Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Roslin J, Adamson"'
Publikováno v:
Free Radical Biology and Medicine. 204:215-225
Autor:
Belinda Faust, Aldons J. Lusis, Karthickeyan Chella Krishnan, Laura Nocito, Shi Su, Mayuko Segawa, Maria E. Zoghbi, Melissa Martinez, Vincent Gutierrez, Jeff Abramson, Elisabeth P. Carpenter, Roslin J. Adamson, C.A. Shintre, Michaela Veliova, Andrea L. Hevener, Dane M. Wolf, Raffi Gharakhanian, Marc Liesa, Margaret R. Young, Jennifer Ngo, Thorsten Althoff, Kiana Mahdaviani, Michael Shum, Alexandra D. Saxberg, Linsey Stiles
Publikováno v:
Sci Transl Med
Although the role of hydrophilic antioxidants in the development of hepatic insulin resistance and nonalcoholic fatty liver disease has been well studied, the role of lipophilic antioxidants remains poorly characterized. A known lipophilic hydrogen p
Autor:
Roslin J. Adamson, Anthony Watts, Helen Attrill, Robert J.C. Gilbert, Alan D. Goddard, Andrew J. Turberfield, Daniele N. Selmi
Publikováno v:
Nano Letters. 11:657-660
Single-particle electron cryomicroscopy permits structural characterization of noncrystalline protein samples, but throughput is limited by problems associated with sample preparation and image processing. Three-dimensional density maps are reconstru
Autor:
Alan D, Goddard, Patricia M, Dijkman, Roslin J, Adamson, Rosana Inácio, dos Reis, Anthony, Watts
Publikováno v:
Methods in enzymology. 556
Membrane proteins are the gatekeepers to the cell and are essential to the function of all cells, controlling the flow of molecules and information across the cell membrane. Much effort has been put into the development of systems for studying membra
Membrane proteins are the gatekeepers to the cell and are essential to the function of all cells, controlling the flow of molecules and information across the cell membrane. Much effort has been put into the development of systems for studying membra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6470fd46af543711a6bb1734f9e4885e
https://doi.org/10.1016/bs.mie.2015.01.004
https://doi.org/10.1016/bs.mie.2015.01.004
Autor:
Roslin J, Adamson, Anthony, Watts
Publikováno v:
Febs Letters
Highlights • Little is known of the kinetics of interactions between GPCRs and their signalling partners. • NTS1 binds Gαi1 and Gαs with affinities of 15 ± 6 nM and 31 ± 18 nM (SE), respectively. • This SPR assay may be applicable to multip
It has been widely demonstrated that G protein-coupled receptors (GPCRs) can form dimers both in vivo and in vitro, a process that has functional consequences. These receptor-receptor interactions take place within a phospholipid bilayer, yet, genera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5f9a79d47b971e7dc100f31cd98339f4
https://doi.org/10.1016/b978-0-12-408143-7.00018-9
https://doi.org/10.1016/b978-0-12-408143-7.00018-9
Autor:
Sylvia Fanucchi, Manuel A. Fernandes, Stoyan Stoychev, Heini W. Dirr, Ikechukwu Achilonu, Nishal Parbhoo, Roslin J. Adamson, Samantha Gildenhuys
Publikováno v:
Biochemistry. 50(32)
The canonical glutathione transferase (GST) fold found in many monomeric and dimeric proteins consists of two domains that differ in structure and conformational dynamics. However, no evidence exists that the two domains unfold/fold independently at
Autor:
Ikechukwu Achilonu, Jonathan Burke, Roslin J. Adamson, Manuel A. Fernandes, Samantha Gildenhuys, Sylvia Fanucchi, Heini W. Dirr, David Balchin
Publikováno v:
Biochimica et biophysica acta. 1804(12)
Cytosolic glutathione transferases (GSTs) are major detoxification enzymes in aerobes. Each subunit has two distinct domains and an active site consisting of a G-site for binding GSH and an H-site for an electrophilic substrate. While the active site
Publikováno v:
Biochemistry. 47(44)
CLIC proteins function as anion channels when their structures convert from a soluble form to an integral membrane form. While very little is known about the mechanism of the conversion process, channel formation and activity are highly pH-dependent.