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  • 1
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    hMSH2-MSH6 recognizes mismatches within the D-loop [Biochemistry] (2014)
    National Academy of Sciences
    Details
    Publication Date: 2014-01-22
    Description: High fidelity homologous DNA recombination depends on mismatch repair (MMR), which antagonizes recombination between divergent sequences by rejecting heteroduplex DNA containing excessive nucleotide mismatches. The hMSH2–hMSH6 heterodimer is the first responder in postreplicative MMR and also plays a prominent role in heteroduplex rejection. Whether a similar molecular mechanism underlies its...
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 2
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    Landscape-scale variation in plant community composition of an African savanna from airborne species mapping (2014)
    Wiley
    Details
    Publication Date: 2014-01-01
    Description: Information on landscape-scale patterns in species distributions and community types is vital for ecological science and effective conservation assessment and planning. However, detailed maps of plant community structure at landscape scales seldom exist due to the inability of field-based inventories to map a sufficient number of individuals over large areas. The Carnegie Airborne Observatory (CAO) collected hyperspectral and lidar data over Kruger National Park, South Africa, and these data were used to remotely identify 〉500?000 tree and shrub crowns over a 144-km2 landscape using stacked support vector machines. Maps of community compositional variation were produced by ordination and clustering, and the importance of hillslope-scale topo-edaphic variation in shaping community structure was evaluated with redundancy analysis. This remote species identification approach revealed spatially complex patterns in woody plant communities throughout the landscape that could not be directly observed using field-based methods alone. We estimated that topo-edaphic variables representing catenal sequences explained 21% of species compositional variation, while we also uncovered important community patterns that were unrelated to catenas, indicating a large role for other soil-related factors in shaping the savanna community. Our results demonstrate the ability of airborne species identification techniques to map biodiversity for the evaluation of ecological controls on community composition over large landscapes. # doi:10.1890/13-0307.1
    Print ISSN: 1051-0761
    Electronic ISSN: 1939-5582
    Topics: Biology
    Published by Wiley on behalf of The Ecological Society of America (ESA).
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  • 3
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    Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants (2008)
    Nature Publishing Group (NPG)
    Details
    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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  • 4
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    Role of the polycomb protein EED in the propagation of repressive histone marks (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-09-22
    Description: Polycomb group proteins have an essential role in the epigenetic maintenance of repressive chromatin states. The gene-silencing activity of the Polycomb repressive complex 2 (PRC2) depends on its ability to trimethylate lysine 27 of histone H3 (H3K27) by the catalytic SET domain of the EZH2 subunit, and at least two other subunits of the complex: SUZ12 and EED. Here we show that the carboxy-terminal domain of EED specifically binds to histone tails carrying trimethyl-lysine residues associated with repressive chromatin marks, and that this leads to the allosteric activation of the methyltransferase activity of PRC2. Mutations in EED that prevent it from recognizing repressive trimethyl-lysine marks abolish the activation of PRC2 in vitro and, in Drosophila, reduce global methylation and disrupt development. These findings suggest a model for the propagation of the H3K27me3 mark that accounts for the maintenance of repressive chromatin domains and for the transmission of a histone modification from mother to daughter cells.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3772642/" 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/PMC3772642/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Margueron, Raphael -- Justin, Neil -- Ohno, Katsuhito -- Sharpe, Miriam L -- Son, Jinsook -- Drury, William J 3rd -- Voigt, Philipp -- Martin, Stephen R -- Taylor, William R -- De Marco, Valeria -- Pirrotta, Vincenzo -- Reinberg, Danny -- Gamblin, Steven J -- GM064844/GM/NIGMS NIH HHS/ -- GM37120/GM/NIGMS NIH HHS/ -- MC_U117584222/Medical Research Council/United Kingdom -- R01 GM064844/GM/NIGMS NIH HHS/ -- R01 GM064844-08/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- Medical Research Council/United Kingdom -- England -- Nature. 2009 Oct 8;461(7265):762-7. doi: 10.1038/nature08398. Epub 2009 Sep 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry, New York University Medical School, 522 First Avenue, New York, New York 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19767730" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Animals ; Cell Line ; Chromatin/chemistry/*genetics/metabolism ; Crystallography, X-Ray ; Drosophila Proteins/chemistry/genetics/*metabolism ; Drosophila melanogaster/*genetics/growth & development/*metabolism ; Enzyme Activation ; *Gene Silencing ; Histone-Lysine N-Methyltransferase/chemistry/metabolism ; Histones/*chemistry/*metabolism ; Lysine/analogs & derivatives/metabolism ; Methylation ; Models, Biological ; Models, Molecular ; Nuclear Proteins/metabolism ; Nucleosomes/chemistry/genetics/metabolism ; Polycomb Repressive Complex 2 ; Protein Binding ; Protein Structure, Tertiary ; Repressor Proteins/chemistry/genetics/*metabolism ; Substrate 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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  • 5
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    Receptor binding by a ferret-transmissible H5 avian influenza virus (2013)
    Nature Publishing Group (NPG)
    Details
    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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  • 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
    Published by Nature Publishing Group (NPG)
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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
    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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  • 9
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    Gyrate atrophy of the retina: inborn error of L-ornithin:2-oxoacid aminotransferase (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-04-14
    Description: Cultured fibroblasts from a patient with gyrate atrophy of the retina do not convert L-ornithine, uniformly labeled with carbon-14, to proline. This metabolic block is caused by deficient L-ornithine:2-oxoacid aminotransferase activity in the patient. Her heterozygote father has intermediate activity of this enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Donnell, J J -- Sandman, R P -- Martin, S R -- New York, N.Y. -- Science. 1978 Apr 14;200(4338):200-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/635581" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Female ; Heterozygote ; Humans ; Ornithine/blood ; Ornithine-Oxo-Acid Transaminase/*deficiency ; Pedigree ; Retinal Degeneration/*enzymology/genetics ; Transaminases/*deficiency
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 10
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    Fund the Biological Survey Unit (2018)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2018-02-16
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Geosciences , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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