Zobrazeno 1 - 10
of 278
pro vyhledávání: '"R.J. Fletterick"'
Publikováno v:
Biochemistry. 34(7)
Histidine substrate specificity has been engineered into trypsin by creating metal binding sites for Ni2+ and Zn2+ ions. The sites bridge the substrate and enzyme on the leaving-group side of the scissile bond. Application of simple steric and geomet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31df28688cfaab734e4c8c1c6000b49e
https://pubmed.ncbi.nlm.nih.gov/7857928
https://pubmed.ncbi.nlm.nih.gov/7857928
Akademický článek
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Publikováno v:
Journal of Biological Chemistry. 262:1449-1455
Acarbose, a pseudotetrasaccharide with a conduritol ring at the nonreducing terminus, is a naturally occurring inhibitor of amylases. It is shown here to be an inhibitor of glycogen phosphorylase and to bind more tightly to the enzyme than the equiva
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d826c95ff286d7b4245d236263c9ca86
https://doi.org/10.1016/s0021-9258(19)75656-7
https://doi.org/10.1016/s0021-9258(19)75656-7
Publikováno v:
Journal of Biological Chemistry. 253:1290-1296
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::88ec93586a85425b421bb9144a355855
https://doi.org/10.1016/s0021-9258(17)38143-7
https://doi.org/10.1016/s0021-9258(17)38143-7
Publikováno v:
Journal of Biological Chemistry. 251:6142-6146
A model of the polypeptide backbone of the dimer of glycogen phosphorylase a (EC 2.4.1.1) was built from a 3 A resolution electron density map derived from x-ray diffraction analysis of native tetragonal crystals and two heavy atom isomorphous replac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::708231f952af0829fc2d700a7239794a
https://doi.org/10.1016/s0021-9258(17)33070-3
https://doi.org/10.1016/s0021-9258(17)33070-3
Autor:
R.J. Fletterick, Neil B. Madsen
Publikováno v:
Trends in Biochemical Sciences. 2:145-148
Glycogen phosphorylase, the archetypal allosteric enzyme, is also metabolically interconvertible between physiologically active and inactive forms in response to hormonal and nervous controls. The crystal structure of the a (active) form at 3.0 A res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a980bb0461fdf543588151d97b9d8990
https://doi.org/10.1016/0968-0004(77)90361-9
https://doi.org/10.1016/0968-0004(77)90361-9
Autor:
R.J. Fletterick, Stephen R. Sprang
Publikováno v:
Journal of Molecular Biology. 131:523-551
The structure of the glucose-inhibited form of glycogen phosphorylase a has been determined at a resolution of 2.5 A. With the aid of the primary sequence derived by Titani et al. (1977) for this enzyme, we have constructed an atomic model of the 97,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d862d8ebb2681b10464ff6d2fd7b00b
https://doi.org/10.1016/0022-2836(79)90006-8
https://doi.org/10.1016/0022-2836(79)90006-8
Publikováno v:
Biochemical and Biophysical Research Communications. 86:1044-1050
Three novel mercury derivatives bearing different electronic charges have been synthesized and used to prepare useful heavy atom derivatives of crystals of glycogen phosphorylase a . While exhibiting some common binding sites on the exterior of the m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7255ec539468e9ff1e726397ff18eecf
https://doi.org/10.1016/0006-291x(79)90222-5
https://doi.org/10.1016/0006-291x(79)90222-5
Publikováno v:
Journal of Biological Chemistry. 253:3343-3351
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a602b505feb6a3255bb3a4dfb4a70ef5
https://doi.org/10.1016/s0021-9258(17)40842-8
https://doi.org/10.1016/s0021-9258(17)40842-8
Autor:
R.J. Fletterick, Stephen R. Sprang
Publikováno v:
Biophysical Journal. (1):175-192
The contribution of intersubunit interactions to allosterically induced conformational changes in phosphorylase are considered. Phosphorylase a, Pa (phosphorylated at Ser-14), is significantly in the active (R) conformation, while phosphorylase b, Pb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e890b133d76023721f72c97867cecae