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  • 1
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    Structure of mammalian AMPK and its regulation by ADP (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-03-15
    Description: The heterotrimeric AMP-activated protein kinase (AMPK) has a key role in regulating cellular energy metabolism; in response to a fall in intracellular ATP levels it activates energy-producing pathways and inhibits energy-consuming processes. AMPK has been implicated in a number of diseases related to energy metabolism including type 2 diabetes, obesity and, most recently, cancer. AMPK is converted from an inactive form to a catalytically competent form by phosphorylation of the activation loop within the kinase domain: AMP binding to the gamma-regulatory domain promotes phosphorylation by the upstream kinase, protects the enzyme against dephosphorylation, as well as causing allosteric activation. Here we show that ADP binding to just one of the two exchangeable AXP (AMP/ADP/ATP) binding sites on the regulatory domain protects the enzyme from dephosphorylation, although it does not lead to allosteric activation. Our studies show that active mammalian AMPK displays significantly tighter binding to ADP than to Mg-ATP, explaining how the enzyme is regulated under physiological conditions where the concentration of Mg-ATP is higher than that of ADP and much higher than that of AMP. We have determined the crystal structure of an active AMPK complex. The structure shows how the activation loop of the kinase domain is stabilized by the regulatory domain and how the kinase linker region interacts with the regulatory nucleotide-binding site that mediates protection against dephosphorylation. From our biochemical and structural data we develop a model for how the energy status of a cell regulates AMPK activity.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3078618/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3078618/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xiao, Bing -- Sanders, Matthew J -- Underwood, Elizabeth -- Heath, Richard -- Mayer, Faith V -- Carmena, David -- Jing, Chun -- Walker, Philip A -- Eccleston, John F -- Haire, Lesley F -- Saiu, Peter -- Howell, Steven A -- Aasland, Rein -- Martin, Stephen R -- Carling, David -- Gamblin, Steven J -- MC_U117584222/Medical Research Council/United Kingdom -- MC_U120027537/Medical Research Council/United Kingdom -- U.1175.03.004.00008(60522)/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- England -- Nature. 2011 Apr 14;472(7342):230-3. doi: 10.1038/nature09932. Epub 2011 Mar 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21399626" target="_blank"〉PubMed〈/a〉
    Keywords: AMP-Activated Protein Kinases/*chemistry/genetics/*metabolism ; Adenosine Diphosphate/*metabolism/*pharmacology ; Adenosine Monophosphate/metabolism/pharmacology ; Adenosine Triphosphate/metabolism/pharmacology ; Allosteric Regulation/drug effects/genetics ; Animals ; Binding Sites ; Crystallography, X-Ray ; Enzyme Activation/drug effects/genetics ; Kinetics ; Magnesium/metabolism ; Mammals ; Models, Molecular ; Phosphorylation/drug effects/genetics ; Protein Binding ; Protein Structure, Tertiary/drug effects/genetics ; Thermodynamics
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    Notum deacylates Wnt proteins to suppress signalling activity (2015)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2015-03-04
    Description: Signalling by Wnt proteins is finely balanced to ensure normal development and tissue homeostasis while avoiding diseases such as cancer. This is achieved in part by Notum, a highly conserved secreted feedback antagonist. Notum has been thought to act as a phospholipase, shedding glypicans and associated Wnt proteins from the cell surface. However, this view fails to explain specificity, as glypicans bind many extracellular ligands. Here we provide genetic evidence in Drosophila that Notum requires glypicans to suppress Wnt signalling, but does not cleave their glycophosphatidylinositol anchor. Structural analyses reveal glycosaminoglycan binding sites on Notum, which probably help Notum to co-localize with Wnt proteins. They also identify, at the active site of human and Drosophila Notum, a large hydrophobic pocket that accommodates palmitoleate. Kinetic and mass spectrometric analyses of human proteins show that Notum is a carboxylesterase that removes an essential palmitoleate moiety from Wnt proteins and thus constitutes the first known extracellular protein deacylase.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4376489/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4376489/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kakugawa, Satoshi -- Langton, Paul F -- Zebisch, Matthias -- Howell, Steven A -- Chang, Tao-Hsin -- Liu, Yan -- Feizi, Ten -- Bineva, Ganka -- O'Reilly, Nicola -- Snijders, Ambrosius P -- Jones, E Yvonne -- Vincent, Jean-Paul -- 090532/Wellcome Trust/United Kingdom -- 090532/Z/09/Z/Wellcome Trust/United Kingdom -- 294523/European Research Council/International -- A10976/Cancer Research UK/United Kingdom -- C375/A10976/Cancer Research UK/United Kingdom -- G0900084/Medical Research Council/United Kingdom -- MC_U117584268/Medical Research Council/United Kingdom -- U117584268/Medical Research Council/United Kingdom -- WT093378MA/Wellcome Trust/United Kingdom -- WT099197MA/Wellcome Trust/United Kingdom -- England -- Nature. 