Zobrazeno 1 - 10
of 113
pro vyhledávání: '"G. W. Leslie"'
Autor:
Jessica Petri, Yoshio Nakatani, Martin G. Montgomery, Scott A. Ferguson, David Aragão, Andrew G. W. Leslie, Adam Heikal, John E. Walker, Gregory M. Cook
Publikováno v:
Open Biology, Vol 9, Iss 6 (2019)
The crystal structure of the F1-catalytic domain of the adenosine triphosphate (ATP) synthase has been determined from the pathogenic anaerobic bacterium Fusobacterium nucleatum. The enzyme can hydrolyse ATP but is partially inhibited. The structure
Externí odkaz:
https://doaj.org/article/d928d5fda41b4803a6e3d06fc8cd121b
Autor:
Eugene Krissinel, Andrey A. Lebedev, Ville Uski, Charles B. Ballard, Ronan M. Keegan, Oleg Kovalevskiy, Robert A. Nicholls, Navraj S. Pannu, Pavol Skubák, John Berrisford, Maria Fando, Bernhard Lohkamp, Marcin Wojdyr, Adam J. Simpkin, Jens M. H. Thomas, Christopher Oliver, Clemens Vonrhein, Grzegorz Chojnowski, Arnaud Basle, Andrew Purkiss, Michail N. Isupov, Stuart McNicholas, Edward Lowe, Josep Triviño, Kevin Cowtan, Jon Agirre, Daniel J. Rigden, Isabel Uson, Victor Lamzin, Ivo Tews, Gerard Bricogne, Andrew G. W. Leslie, David G. Brown
Nowadays, progress in the determination of three-dimensional macromolecular structures from diffraction images is achieved partly at the cost of increasing data volumes. This is due to the deployment of modern high-speed, high-resolution detectors, t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70211be538eb43722afb9f6169aea790
https://eprints.soton.ac.uk/471374/
https://eprints.soton.ac.uk/471374/
Publikováno v:
Science. 364:775-778
A GPCR seen in the active state G protein–coupled receptors (GPCRs) are exceptionally good targets for drug development. Warne et al. describe four crystal structures of complexes of a GPCR—the β1-adrenergic receptor—in its active state. They
Autor:
Jennifer L Miller-Gallacher, Rony Nehmé, Tony Warne, Patricia C Edwards, Gebhard F X Schertler, Andrew G W Leslie, Christopher G Tate
Publikováno v:
PLoS ONE, Vol 9, Iss 3, p e92727 (2014)
The β1-adrenoceptor (β1AR) is a G protein-coupled receptor (GPCR) that is activated by the endogenous agonists adrenaline and noradrenaline. We have determined the structure of an ultra-thermostable β1AR mutant bound to the weak partial agonist cy
Externí odkaz:
https://doaj.org/article/50b41481c95544ee93db8f60e8bb5d68
Autor:
Graham C. Robinson, John V. Bason, Martin G. Montgomery, Ian M. Fearnley, David M. Mueller, Andrew G. W. Leslie, John E. Walker
Publikováno v:
Open Biology, Vol 3, Iss 2 (2013)
The structure of F1-ATPase from Saccharomyces cerevisiae inhibited by the yeast IF1 has been determined at 2.5 Å resolution. The inhibitory region of IF1 from residues 1 to 36 is entrapped between the C-terminal domains of the αDP- and βDP-subunit
Externí odkaz:
https://doaj.org/article/786b3de32e564d7ca22815d4b8b27ec7
Publikováno v:
PLoS ONE, Vol 8, Iss 8, p e70892 (2013)
Thermophilic DNA polymerases of the polB family are of great importance in biotechnological applications including high-fidelity PCR. Of particular interest is the relative promiscuity of engineered versions of the exo- form of polymerases from the T
Externí odkaz:
https://doaj.org/article/daad31c361ba4c1d978eee1c78aa59e2
Autor:
Jessica, Petri, Yoshio, Nakatani, Martin G, Montgomery, Scott A, Ferguson, David, Aragão, Andrew G W, Leslie, Adam, Heikal, John E, Walker, Gregory M, Cook
Publikováno v:
Open Biology
The crystal structure of the F1-catalytic domain of the adenosine triphosphate (ATP) synthase has been determined from the pathogenic anaerobic bacterium Fusobacterium nucleatum. The enzyme can hydrolyse ATP but is partially inhibited. The structure
Autor:
Gregory M. Cook, Alice Tianbu Zhang, Andrew G. W. Leslie, Martin G. Montgomery, John E. Walker
The crystal structure of the F 1 -catalytic domain of the adenosine triphosphate (ATP) synthase has been determined from Mycobacterium smegmatis which hydrolyzes ATP very poorly. The structure of the α 3 β 3 -component of the catalytic domain is si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e0287b897e91ee901c1b58f752243c7
https://europepmc.org/articles/PMC6410841/
https://europepmc.org/articles/PMC6410841/
Autor:
Andrew G. W. Leslie, John E. Walker, Gregory M. Cook, Scott A. Ferguson, Martin G. Montgomery
Publikováno v:
'Proceedings of the National Academy of Sciences of the USA ', vol: 113, pages: 10860-10865 (2016)
The crystal structure has been determined of the F1-catalytic domain of the F-ATPase from Caldalkalibacillus thermarum, which hydrolyzes adenosine triphosphate (ATP) poorly. It is very similar to those of active mitochondrial and bacterial F1-ATPases
Publikováno v:
Nature
An engineered G protein is used to bind to and stabilize the active conformation of the adenosine A2A receptor, enabling the acquisition of an X-ray crystal structure of this GPCR in an active state. G-protein-coupled receptors (GPCRs) are essential