Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Colin T, Davis"'
Autor:
Amy E. M. Beedle, Marc Mora, Colin T. Davis, Ambrosius P. Snijders, Guillaume Stirnemann, Sergi Garcia-Manyes
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
Mechanical force can facilitate thermodynamically unfavourable reactions. Here, the authors found that a stretching force can promote the SN2 cleavage of a protein disulfide bond by weak nucleophilic thiols, and that removing this force reverses the
Externí odkaz:
https://doaj.org/article/2cbe03a88f0e4c9ea6271c72af65ffeb
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d743b812b876a042c11128faabf0da0
https://doi.org/10.1038/nature06161
https://doi.org/10.1038/nature06161
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::85d0552fbfec40bf21c0799e7d09d39a
https://doi.org/10.1074/jbc.m513455200
https://doi.org/10.1074/jbc.m513455200
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d61dd9a9af575a95decbbbd1cc99f2d
Crystal Structure and Functional Analysis of Ras Binding to Its Effector Phosphoinositide 3-Kinase γ
Autor:
Edward H. Walker, Colin T. Davis, Olga Perisic, Len R. Stephens, Michael E. Pacold, John F. Eccleston, Phillip T. Hawkins, Roger L. Williams, Sabine Suire, Samuel Lara-Gonzalez
Publikováno v:
Europe PubMed Central
Ras activation of phosphoinositide 3-kinase (PI3K) is important for survival of transformed cells. We find that PI3Kgamma is strongly and directly activated by H-Ras G12V in vivo or by GTPgammaS-loaded H-Ras in vitro. We have determined a crystal str
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97a5a2572424778f65fc651771a201e2
https://doi.org/10.1016/s0092-8674(00)00196-3
https://doi.org/10.1016/s0092-8674(00)00196-3
Autor:
Joseph P. Albanesi, David M. Jameson, Barbara Barylko, Colin T. Davis, Derk D. Binns, John F. Eccleston, Michael K. Helms
Publikováno v:
Biochemistry. 39:7188-7196
Dynamin II is a 98 kDa protein (870 amino acids) required for the late stages of clathrin-mediated endocytosis. The GTPase activity of dynamin is required for its function in the budding stages of receptor-mediated endocytosis and synaptic vesicle re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eeaba31ff909ae8c516b83d79ec60f21
https://doi.org/10.1021/bi000033r
https://doi.org/10.1021/bi000033r
Autor:
John F. Eccleston, Theordore L. Hazlett, Bonnie S. Watson, Arthur E. Johnson, David M. Jameson, Colin T. Davis
Publikováno v:
Biochemistry. 34:7904-7912
The distance between the corner of the L-shaped transfer RNA and the GTP bound to elongation factor Tu (EF-Tu) in the aminoacyl-tRNA.EF-Tu.GTP ternary complex was measured using fluorescence energy transfer. The donor dye, fluorescein (Fl), was attac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::044db983c66bbce449d53a19da7ab149
https://doi.org/10.1021/bi00024a015
https://doi.org/10.1021/bi00024a015
Autor:
John F. Eccleston, Barbara Clough, Arsen Petrovic, Colin T. Davis, Kaveri Rangachari, Robert J.M. Wilson
Publikováno v:
Protein science : a publication of the Protein Society. 17(7)
Bacteria, as well as the plastid organelles of algae and higher plants, utilize proteins of the suf operon. These are involved in Fe-S cluster assembly, particularly under conditions of iron limitation or oxidative stress. Genetic experiments in some
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::91d5b89027c73f9248e59dc970010900
https://pubmed.ncbi.nlm.nih.gov/18413861
https://pubmed.ncbi.nlm.nih.gov/18413861
Publikováno v:
The Journal of biological chemistry. 281(13)
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9499d8c7c319ca3b1086eca3126b8bd7
https://pubmed.ncbi.nlm.nih.gov/16431905
https://pubmed.ncbi.nlm.nih.gov/16431905
Publikováno v:
European biophysics journal : EBJ. 31(4)
Dynamin is a large molecular weight GTPase. Amongst other biological processes, it is involved in clathrin-dependent endocytosis. It can self-assemble or assemble on other macromolecular structures that result in an increase in its GTPase activity. I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e507f9d925623f5872b47a5a8299d1c0
https://pubmed.ncbi.nlm.nih.gov/12122474
https://pubmed.ncbi.nlm.nih.gov/12122474