2015 Mar 12;519(7542):187-92. doi: 10.1038/nature14259. Epub 2015 Feb 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC's National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK. ; Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK. ; Glycosciences Laboratory, Imperial College London, Department of Medicine, Du Cane Road, London W12 0NN, UK. ; Cancer Research UK, London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3LY, UK. ; Cancer Research UK, Clare Hall Laboratories, Blanche Lane, South Mimms, Potters Bar, Hertfordshire EN6 3LD, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25731175" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Animals ; Binding Sites ; Carboxylesterase/chemistry/*metabolism ; Drosophila Proteins/chemistry/*metabolism ; Esterases/chemistry/genetics/*metabolism ; Fatty Acids, Monounsaturated/metabolism ; Glycosylphosphatidylinositols/metabolism ; Glypicans/metabolism ; Humans ; Kinetics ; Ligands ; Mass Spectrometry ; Models, Molecular ; Protein Binding ; Wnt Proteins/*chemistry/*metabolism ; *Wnt Signaling Pathway
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
    Electronic Resource
    Electronic Resource
    Bovine annexin V isoforms: A molecular weight difference of 4 kD by SDS-PAGE, 9 D by mass spectrometry (1992)
    Springer
    The protein journal 11 (1992), S. 373-374 
    Details
    ISSN: 1573-4943
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01673730
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  • 4
    Electronic Resource
    Electronic Resource
    Identification of chiral isomers by fast atom bombardment/mass spectrometry: Dialkyl tartrates (1988)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 16 (1988), S. 357-360 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A chiral effect has been observed for formation of protonated dimers of dialkyl tartrates under fast atom bombardment, analogous to the chemical ionization behaviour reported previously. Homochiral dimers show greater stability than the heterochiral dimers, as is evidenced by their enhanced formation and lesser tendency to undergo metastable breakdown. The difference in stability is related to the size of the alkyl group.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200160170
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  • 5
    Electronic Resource
    Electronic Resource
    Use of gas chromatography/mass spectrometry selected-ion recording for sterol content pattern recognition in fungal classification (1989)
    New York, NY : Wiley-Blackwell
    Rapid Communications in Mass Spectrometry 3 (1989), S. 230-232 
    Details
    ISSN: 0951-4198
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Physics
    Notes: Chemotaxonomic studies are frequently limited by the volume of data obtained and the difficulty of reducing this to statistically interpretable results. This paper describes the use of a straightforward procedure for relating the pattern of occurrence of sterols in fungi, analysed by mass spectrometry, to their classification.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/rcm.1290030707
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  • 6
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    Continuous 'stunted outbursts detected from the cataclysmic variable KIC 9202990 using Kepler data (2015)
    Oxford University Press
    Details
    Publication Date: 2015-11-27
    Description: Based on early Kepler data, Østensen et al. found that KIC 9202990 showed a 4-h and a two-week photometric period. They suggested the 4-h period was a signature of an orbital period; the longer period was possibly due to precession of an accretion disc and KIC 9202990 was a cataclysmic variable with an accretion disc which is always in a bright state (a nova-like system). Using the full Kepler data set on KIC 9202990 which covers 1421 d (Quarter 2–17), and includes 1-min cadence data from the whole of Quarters 5 and 16, we find that the 4-h period is stable and therefore a signature of the binary orbital period. In contrast, the 10–12 d period is not stable and shows an amplitude between 20 and 50 per cent. This longer period modulation is similar to those nova-like systems which show ‘stunted’ outbursts. We discuss the problems that a precessing disc model has in explaining the observed characteristics and indicate why we favour a stunted outburst model. Although such stunted events are considered to be related to the standard disc instability mechanism, their origin is not well understood. KIC 9202990 shows the lowest amplitude and shortest period of continuous stunted outburst systems, making it an ideal target to better understand stunted outbursts and accretion instabilities in general.
    Print ISSN: 0035-8711
    Electronic ISSN: 1365-2966
    Topics: Physics
    Published by Oxford University Press
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