Zobrazeno 1 - 10
of 44
pro vyhledávání: '"Gaye F. White"'
Autor:
Michael P. Norman, Marcus J. Edwards, Gaye F. White, Joshua A. J. Burton, Julea N. Butt, David J. Richardson, Ricardo O. Louro, Catarina M. Paquete, Thomas A. Clarke
Publikováno v:
mBio, Vol 14, Iss 1 (2023)
ABSTRACT Many bacteria of the genus Shewanella are facultative anaerobes able to reduce a broad range of soluble and insoluble substrates, including Fe(III) mineral oxides. Under anoxic conditions, the bacterium Shewanella oneidensis MR-1 uses a pori
Externí odkaz:
https://doaj.org/article/3ca985b053494e71b746ed11cbf4c2a4
Autor:
Américo G. Duarte, Teresa Catarino, Gaye F. White, Diana Lousa, Sinje Neukirchen, Cláudio M. Soares, Filipa L. Sousa, Thomas A. Clarke, Inês A. C. Pereira
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
The bacterial complex QrcABCD plays a key role in the bioenergetics of sulfate respiration. Here, Duarte et al. show that this complex is electrogenic, with protons and electrons required for quinone reduction being extracted from opposite sides of t
Externí odkaz:
https://doaj.org/article/6cf2dc0875e546638dde5e256a8f387b
Autor:
Filipa L. Sousa, Thomas A. Clarke, Cláudio M. Soares, Diana Lousa, Teresa Catarino, Inês A. C. Pereira, Gaye F. White, Sinje Neukirchen, Américo G. Duarte
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
Nature Communications
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Nature Communications
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
The bioenergetics of anaerobic metabolism frequently relies on redox loops performed by membrane complexes with substrate- and quinone-binding sites on opposite sides of the membrane. However, in sulfate respiration (a key process in the biogeochemic
Autor:
Kendall Baker, Andrew M. Riley, Andrew M. Hemmings, Stuart A. Rushworth, Barry V. L. Potter, Stephen J Mills, Gaye F. White, Charles A. Brearley, Hayley Whitfield
Publikováno v:
Journal of Medicinal Chemistry
Src homology 2 domain-containing inositol phosphate phosphatase 2 (SHIP2) is one of the 10 human inositol phosphate 5-phosphatases. One of its physiological functions is dephosphorylation of phosphatidylinositol 3,4,5-trisphosphate, PtdIns(3,4,5)P3.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4852afdda095678d6e72cb7f09619aca
https://doi.org/10.1021/acs.jmedchem.0c01944
https://doi.org/10.1021/acs.jmedchem.0c01944
Autor:
Charles A. Brearley, Andrew M. Riley, Barry V. L. Potter, Hayley Whitfield, Andrew M. Hemmings, Colleen Sprigg, Gaye F. White
Publikováno v:
Biochemical Journal
Inositol polyphosphates are ubiquitous molecular signals in metazoans, as are their pyrophosphorylated derivatives that bear a so-called ‘high-energy’ phosphoanhydride bond. A structural rationale is provided for the ability of Arabidopsis inosit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b97af12caa03ef2df78da5aa238a98b
https://ueaeprints.uea.ac.uk/id/eprint/75939/
https://ueaeprints.uea.ac.uk/id/eprint/75939/
Autor:
Stephen J Mills, Vasily S. Oganesyan, Gaye F. White, Christopher Prior, Kendall Baker, Hayley Whitfield, Barry V. L. Potter, Andrew M. Riley, Charles A. Brearley
Publikováno v:
ACS Medicinal Chemistry Letters
SHIP2 (SH2-domain containing inositol 5-phosphatase type 2) is a canonical 5-phosphatase, which, through its catalytic action on PtdInsP3, regulates the PI3K/Akt pathway and metabolic action of insulin. It is a drug target, but there is limited evide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61c1fdc0ff36cc06f913c1079aedc331
https://ueaeprints.uea.ac.uk/id/eprint/72808/
https://ueaeprints.uea.ac.uk/id/eprint/72808/
Publikováno v:
SSRN Electronic Journal.
A growing number of bacteria are recognised to conduct electrons across their cell envelope and yet molecular details of the mechanisms supporting this process remain unknown. Here we report the atomic structure of an outer membrane spanning protein
Autor:
Colin W J, Lockwood, Jessica H, van Wonderen, Marcus J, Edwards, Samuel E H, Piper, Gaye F, White, Simone, Newton-Payne, David J, Richardson, Thomas A, Clarke, Julea N, Butt
Publikováno v:
Methods in enzymology. 613
Certain bacterial species have a natural ability to exchange electrons with extracellular redox partners. This behavior allows coupling of catalytic transformations inside bacteria to complementary redox transformations of catalysts and electrodes ou
Autor:
Erwin Reisner, Gaye F. White, Thomas A. Clarke, David J. Richardson, Lars J. C. Jeuken, Colin W. J. Lockwood, Julea N. Butt, Ee Taek Hwang, Manuela A. Gross, Emma V. Ainsworth, Tsubasa Sakai
Publikováno v:
Chembiochem
The transfer of photoenergized electrons from extracellular photosensitizers across a bacterial cell envelope to drive intracellular chemical transformations represents an attractive way to harness nature's catalytic machinery for solar‐assisted ch
Publikováno v:
Cell
Summary A growing number of bacteria are recognized to conduct electrons across their cell envelope, and yet molecular details of the mechanisms supporting this process remain unknown. Here, we report the atomic structure of an outer membrane spannin