-butyloxycarbonyl)-L-alanyl-L-alanyl- L-prolyl]amino]-2-methylpropyl]-phenoxyphosphinyl]oxy]propanoyl]- L-alanine methyl ester,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c04e141626b42cee8e15aecf8cbe6c04
https://doi.org/10.1021/bi00222a032
https://doi.org/10.1021/bi00222a032
Publikováno v:
Journal of the American Chemical Society. 113:9382-9384
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ab1cb1df25bfde285d71ece3d6f63b0f
https://doi.org/10.1021/ja00024a061
https://doi.org/10.1021/ja00024a061
Publikováno v:
Biochemistry. 30(43)
Binding pocket mutants of alpha-lytic protease (Met 192----Ala and Met 213----Ala) have been constructed recently in an effort to create a protease specific for Met just prior to the scissile bond. Instead, mutation resulted in proteases with extraor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a636bdd6884e7305340882b1f709582
https://pubmed.ncbi.nlm.nih.gov/1931963
https://pubmed.ncbi.nlm.nih.gov/1931963
Autor:
Roger Bone
Publikováno v:
Disease-a-Month. 36:131
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b99a9ade3d5bfd172d5f73da64b3f5db
https://doi.org/10.1016/0011-5029(90)90024-l
https://doi.org/10.1016/0011-5029(90)90024-l
Publikováno v:
Scopus-Elsevier
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b31880f8fd1025e62c5ceffac71493db
https://doi.org/10.1021/ja00343a044
https://doi.org/10.1021/ja00343a044
Autor:
Roger Bone, Richard Wolfenden
Publikováno v:
Journal of the American Chemical Society. 107:4772-4777
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a5b1719de797433e2c51ffd4e1d2326f
https://doi.org/10.1021/ja00302a028
https://doi.org/10.1021/ja00302a028
Publikováno v:
Biochemistry. 28:7600-7609
To better understand the structural basis of enzyme specificity, the structures of complexes formed between a-lytic protease, an extracellular serine protease of Lysobacter enzymogenes, and five inhibitory peptide boronic acids ( R2-boroX, where R2 i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a34dc0d85c37c6932bf1f80bf448fd4
https://doi.org/10.1021/bi00445a015
https://doi.org/10.1021/bi00445a015