Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Ian N, Watt"'
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
Publikováno v:
Proceedings of the National Academy of Sciences. 116:10354-10359
The endogenous inhibitor of ATP synthase in mitochondria, called IF1, conserves cellular energy when the proton-motive force collapses by inhibiting ATP hydrolysis. Around neutrality, the 84-amino-acid bovine IF1 is thought to self-assemble into acti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7571bfd7d8a7f25e862bcf231332e07e
https://doi.org/10.1073/pnas.1903535116
https://doi.org/10.1073/pnas.1903535116
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 116(21)
The endogenous inhibitor of ATP synthase in mitochondria, called IF(1), conserves cellular energy when the proton-motive force collapses by inhibiting ATP hydrolysis. Around neutrality, the 84-amino-acid bovine IF(1) is thought to self-assemble into
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::98f453f7358cec28cf31173f1dd16bda
https://pubmed.ncbi.nlm.nih.gov/31064873
https://pubmed.ncbi.nlm.nih.gov/31064873
Publikováno v:
Proceedings of the National Academy of Sciences. 107:16823-16827
The catalytic domain of the F-ATPase in mitochondria protrudes into the matrix of the organelle, and is attached to the membrane domain by central and peripheral stalks. Energy for the synthesis of ATP from ADP and phosphate is provided by the transm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4453f44b30c8b0a8c23bde4de42baa2
https://doi.org/10.1073/pnas.1011099107
https://doi.org/10.1073/pnas.1011099107
Autor:
Michael J.O. Wakelam, Ian M. Fearnley, John E. Walker, Martin G. Montgomery, Ian N. Watt, Qifeng Zhang, Edgar Morales-Ríos, Shujing Ding
Publikováno v:
Open Biology, Vol 5, Iss 9 (2015)
'Open Biology ', vol: 5, pages: 150119-1-150119-9 (2015)
Open Biology
'Open Biology ', vol: 5, pages: 150119-1-150119-9 (2015)
Open Biology
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://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc8855ba6fc274759745418a28887d99
https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.150119
https://royalsocietypublishing.org/doi/pdf/10.1098/rsob.150119
Autor:
Marie C. Mikl, Wolf Reik, Cristina Rada, Mason Lu, Sarah L. Davies, Ian N. Watt, Michael S. Neuberger
Publikováno v:
Molecular and Cellular Biology. 25:7270-7277
The activation-induced deaminase/apolipoprotein B-editing catalytic subunit 1 (AID/APOBEC) family comprises four groups of proteins. Both AID, a lymphoid-specific DNA deaminase that triggers antibody diversification, and APOBEC2 (function unknown) ar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6be49c962b0a2fe9d23dd65d2467324
https://doi.org/10.1128/mcb.25.16.7270-7277.2005
https://doi.org/10.1128/mcb.25.16.7270-7277.2005
Autor:
Ian N. Watt, Gary R. McLean, Ole Olsen, John W. Schrader, John S. Babcook, P. Rathanaswami, Kevin B. Leslie
Publikováno v:
The Journal of Immunology. 174:4768-4778
Most primates, including humans, are chronically infected with cospecifically evolved, potentially pathogenic CMV. Abs that bind a 10-aa linear epitope (antigenic determinant 2 site 1) within the extracellular domain of human CMV glycoprotein B neutr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15611742b57e2374ffb27e0048a1e76f
https://doi.org/10.4049/jimmunol.174.8.4768
https://doi.org/10.4049/jimmunol.174.8.4768
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 109(29)
Mitochondrial ATP synthase is responsible for the synthesis of ATP, a universal energy currency in cells. Whereas X-ray crystallography has revealed the structure of the soluble region of the complex and the membrane-intrinsic c-subunits, little is k
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24d6ccb9e86eeb33711d8262d8988a0f
https://pubmed.ncbi.nlm.nih.gov/22753497
https://pubmed.ncbi.nlm.nih.gov/22753497
Autor:
Reuben S. Harris, Rupert Beale, Cristina Rada, Ian N. Watt, Michael S. Neuberger, Svend K. Petersen-Mahrt
Publikováno v:
Journal of molecular biology. 337(3)
To investigate the extent to which in vivo mutation spectra might reflect the intrinsic specificities of active mutators, genetic and biochemical assays were used to analyse the DNA target specificities of cytidine deaminases of the APOBEC family. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df0524d2bb17241b2268b559acfb37ae
https://pubmed.ncbi.nlm.nih.gov/15019779
https://pubmed.ncbi.nlm.nih.gov/15019779
Autor:
Michael H. Malim, Heather M Craig, Ann M. Sheehy, Ian N. Watt, Michael S. Neuberger, Kate N. Bishop, Svend K. Petersen-Mahrt, Reuben S. Harris
Publikováno v:
Cell. 116:629
CEM15/APOBEC3G is a cellular protein required for resistance to infection by virion infectivity factor (Vif)-deficient human immunodeficiency virus (HIV). Here, using a murine leukemia virus (MLV)-based system, we provide evidence that CEM15/APOBEC3G
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c4a4c565038ee76f1ae0c64dee62f82
https://doi.org/10.1016/s0092-8674(04)00163-1
https://doi.org/10.1016/s0092-8674(04)00163-1