Zobrazeno 1 - 10
of 72
pro vyhledávání: '"John F, Eccleston"'
Autor:
Faith V. Mayer, Stephen R. Martin, David Carmena, Matthew J. Sanders, Bing Xiao, Rein Aasland, David Carling, Chun-Xia Jing, Steven Howell, Richard Heath, Peter Saiu, Elizabeth Underwood, Lesley F. Haire, John F. Eccleston, Steven J. Gamblin, Philip A. Walker
Publikováno v:
Nature
The heterotrimeric AMP-activated protein kinase (AMPK) has a key role in regulating cellular energy metabolism; in response to a fall in intracellular ATP levels it activates energy-producing pathways and inhibits energy-consuming processes. AMPK has
Publikováno v:
Translational Research. 156:55-67
In iron overload conditions, plasma contains non-transferrin bound iron species, collectively referred to as plasma NTBI. These include iron citrate species, some of which are protein bound. Because NTBI is taken into tissues susceptible to iron load
Autor:
Johan P. Turkenburg, John E. T. Corrie, Michael A. Ferenczi, Madeleine H. Moore, David R. Trentham, John F. Eccleston
Publikováno v:
Journal of Physical Organic Chemistry. 21:286-298
pH-dependent interconversion between ring and chain forms of sultams/sulfonamides derived from conjugates of sulforhodamines with amines, and the associated sulfonamide ionization, have been studied by a combination of equilibrium and kinetic methods
Autor:
Chun Jing, John F. Eccleston, Colin T. Davis, Stephen R. Martin, Philippe Leone, Fiona C. Leiper, Richard Heath, Peter Saiu, Bing Xiao, Lesley F. Haire, Philip A. Walker, David Carling, Steven J. Gamblin
Publikováno v:
Nature
Nature, 2007, 449 (7161), pp.496-500. ⟨10.1038/nature06161⟩
Nature, Nature Publishing Group, 2007, 449 (7161), pp.496-500. ⟨10.1038/nature06161⟩
Nature, 2007, 449 (7161), pp.496-500. ⟨10.1038/nature06161⟩
Nature, Nature Publishing Group, 2007, 449 (7161), pp.496-500. ⟨10.1038/nature06161⟩
AMP-activated protein kinase (AMPK) is a central regulator of energy homeostasis in mammals. This crystal structure of the trimeric regulatory fragment of mammalian AMPK reveals the modes of AMP and ATP binding. AMP-activated protein kinase (AMPK) re
Autor:
John F. Eccleston, Jeffrey J. Babon, William D. Morgan, James Feeney, Geoffrey Kelly, Anthony A. Holder
Publikováno v:
Molecular and Biochemical Parasitology. 153:31-40
Plasmodium vivax infection is the second most common cause of malaria throughout the world. Like other Plasmodium species, P. vivax has a large protein complex, MSP-1, located on the merozoite surface. The C-terminal MSP-1 sub-unit, MSP-1(42), is cle
Publikováno v:
Journal of Biological Chemistry. 281:8371-8378
Protein products of the suf operon are involved in iron-sulfur metabolism. SufC is an ATPase that can interact with SufB in the absence of nucleotide. We have studied the transient kinetics of the SufC ATPase mechanism using the fluorescent ATP analo
Publikováno v:
Biochemistry. 42:3956-3965
Individual rate constants have been determined for each step of the Ras.GTP hydrolysis mechanism, activated by neurofibromin. Fluorescence intensity and anisotropy stopped-flow measurements used the fluorescent GTP analogue, mantGTP (2'(3')-O-(N-meth
Autor:
John F. Eccleston, Colin T. Davis, John C. Croney, Kazuhiro Oiwa, David M. Jameson, Michael Anson
Publikováno v:
Biophysical Journal. 84(1):634-642
Ribose-modified highly-fluorescent sulfoindocyanine ATP and ADP analogs, 2′(3′)- O -Cy3-EDA-AT(D)P, with kinetics similar to AT(D)P, enable myosin and actomyosin ATPase enzymology with single substrate molecules. Stopped-flow studies recording bo
Autor:
John C. Croney, Michael J. Blackman, David M. Jameson, Geoff Kelly, John E. T. Corrie, John F. Eccleston
Publikováno v:
Biochemistry. 41:12244-12252
Activation of the proenzyme form of the malarial protease PfSUB-1 involves the autocatalytic cleavage of an Asp-Asn bond within the internal sequence motif (215)LVSADNIDIS(224). A synthetic decapeptide based on this sequence but with the N- and C-ter
Publikováno v:
Journal of Biological Chemistry. 276:41255-41262
Mog1 is a nuclear protein that interacts with Ran, the Ras family GTPase that confers directionality to nuclear import and export pathways. Deletion of MOG1 in Saccharomyces cerevisiae (Deltamog1) causes temperature-sensitive growth and defects in nu