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  • 1
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    The very energetic, broad-lined Type Ic supernova 2010ah (PTF10bzf) in the context of GRB/SNe (2013)
    Oxford University Press
    Details
    Publication Date: 2013-06-09
    Description: SN 2010ah, a very broad-lined Type Ic supernova (SN) discovered by the Palomar Transient Factory, was interesting because of its relatively high luminosity and the high velocity of the absorption lines, which was comparable to that of gamma-ray burst (GRB)/SNe, suggesting a high explosion kinetic energy. However, no GRB was detected in association with the SN. Here, the properties of SN 2010ah are determined with higher accuracy than previous studies through modelling. New Subaru telescope photometry is presented. A bolometric light curve is constructed taking advantage of the spectral similarity with SN 1998bw. Radiation transport tools are used to reproduce the spectra and the light curve. The results thus obtained regarding ejecta mass, composition and kinetic energy are then used to compute a synthetic light curve. This is in reasonable agreement with the early bolometric light curve of SN 2010ah, but a high abundance of 56 Ni at high velocity is required to reproduce the early rise, while a dense inner core must be used to reproduce the slow decline at late phases. The high-velocity 56 Ni cannot have been located on our line of sight, which may be indirect evidence for an off-axis, aspherical explosion. The main properties of SN 2010ah are: ejected mass M ej 3 M ; kinetic energy E kin 10 52  erg, M( 56 Ni) 0.25 M . The mass located at v 0.1 c is ~0.2 M . Although these values, in particular the E kin , are quite large for a Type Ic SN, they are all smaller (especially M ej ) than those typical of GRB/SNe. This confirms the tendency for these quantities to correlate, and suggests that there are minimum requirements for a GRB/SN, which SN 2010ah may not meet although it comes quite close. Depending on whether a neutron star or a black hole was formed following core collapse, SN 2010ah was the explosion of a CO core of ~5 to 6 M , pointing to a progenitor mass of ~24–28 M .
    Print ISSN: 0035-8711
    Electronic ISSN: 1365-2966
    Topics: Physics
    Published by Oxford University Press
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  • 2
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    Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants (2008)
    Nature Publishing Group (NPG)
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    Publication Date: 2008-05-16
    Description: The potential impact of pandemic influenza makes effective measures to limit the spread and morbidity of virus infection a public health priority. Antiviral drugs are seen as essential requirements for control of initial influenza outbreaks caused by a new virus, and in pre-pandemic plans there is a heavy reliance on drug stockpiles. The principal target for these drugs is a virus surface glycoprotein, neuraminidase, which facilitates the release of nascent virus and thus the spread of infection. Oseltamivir (Tamiflu) and zanamivir (Relenza) are two currently used neuraminidase inhibitors that were developed using knowledge of the enzyme structure. It has been proposed that the closer such inhibitors resemble the natural substrate, the less likely they are to select drug-resistant mutant viruses that retain viability. However, there have been reports of drug-resistant mutant selection in vitro and from infected humans. We report here the enzymatic properties and crystal structures of neuraminidase mutants from H5N1-infected patients that explain the molecular basis of resistance. Our results show that these mutants are resistant to oseltamivir but still strongly inhibited by zanamivir owing to an altered hydrophobic pocket in the active site of the enzyme required for oseltamivir binding. Together with recent reports of the viability and pathogenesis of H5N1 (ref. 7) and H1N1 (ref. 8) viruses with neuraminidases carrying these mutations, our results indicate that it would be prudent for pandemic stockpiles of oseltamivir to be augmented by additional antiviral drugs, including zanamivir.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Collins, Patrick J -- Haire, Lesley F -- Lin, Yi Pu -- Liu, Junfeng -- Russell, Rupert J -- Walker, Philip A -- Skehel, John J -- Martin, Stephen R -- Hay, Alan J -- Gamblin, Steven J -- MC_U117512711/Medical Research Council/United Kingdom -- MC_U117512723/Medical Research Council/United Kingdom -- MC_U117570592/Medical Research Council/United Kingdom -- MC_U117584222/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- England -- Nature. 