S
Simon H. J. Brown
Researcher at University of Wollongong
Publications - 64
Citations - 2535
Simon H. J. Brown is an academic researcher from University of Wollongong. The author has contributed to research in topics: Protein subunit & Insulin resistance. The author has an hindex of 27, co-authored 61 publications receiving 2147 citations. Previous affiliations of Simon H. J. Brown include RMIT University & Brien Holden Vision Institute.
Papers
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Journal ArticleDOI
Mouse strain-dependent variation in obesity and glucose homeostasis in response to high-fat feeding
Magdalene K. Montgomery,Nicole L Hallahan,Simon H. J. Brown,Menghan Liu,Todd W. Mitchell,Gregory J. Cooney,Gregory J. Cooney,Nigel Turner,Nigel Turner +8 more
TL;DR: Findings indicate that most mouse strains develop metabolic defects on an HFD, however, there are inherent differences between strains, and thus the genetic background needs to be considered carefully in metabolic studies.
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Signaling through cAMP and cAMP-dependent protein kinase: Diverse strategies for drug design
TL;DR: These structures reveal for the first time the remarkable malleability of the regulatory subunits and the CNB domains and provide a new paradigm for designing isoform-specific activators and inhibitors of PKA.
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Analysis of unsaturated lipids by ozone-induced dissociation.
TL;DR: In this paper, the capabilities and limitations of tandem mass spectrometry to provide this level of structural specificity in the analysis of lipids present in complex biological extracts are reviewed. And the capabilities of ozone-induced dissociation to identify the position(s) of double bonds in unsaturated lipids are discussed.
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A comparison of patient matched meibum and tear lipidomes.
Simon H. J. Brown,Carolina Kunnen,Eva Duchoslav,Naveen K. Dolla,Michael J. Kelso,Eric B. Papas,Percy Lazon de la Jara,Mark D. P. Willcox,Stephen J. Blanksby,Todd W. Mitchell +9 more
TL;DR: In this paper, the molecular lipid composition of patient-matched tear and meibum samples was quantified using chip-based nanoelectrospray ionization tandem mass spectrometry.
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PKA Type IIα Holoenzyme Reveals a Combinatorial Strategy for Isoform Diversity
TL;DR: To understand the molecular basis for isoform diversity, the crystal structure of an RIIα holoenzyme was solved and compared it to the RIαholoenzyme and provided a new paradigm for designing isoform-specific activators or antagonists for PKA.