Zobrazeno 1 - 10
of 49
pro vyhledávání: '"Martin G. Montgomery"'
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:
Edgar Morales-Rios, Ian N. Watt, Qifeng Zhang, Shujing Ding, Ian M. Fearnley, Martin G. Montgomery, Michael J. O. Wakelam, John E. Walker
Publikováno v:
Open Biology, Vol 5, Iss 9 (2015)
The structures of F-ATPases have been determined predominantly with mitochondrial enzymes, but hitherto no F-ATPase has been crystallized intact. A high-resolution model of the bovine enzyme built up from separate sub-structures determined by X-ray c
Externí odkaz:
https://doaj.org/article/8d07d2071bff4f70952556789d5b0398
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
Autor:
Michael J. Runswick, John V. Bason, Martin G. Montgomery, Graham C. Robinson, Ian M. Fearnley, John E. Walker
Publikováno v:
Open Biology, Vol 3, Iss 2 (2013)
The mitochondrial F1-ATPase inhibitor protein, IF1, inhibits the hydrolytic, but not the synthetic activity of the F-ATP synthase, and requires the hydrolysis of ATP to form the inhibited complex. In this complex, the α-helical inhibitory region of
Externí odkaz:
https://doaj.org/article/cd035229ce724da68e175bd514bdacc5
The structure has been determined by electron cryomicroscopy of the adenosine triphosphate (ATP) synthase from Mycobacterium smegmatis . This analysis confirms features in a prior description of the structure of the enzyme, but it also describes othe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47f3f7d14e23094910b168c538fc856f
https://www.repository.cam.ac.uk/handle/1810/332375
https://www.repository.cam.ac.uk/handle/1810/332375
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance As the world tackles the COVID-19 pandemic, other widespread infectious diseases, including tuberculosis (TB), take their toll on humans, and those with TB are more likely to die from COVID-19 infection. Bedaquiline (BD), an anti-TB drug
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c733698659081615675662f967667fed
https://pubmed.ncbi.nlm.nih.gov/34782468
https://pubmed.ncbi.nlm.nih.gov/34782468
Autor:
Anna Zhou, Alexis Rohou, Daniel G Schep, John V Bason, Martin G Montgomery, John E Walker, Nikolaus Grigorieff, John L Rubinstein
Publikováno v:
eLife, Vol 4 (2015)
Adenosine triphosphate (ATP), the chemical energy currency of biology, is synthesized in eukaryotic cells primarily by the mitochondrial ATP synthase. ATP synthases operate by a rotary catalytic mechanism where proton translocation through the membra
Externí odkaz:
https://doaj.org/article/89a50ce12b3848248676e372296fa06c
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance Mitochondria are the powerhouses of eukaryotic cells. Pairs of molecular machines with a rotary action, called ATP synthase, are embedded in their inner membranes and produce adenosine triphosphate, ATP, the fuel of life. These dimers fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68b8cc1a9a6e38d3aa8348df85ba635b
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance The production of ATP in mitochondria requires the oxidation of energy rich compounds to generate a proton motive force (pmf), a chemical potential difference for protons across the inner membrane. This pmf powers the ATP synthase, a mol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70eec0f3d42314c7ccf546939cfa774a
https://pubmed.ncbi.nlm.nih.gov/33168734
https://pubmed.ncbi.nlm.nih.gov/33168734
SUMMARYThe ATP synthase complexes in mitochondria make the ATP required to sustain life by a rotary mechanism. Their membrane domains are embedded in the inner membranes of the organelle and they dimerize via interactions between their membrane domai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e474392935e60c15f9ca31b7407964c7
https://doi.org/10.1101/2020.09.18.303636
https://doi.org/10.1101/2020.09.18.303636