J
Julian J. Adams
Researcher at St. Vincent's Institute of Medical Research
Publications - 19
Citations - 1443
Julian J. Adams is an academic researcher from St. Vincent's Institute of Medical Research. The author has contributed to research in topics: Ligand (biochemistry) & Amyloid precursor protein. The author has an hindex of 11, co-authored 19 publications receiving 1393 citations. Previous affiliations of Julian J. Adams include University of Canterbury.
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Journal ArticleDOI
AMP-activated protein kinase, super metabolic regulator.
Bruce E. Kemp,David Stapleton,Duncan J. Campbell,Zhi-Ping Chen,Sid Murthy,M. Walter,Archana Gupta,Julian J. Adams,Frosa Katsis,B.J. van Denderen,Ian G. Jennings,Tristan J. Iseli,Belinda J. Michell,Lee A. Witters +13 more
TL;DR: The AMP-activated protein kinase (AMPK) is a metabolic-stress-sensingprotein kinase that regulates metabolism in response to energy demand and supply by directly phosphorylating rate-limiting enzymes in metabolic pathways as well as controlling gene expression.
Journal ArticleDOI
Model for growth hormone receptor activation based on subunit rotation within a receptor dimer
Richard J. C. Brown,Julian J. Adams,Rebecca A. Pelekanos,Yu Wan,William J. McKinstry,Kathryn Palethorpe,Ruth M. Seeber,Thea A. Monks,Karin A. Eidne,Michael W. Parker,Michael J. Waters +10 more
TL;DR: It is shown that there is no substantial change in the crystal structure of the liganded and unliganded human GHR extracellular domain, and an activation mechanism involving a relative rotation of subunits within a dimeric receptor as a result of asymmetric placement of the receptor-binding sites on the ligand is proposed.
Journal ArticleDOI
Intrasteric control of AMPK via the γ1 subunit AMP allosteric regulatory site
Julian J. Adams,Zhi-Ping Chen,Bryce J. W. van Denderen,Craig J. Morton,Michael W. Parker,Lee A. Witters,David Stapleton,Bruce E. Kemp +7 more
TL;DR: It is proposed that ATP acts as an intrasteric inhibitor by bridging the α and γ subunits and that AMP functions to derepress AMPK activity.
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Nitrosylation of human glutathione transferase P1-1 with dinitrosyl diglutathionyl iron complex in vitro and in vivo
Eleonora Cesareo,Lorien J. Parker,Jens Z. Pedersen,Marzia Nuccetelli,A.P. Mazzetti,Anna Pastore,Giorgio Federici,Giorgio Federici,Anna Maria Caccuri,Giorgio Ricci,Julian J. Adams,Michael W. Parker,Mario Lo Bello +12 more
TL;DR: Electron paramagnetic resonance spectroscopy studies on intact Escherichia coli cells expressing the recombinant GST P1-1 enzyme indicate that bacterial cells, in response to NO treatment, are able to form the dinitrosyl diglutathionyl iron complex using intracellular iron and GSH.
Journal ArticleDOI
Structural Studies of the Alzheimer's Amyloid Precursor Protein Copper-binding Domain Reveal How it Binds Copper Ions
Geoffrey K-W Kong,Julian J. Adams,Hugh H. Harris,John F. Boas,Cyril C. Curtain,Cyril C. Curtain,Denise Galatis,Denise Galatis,Colin L. Masters,Colin L. Masters,Kevin J. Barnham,Kevin J. Barnham,William J. McKinstry,Roberto Cappai,Michael W. Parker +14 more
TL;DR: The atomic structures of apo CuBD from three crystal forms are described and found they have identical Cu-binding sites despite the different crystal lattices, providing a mechanism by which CuBD could readily transfer Cu ions to other proteins.