2008 Jun 26;453(7199):1258-61. doi: 10.1038/nature06956. Epub 2008 May 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC-National Institute for Medical Research, Mill Hill, London NW7 1AA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18480754" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallography, X-Ray ; *Drug Resistance, Viral ; Enzyme Inhibitors/chemistry/metabolism/pharmacology ; Humans ; Influenza A Virus, H1N1 Subtype/drug effects/enzymology/genetics ; Influenza A Virus, H5N1 Subtype/*drug effects/*enzymology/genetics ; Influenza, Human/virology ; Kinetics ; Models, Molecular ; Molecular Conformation ; Mutation/*genetics ; Neuraminidase/antagonists & inhibitors/*chemistry/*genetics/metabolism ; Oseltamivir/chemistry/metabolism/*pharmacology ; Protein Binding ; Zanamivir/pharmacology
    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
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    Receptor binding by a ferret-transmissible H5 avian influenza virus (2013)
    Nature Publishing Group (NPG)
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    Publication Date: 2013-04-26
    Description: Cell-surface-receptor binding by influenza viruses is a key determinant of their transmissibility, both from avian and animal species to humans as well as from human to human. Highly pathogenic avian H5N1 viruses that are a threat to public health have been observed to acquire affinity for human receptors, and transmissible-mutant-selection experiments have identified a virus that is transmissible in ferrets, the generally accepted experimental model for influenza in humans. Here, our quantitative biophysical measurements of the receptor-binding properties of haemagglutinin (HA) from the transmissible mutant indicate a small increase in affinity for human receptor and a marked decrease in affinity for avian receptor. From analysis of virus and HA binding data we have derived an algorithm that predicts virus avidity from the affinity of individual HA-receptor interactions. It reveals that the transmissible-mutant virus has a 200-fold preference for binding human over avian receptors. The crystal structure of the transmissible-mutant HA in complex with receptor analogues shows that it has acquired the ability to bind human receptor in the same folded-back conformation as seen for HA from the 1918, 1957 (ref. 4), 1968 (ref. 5) and 2009 (ref. 6) pandemic viruses. This binding mode is substantially different from that by which non-transmissible wild-type H5 virus HA binds human receptor. The structure of the complex also explains how the change in preference from avian to human receptors arises from the Gln226Leu substitution, which facilitates binding to human receptor but restricts binding to avian receptor. Both features probably contribute to the acquisition of transmissibility by this mutant virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xiong, Xiaoli -- Coombs, Peter J -- Martin, Stephen R -- Liu, Junfeng -- Xiao, Haixia -- McCauley, John W -- Locher, Kathrin -- Walker, Philip A -- Collins, Patrick J -- Kawaoka, Yoshihiro -- Skehel, John J -- Gamblin, Steven J -- BB/E010806/Biotechnology and Biological Sciences Research Council/United Kingdom -- MC_U117512723/Medical Research Council/United Kingdom -- MC_U117584222/Medical Research Council/United Kingdom -- U117512723/Medical Research Council/United Kingdom -- U117570592/Medical Research Council/United Kingdom -- U117584222/Medical Research Council/United Kingdom -- England -- Nature. 2013 May 16;497(7449):392-6. doi: 10.1038/nature12144. Epub 2013 Apr 24.〈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/23615615" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Birds/metabolism/virology ; Chick Embryo ; Crystallography, X-Ray ; Ferrets/*virology ; Hemagglutinin Glycoproteins, Influenza Virus/*chemistry/genetics/*metabolism ; *Host Specificity ; Humans ; Influenza A Virus, H5N1 Subtype/chemistry/*genetics/*metabolism/pathogenicity ; Models, Biological ; Models, Molecular ; Mutation ; Orthomyxoviridae Infections/*transmission/*virology ; Protein Conformation ; Receptors, Virus/*metabolism ; Species Specificity
    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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  • 4
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    HIV-1 restriction factor SAMHD1 is a deoxynucleoside triphosphate triphosphohydrolase (2011)
    Nature Publishing Group (NPG)
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    Publication Date: 2011-11-08
    Description: SAMHD1, an analogue of the murine interferon (IFN)-gamma-induced gene Mg11 (ref. 1), has recently been identified as a human immunodeficiency virus-1 (HIV-1) restriction factor that blocks early-stage virus replication in dendritic and other myeloid cells and is the target of the lentiviral protein Vpx, which can relieve HIV-1 restriction. SAMHD1 is also associated with Aicardi-Goutieres syndrome (AGS), an inflammatory encephalopathy characterized by chronic cerebrospinal fluid lymphocytosis and elevated levels of the antiviral cytokine IFN-alpha. The pathology associated with AGS resembles congenital viral infection, such as transplacentally acquired HIV. Here we show that human SAMHD1 is a potent dGTP-stimulated triphosphohydrolase that converts deoxynucleoside triphosphates to the constituent deoxynucleoside and inorganic triphosphate. The crystal structure of the catalytic core of SAMHD1 reveals that the protein is dimeric and indicates a molecular basis for dGTP stimulation of catalytic activity against dNTPs. We propose that SAMHD1, which is highly expressed in dendritic cells, restricts HIV-1 replication by hydrolysing the majority of cellular dNTPs, thus inhibiting reverse transcription and viral complementary DNA (cDNA) synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldstone, David C -- Ennis-Adeniran, Valerie -- Hedden, Joseph J -- Groom, Harriet C T -- Rice, Gillian I -- Christodoulou, Evangelos -- Walker, Philip A -- Kelly, Geoff -- Haire, Lesley F -- Yap, Melvyn W -- de Carvalho, Luiz Pedro S -- Stoye, Jonathan P -- Crow, Yanick J -- Taylor, Ian A -- Webb, Michelle -- MC_U117512710/Medical Research Council/United Kingdom -- MC_U117533887/Medical Research Council/United Kingdom -- MC_U117565647/Medical Research Council/United Kingdom -- MC_UP_A253_1111/Medical Research Council/United Kingdom -- U117512710/Medical Research Council/United Kingdom -- U117565647/Medical Research Council/United Kingdom -- England -- Nature. 2011 Nov 6;480(7377):379-82. doi: 10.1038/nature10623.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Structure, MRC National Institute for Medical Research, London NW7 1AA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22056990" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Biocatalysis ; Catalytic Domain ; Crystallography, X-Ray ; Dendritic Cells/metabolism/virology ; Deoxyadenine Nucleotides/metabolism ; Deoxycytosine Nucleotides/metabolism ; Deoxyguanine Nucleotides/metabolism ; HIV-1/*physiology ; Humans ; Hydrolysis ; Models, Biological ; Models, Molecular ; Monomeric GTP-Binding Proteins/*chemistry/genetics/*metabolism ; Myeloid Cells/virology ; Nucleoside-Triphosphatase/*chemistry/genetics/*metabolism ; Protein Structure, Tertiary ; Reverse Transcription ; Thymine Nucleotides/metabolism ; Viral Regulatory and Accessory Proteins/metabolism ; Virus Replication
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 5
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    Structural basis of lentiviral subversion of a cellular protein degradation pathway (2013)
    Nature Publishing Group (NPG)
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    Publication Date: 2013-12-18
    Description: Lentiviruses contain accessory genes that have evolved to counteract the effects of host cellular defence proteins that inhibit productive infection. One such restriction factor, SAMHD1, inhibits human immunodeficiency virus (HIV)-1 infection of myeloid-lineage cells as well as resting CD4(+) T cells by reducing the cellular deoxynucleoside 5'-triphosphate (dNTP) concentration to a level at which the viral reverse transcriptase cannot function. In other lentiviruses, including HIV-2 and related simian immunodeficiency viruses (SIVs), SAMHD1 restriction is overcome by the action of viral accessory protein x (Vpx) or the related viral protein r (Vpr) that target and recruit SAMHD1 for proteasomal degradation. The molecular mechanism by which these viral proteins are able to usurp the host cell's ubiquitination machinery to destroy the cell's protection against these viruses has not been defined. Here we present the crystal structure of a ternary complex of Vpx with the human E3 ligase substrate adaptor DCAF1 and the carboxy-terminal region of human SAMHD1. Vpx is made up of a three-helical bundle stabilized by a zinc finger motif, and wraps tightly around the disc-shaped DCAF1 molecule to present a new molecular surface. This adapted surface is then able to recruit SAMHD1 via its C terminus, making it a competent substrate for the E3 ligase to mark for proteasomal degradation. The structure reported here provides a molecular description of how a lentiviral accessory protein is able to subvert the cell's normal protein degradation pathway to inactivate the cellular viral defence system.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3886899/" 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/PMC3886899/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwefel, David -- Groom, Harriet C T -- Boucherit, Virginie C -- Christodoulou, Evangelos -- Walker, Philip A -- Stoye, Jonathan P -- Bishop, Kate N -- Taylor, Ian A -- 084955/Wellcome Trust/United Kingdom -- MC_U117512710/Medical Research Council/United Kingdom -- MC_U117565647/Medical Research Council/United Kingdom -- MC_U117592729/Medical Research Council/United Kingdom -- U117512710/Medical Research Council/United Kingdom -- U11756564/Medical Research Council/United Kingdom -- U117592729/Medical Research Council/United Kingdom -- England -- Nature. 2014 Jan 9;505(7482):234-8. doi: 10.1038/nature12815. Epub 2013 Dec 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Structure, MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK. ; Division of Virology, 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/24336198" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/*metabolism ; Cercocebus atys/virology ; Crystallography, X-Ray ; HIV/*chemistry/*physiology ; Host-Pathogen Interactions ; Humans ; Models, Molecular ; Molecular Sequence Data ; Monomeric GTP-Binding Proteins/chemistry/*metabolism ; Proteasome Endopeptidase Complex/metabolism ; *Proteolysis ; Simian Immunodeficiency Virus/chemistry/physiology ; Ubiquitination ; Viral Regulatory and Accessory Proteins/*chemistry/*metabolism ; vpr Gene Products, Human Immunodeficiency Virus/chemistry/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 6
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    Structure of mammalian AMPK and its regulation by ADP (2011)
    Nature Publishing Group (NPG)
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    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
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  • 7
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    Receptor binding by an H7N9 influenza virus from humans (2013)
    Nature Publishing Group (NPG)
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    Publication Date: 2013-06-22
    Description: Of the 132 people known to have been infected with H7N9 influenza viruses in China, 37 died, and many were severely ill. Infection seems to have involved contact with infected poultry. We have examined the receptor-binding properties of this H7N9 virus and compared them with those of an avian H7N3 virus. We find that the human H7 virus has significantly higher affinity for alpha-2,6-linked sialic acid analogues ('human receptor') than avian H7 while retaining the strong binding to alpha-2,3-linked sialic acid analogues ('avian receptor') characteristic of avian viruses. The human H7 virus does not, therefore, have the preference for human versus avian receptors characteristic of pandemic viruses. X-ray crystallography of the receptor-binding protein, haemagglutinin (HA), in complex with receptor analogues indicates that both human and avian receptors adopt different conformations when bound to human H7 HA than they do when bound to avian H7 HA. Human receptor bound to human H7 HA exits the binding site in a different direction to that seen in complexes formed by HAs from pandemic viruses and from an aerosol-transmissible H5 mutant. The human-receptor-binding properties of human H7 probably arise from the introduction of two bulky hydrophobic residues by the substitutions Gln226Leu and Gly186Val. The former is shared with the 1957 H2 and 1968 H3 pandemic viruses and with the aerosol-transmissible H5 mutant. We conclude that the human H7 virus has acquired some of the receptor-binding characteristics that are typical of pandemic viruses, but its retained preference for avian receptor may restrict its further evolution towards a virus that could transmit efficiently between humans, perhaps by binding to avian-receptor-rich mucins in the human respiratory tract rather than to cellular receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xiong, Xiaoli -- Martin, Stephen R -- Haire, Lesley F -- Wharton, Stephen A -- Daniels, Rodney S -- Bennett, Michael S -- McCauley, John W -- Collins, Patrick J -- Walker, Philip A -- Skehel, John J -- Gamblin, Steven J -- MC_U117584222/Medical Research Council/United Kingdom -- MC_U117585868/Medical Research Council/United Kingdom -- U117512723/PHS HHS/ -- U117570592/PHS HHS/ -- U117584222/PHS HHS/ -- U117585868/PHS HHS/ -- England -- Nature. 2013 Jul 25;499(7459):496-9. doi: 10.1038/nature12372.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW71AA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23787694" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Birds/metabolism/virology ; Crystallography, X-Ray ; Hemagglutinin Glycoproteins, Influenza Virus/chemistry/metabolism ; Humans ; Influenza A Virus, H7N3 Subtype/metabolism ; Influenza A virus/chemistry/isolation & purification/*metabolism ; Influenza, Human/*virology ; Models, Molecular ; Mucins/chemistry/metabolism ; N-Acetylneuraminic Acid/analogs & derivatives/chemistry/*metabolism ; Protein Binding ; Protein Conformation ; Receptors, Virus/chemistry/*metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 8
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    Receptor binding by H10 influenza viruses (2014)
    Nature Publishing Group (NPG)
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    Publication Date: 2014-05-30
    Description: H10N8 follows H7N9 and H5N1 as the latest in a line of avian influenza viruses that cause serious disease in humans and have become a threat to public health. Since December 2013, three human cases of H10N8 infection have been reported, two of whom are known to have died. To gather evidence relating to the epidemic potential of H10 we have determined the structure of the haemagglutinin of a previously isolated avian H10 virus and we present here results relating especially to its receptor-binding properties, as these are likely to be major determinants of virus transmissibility. Our results show, first, that the H10 virus possesses high avidity for human receptors and second, from the crystal structure of the complex formed by avian H10 haemagglutinin with human receptor, it is clear that the conformation of the bound receptor has characteristics of both the 1918 H1N1 pandemic virus and the human H7 viruses isolated from patients in 2013 (ref. 3). We conclude that avian H10N8 virus has sufficient avidity for human receptors to account for its infection of humans but that its preference for avian receptors should make avian-receptor-rich human airway mucins an effective block to widespread infection. In terms of surveillance, particular attention will be paid to the detection of mutations in the receptor-binding site of the H10 haemagglutinin that decrease its avidity for avian receptor, and could enable it to be more readily transmitted between humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vachieri, Sebastien G -- Xiong, Xiaoli -- Collins, Patrick J -- Walker, Philip A -- Martin, Stephen R -- Haire, Lesley F -- Zhang, Ying -- McCauley, John W -- Gamblin, Steven J -- Skehel, John J -- MC_U117512723/Medical Research Council/United Kingdom -- U117570592/Medical Research Council/United Kingdom -- U117584222/Medical Research Council/United Kingdom -- U117585868/Medical Research Council/United Kingdom -- England -- Nature. 2014 Jul 24;511(7510):475-7. doi: 10.1038/nature13443.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK [2]. ; 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/24870229" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Birds/*virology ; Crystallography, X-Ray ; Hemagglutinin Glycoproteins, Influenza Virus/chemistry/metabolism ; Humans ; Influenza A Virus, H1N1 Subtype/chemistry ; Influenza A Virus, H7N9 Subtype/chemistry ; Models, Molecular ; Orthomyxoviridae/*chemistry/*metabolism ; Receptors, Virus/*chemistry/*metabolism ; Zoonoses/transmission/virology
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    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 9
    Electronic Resource
    Electronic Resource
    The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways (2001)
    [s.l.] : Macmillian Magazines Ltd.
    Nature 411 (2001), S. 215-219 
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    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Small G proteins are GTP-dependent molecular switches that regulate numerous cellular functions. They can be classified into homologous subfamilies that are broadly associated with specific biological processes. Cross-talk between small G-protein families has an important role in signalling, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/35075620
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  • 10
    Electronic Resource
    Electronic Resource
    A SYSTEMS OVERVIEW OF TRANSDUCERS (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 189 (1972), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1972.tb13122.x
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